MouseMine: Keyword Search

Publication

First Author:	Kume T
Year:	2000
Journal:	Development
Title:	Murine forkhead/winged helix genes Foxc1 (Mf1) and Foxc2 (Mfh1) are required for the early organogenesis of the kidney and urinary tract.
Volume:	127
Issue:	7
Pages:	1387-95

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Publication

10332027 | J:55377

First Author:	Venables JP
Year:	1999
Journal:	Hum Mol Genet
Title:	T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis.
Volume:	8
Issue:	6
Pages:	959-69

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Publication

21909098 | J:175965

First Author:	Tammela T
Year:	2011
Journal:	Nat Cell Biol
Title:	VEGFR-3 controls tip to stalk conversion at vessel fusion sites by reinforcing Notch signalling.
Volume:	13
Issue:	10
Pages:	1202-13

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Publication

21907141 | J:176654

First Author:	McCormick JA
Year:	2011
Journal:	Cell Metab
Title:	A SPAK isoform switch modulates renal salt transport and blood pressure.
Volume:	14
Issue:	3
Pages:	352-64

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Publication

7607678 | J:24458

First Author:	Bar I
Year:	1995
Journal:	Genomics
Title:	A YAC contig containing the reeler locus with preliminary characterization of candidate gene fragments.
Volume:	26
Issue:	3
Pages:	543-9

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Publication

26079578 | J:225741

First Author:	Kanady JD
Year:	2015
Journal:	Dev Biol
Title:	Combining Foxc2 and Connexin37 deletions in mice leads to severe defects in lymphatic vascular growth and remodeling.
Volume:	405
Issue:	1
Pages:	33-46

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Publication

27214551 | J:237068

First Author:	Fatima A
Year:	2016
Journal:	J Clin Invest
Title:	Foxc1 and Foxc2 deletion causes abnormal lymphangiogenesis and correlates with ERK hyperactivation.
Volume:	126
Issue:	7
Pages:	2437-51

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Publication

22736606 | J:213975

First Author:	Tian H
Year:	2012
Journal:	Invest Ophthalmol Vis Sci
Title:	Ocular anterior segment dysgenesis upon ablation of p120 catenin in neural crest cells.
Volume:	53
Issue:	9
Pages:	5139-53

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Publication

32182215 | J:309377

First Author:	Betterman KL
Year:	2020
Journal:	J Clin Invest
Title:	Atypical cadherin FAT4 orchestrates lymphatic endothelial cell polarity in response to flow.
Volume:	130
Issue:	6
Pages:	3315-3328

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Publication

28242756 | J:241874

First Author:	Barilari M
Year:	2017
Journal:	EMBO J
Title:	ZRF1 is a novel S6 kinase substrate that drives the senescence programme.
Volume:	36
Issue:	6
Pages:	736-750

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Publication

15465483 | J:93150

First Author:	Dagenais SL
Year:	2004
Journal:	Gene Expr Patterns
Title:	Foxc2 is expressed in developing lymphatic vessels and other tissues associated with lymphedema-distichiasis syndrome.
Volume:	4
Issue:	6
Pages:	611-9

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Publication

38933921 | J:350084

First Author:	Zhang L
Year:	2024
Journal:	Front Genet
Title:	Integrative transcriptomic profiling of ncRNAs and mRNAs in developing mouse lens.
Volume:	15

Pages:	1405715

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Publication

33953184 | J:319854

First Author:	Youlten SE
Year:	2021
Journal:	Nat Commun
Title:	Osteocyte transcriptome mapping identifies a molecular landscape controlling skeletal homeostasis and susceptibility to skeletal disease.
Volume:	12
Issue:	1
Pages:	2444

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Protein

Q8C8B5

Organism:	Mus musculus/domesticus
Length:	240
Fragment?:	false

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Protein

A0A1Y7VJ41

Organism:	Mus musculus/domesticus
Length:	132
Fragment?:	true

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Publication

23545411 | -

First Author:	Scheffner M
Year:	2014
Journal:	Biochim Biophys Acta
Title:	Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects.
Volume:	1843
Issue:	1
Pages:	61-74

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Protein Domain

IPR028690 | SYT16

Type:	Family
Description:	Synaptotagmin-16 (SYT16) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains. SYT16 is Ca(2+)-independent and may be involved in membrane trafficking in specific tissues outside the brain [].

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Protein Domain

IPR041510 | DUF5523

Type:	Domain
Description:	This entry represents a domain of unknown function found in Eukaryotes. Many (but not all) proteins matched by this entry, such as the human protein Coiled-coil and C2 domain-containing protein 2A (), also contain and domains at the C-terminal region.

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Protein Domain

IPR037767 | C2A_Mug190-like

Type:

Domain

Description:

Meiotically up-regulated gene 190 protein (Mug190) from Schizosaccharomyces pombe derives its name from a study to identify genes essential for meiosis []. It is thought to correspond to tricalbin 2 in Saccharomyces cerevisiae. Tricalbins are C2 domain proteins involved in ER-plasma membrane tethering [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry represents the first C2 repeat of Mug190, C2A, and has a type-II topology [].

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Protein Domain

IPR032348 | HECW_N

Type:	Domain
Description:	This entry represents a domain found in E3 ubiquitin-protein ligases HECW1 and HECW2 that lies upstream of the C2 domain. Its function is not clearly understood, but it might be to determine the substrate spectrum of the ligase [].

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Protein Domain

IPR042455 | DOCK_N_sub1

Type:	Homologous_superfamily
Description:	This superfamily represents the subdomain 1 found in the N-terminal domain of the protein dedicator of cytokinesis DOCK. Its function is unknown. The N-terminal domain is found between the variant SH3 domain and the C2 domain [].

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Publication

1445255 | -

First Author:	Ahmed S
Year:	1992
Journal:	Biochem J
Title:	The Caenorhabditis elegans unc-13 gene product is a phospholipid-dependent high-affinity phorbol ester receptor.
Volume:	287 ( Pt 3)

Pages:	995-9

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Publication

2062851 | -

First Author:	Maruyama IN
Year:	1991
Journal:	Proc Natl Acad Sci U S A
Title:	A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans.
Volume:	88
Issue:	13
Pages:	5729-33

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Publication

10233166 | -

First Author:	Song Y
Year:	1999
Journal:	Mol Biol Cell
Title:	Human munc13 is a diacylglycerol receptor that induces apoptosis and may contribute to renal cell injury in hyperglycemia.
Volume:	10
Issue:	5
Pages:	1609-19

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Publication

16177003 | J:150394

First Author:	Jouret F
Year:	2005
Journal:	J Am Soc Nephrol
Title:	Ubiquitous and kidney-specific subunits of vacuolar H+-ATPase are differentially expressed during nephrogenesis.
Volume:	16
Issue:	11
Pages:	3235-46

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Protein Domain

IPR043566 | Rabphilin/DOC2/Noc2

Type:

Family

Description:

This entry includes Rabphilin and Doc2. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: Rabphilin contains an N-terminal Rab-binding domain (RBD), whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID) []. This entry also includes Noc2 (also known as Rabphilin-3A-like protein), which is a potential effector of Ras-associated binding proteins Rab3A and Rab27A. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains [].

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Protein Domain

IPR012968 | FerIin_dom

Type:

Domain

Description:

The ferlin gene family are characterised by multiple tandem C2 domains and a C-terminal transmembrane domain. They are found in a wide range of species and their function remains unknown, however, mutations in its two most well-characterised members, dysferlin and otoferlin, have been implicated in human disease [].This domain is present in proteins of the Ferlin family, which includes Otoferlin, Myoferlin and Dysferlin. It is often located between two C2 domains [].

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Publication

28341745 | J:242765

First Author:	Murakami A
Year:	2017
Journal:	J Biol Chem
Title:	Phospholipase C-related, but catalytically inactive protein (PRIP) up-regulates osteoclast differentiation via calcium-calcineurin-NFATc1 signaling.
Volume:	292
Issue:	19
Pages:	7994-8006

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Publication

17301177 | J:118363

First Author:	Mizokami A
Year:	2007
Journal:	J Neurosci
Title:	Phospholipase C-related inactive protein is involved in trafficking of gamma2 subunit-containing GABA(A) receptors to the cell surface.
Volume:	27
Issue:	7
Pages:	1692-701

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Publication

24945349 | J:218954

First Author:	Okumura T
Year:	2014
Journal:	PLoS One
Title:	Phospholipase C-related catalytically inactive protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase.
Volume:	9
Issue:	6
Pages:	e100559

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Publication

17254016 | J:299556

First Author:	Kanematsu T
Year:	2007
Journal:	J Neurochem
Title:	Phospholipase C-related inactive protein is implicated in the constitutive internalization of GABAA receptors mediated by clathrin and AP2 adaptor complex.
Volume:	101
Issue:	4
Pages:	898-905

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Publication

26706316 | J:231034

First Author:	Oue K
Year:	2016
Journal:	J Biol Chem
Title:	Phospholipase C-related Catalytically Inactive Protein Is a New Modulator of Thermogenesis Promoted by β-Adrenergic Receptors in Brown Adipocytes.
Volume:	291
Issue:	8
Pages:	4185-96

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Publication

21757756 | J:176616

First Author:	Tsutsumi K
Year:	2011
Journal:	J Biol Chem
Title:	Involvement of PRIP, phospholipase C-related, but catalytically inactive protein, in bone formation.
Volume:	286
Issue:	35
Pages:	31032-42

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Publication

19553601 | J:153159

First Author:	Matsuda M
Year:	2009
Journal:	Biol Reprod
Title:	Involvement of phospholipase C-related inactive protein in the mouse reproductive system through the regulation of gonadotropin levels.
Volume:	81
Issue:	4
Pages:	681-9

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Publication

19996098 | J:159766

First Author:	Fujii M
Year:	2010
Journal:	J Biol Chem
Title:	Phospholipase C-related but catalytically inactive protein is required for insulin-induced cell surface expression of gamma-aminobutyric acid type A receptors.
Volume:	285
Issue:	7
Pages:	4837-46

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Publication

31589911 | J:294290

First Author:	Yamawaki Y
Year:	2019
Journal:	Neurochem Int
Title:	Phospholipase C-related catalytically inactive protein regulates lipopolysaccharide-induced hypothalamic inflammation-mediated anorexia in mice.
Volume:	131

Pages:	104563

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Publication

16754670 | J:116460

First Author:	Kanematsu T
Year:	2006
Journal:	J Biol Chem
Title:	Modulation of GABA(A) receptor phosphorylation and membrane trafficking by phospholipase C-related inactive protein/protein phosphatase 1 and 2A signaling complex underlying brain-derived neurotrophic factor-dependent regulation of GABAergic inhibition.
Volume:	281
Issue:	31
Pages:	22180-9

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Publication

28360101 | J:242764

First Author:	Matsuda M
Year:	2017
Journal:	J Biol Chem
Title:	Phospholipase C-related but catalytically inactive proteins regulate ovarian follicle development.
Volume:	292
Issue:	20
Pages:	8369-8380

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Publication

34859819 | J:327722

First Author:	Gao J
Year:	2022
Journal:	J Cell Sci
Title:	Phospholipase C-related but catalytically inactive protein acts as a positive regulator of insulin signalling in adipocytes.
Volume:	135
Issue:	1

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Publication

20412381 | J:161821

First Author:	Mizokami A
Year:	2010
Journal:	J Neurochem
Title:	GABA(A) receptor subunit alteration-dependent diazepam insensitivity in the cerebellum of phospholipase C-related inactive protein knockout mice.
Volume:	114
Issue:	1
Pages:	302-10

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Allele

Pax3<tm1Mrc> | MGI:3487369

Name:	paired box 3; targeted mutation 1, Mario R Capecchi
Allele Type:	Targeted
Attribute String:	Inserted expressed sequence, Reporter

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Strain

MGI:4819369 | C57BL/6J-Unc13d<Jinx>/Mmucd

Attribute String:

mutant strain, coisogenic, chemically induced mutation

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Publication

25239803 | J:218680

First Author:	Yang F
Year:	2014
Journal:	Am J Physiol Heart Circ Physiol
Title:	Granule cargo release from bone marrow-derived cells sustains cardiac hypertrophy.
Volume:	307
Issue:	10
Pages:	H1529-38

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Publication

22589474 | J:189036

First Author:	Peters CG
Year:	2012
Journal:	Blood
Title:	Granule exocytosis is required for platelet spreading: differential sorting of α-granules expressing VAMP-7.
Volume:	120
Issue:	1
Pages:	199-206

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Publication

25158625 | J:230479

First Author:	Jonnalagadda D
Year:	2014
Journal:	Biochim Biophys Acta
Title:	Granule-mediated release of sphingosine-1-phosphate by activated platelets.
Volume:	1841
Issue:	11
Pages:	1581-9

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Publication

23590328 | J:341931

First Author:	Dudenhöffer-Pfeifer M
Year:	2013
Journal:	Traffic
Title:	Different Munc13 isoforms function as priming factors in lytic granule release from murine cytotoxic T lymphocytes.
Volume:	14
Issue:	7
Pages:	798-809

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Publication

24488096 | J:229350

First Author:	Bird CH
Year:	2014
Journal:	Cell Death Differ
Title:	The granzyme B-Serpinb9 axis controls the fate of lymphocytes after lysosomal stress.
Volume:	21
Issue:	6
Pages:	876-87

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Publication

20939018 | J:350164

First Author:	Kariya Y
Year:	2011
Journal:	J Bone Miner Res
Title:	Rab27a and Rab27b are involved in stimulation-dependent RANKL release from secretory lysosomes in osteoblastic cells.
Volume:	26
Issue:	4
Pages:	689-703

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Publication

20435885 | J:163507

First Author:	Ren Q
Year:	2010
Journal:	Blood
Title:	Munc13-4 is a limiting factor in the pathway required for platelet granule release and hemostasis.
Volume:	116
Issue:	6
Pages:	869-77

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Publication

28553937 | J:246819

First Author:	Hoeck JD
Year:	2017
Journal:	Nat Cell Biol
Title:	Stem cell plasticity enables hair regeneration following Lgr5⁺ cell loss.
Volume:	19
Issue:	6
Pages:	666-676

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Publication

39480809 | J:360663

First Author:	Walther N
Year:	2024
Journal:	Cell Rep
Title:	Automated live-cell single-molecule tracking in enteroid monolayers reveals transcription factor dynamics probing lineage-determining function.
Volume:	43
Issue:	11
Pages:	114914

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Publication

32327656 | J:292817

First Author:	Cao W
Year:	2020
Journal:	Nat Commun
Title:	LGR5 marks targetable tumor-initiating cells in mouse liver cancer.
Volume:	11
Issue:	1
Pages:	1961

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Strain

MGI:6111720 | B6;FVB-Col1a1<tm1.1(tetO-mStrawberry/Atg4b*C74A)Kmln>/J

Attribute String:

mutant stock, targeted mutation

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Genotype

Symbol:	Unc13d/Unc13d
Background:	C57BL/6J-Unc13d/Mmucd
Zygosity:	hm
Has Mutant Allele:	true

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Genotype

Symbol:	Ighm/Ighm Igkc/Igkc Igl/Igl
Background:	involves: 129P2/OlaHsd * 129/Sv
Zygosity:	cx
Has Mutant Allele:	true

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Genotype

Symbol:	Lgr5/Lgr5<+>
Background:	involves: C57BL/6N
Zygosity:	ht
Has Mutant Allele:	true

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Protein Domain

IPR037733 | Ext_Synaptotagmin_C2A

Type:

Domain

Description:

The extended-synaptotagmins derive their name from their partial domain structure similarity to the synaptotagmins, characterised by an N-terminal membrane anchor and cytosolically exposed C2 domains. Additionally they contain an SMP (synaptotagmin-like mitochondrial-lipid-binding protein) domain and multiple C2 domains (five in E-Syt1 and three in E-Syt2 and E-Syt3). However, the function of extended-synaptotagmins is different to that of synaptotagmins, which are involved in secretory vesicle tethering to the plasma membrane and exocytosis. The extended-synaptotagmins are located to the endoplasmic reticulum (ER), and tether this organelle to the plasma membrane via their C2 domains. They transport glycerolipids between the two bilayers via their lipid-harboring SMP domains. Ca2+ regulates their membrane tethering and lipid transport function [, , ].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry matches the first C2 repeat in extendend synaptotagmins (the first and the third in E-Syt1), with a type-I topology [].

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Protein Domain

IPR037749 | Ext_Synaptotagmin_C2B

Type:

Domain

Description:

The extended-synaptotagmins derive their name from their partial domain structure similarity to the synaptotagmins, characterised by an N-terminal membrane anchor and cytosolically exposed C2 domains. Additionally they contain an SMP (synaptotagmin-like mitochondrial-lipid-binding protein) domain and multiple C2 domains (five in E-Syt1 and three in E-Syt2 and E-Syt3). However, the function of extended-synaptotagmins is different to that of synaptotagmins, which are involved in secretory vesicle tethering to the plasma membrane and exocytosis. The extended-synaptotagmins are located to the endoplasmic reticulum (ER), and tether this organelle to the plasma membrane via their C2 domains. They transport glycerolipids between the two bilayers via their lipid-harboring SMP domains. Ca2+ regulates their membrane tethering and lipid transport function [, , ].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry represents the second C2 domain in extendend synaptotagmins (and the second and fourth domains in extended E-Syt1), which have a type-I topology [].

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Protein Domain

IPR037756 | C2D_Tricalbin

Type:

Domain

Description:

Tricalbins (Tcb1/2/3) are yeast orthologues of the extended synaptotagmins. Tricalbins contain a transmembrane domain in their N-termini and lipid-binding C2 domains in their long cytoplasmic carboxyl-termini. As extended synaptotagmins, tricalbins also possess a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that is found in proteins localized to ER-organelle contact sites []. The ER-plasma membrane tethering function of tricalbins mediates the formation of ER-PM contacts sites []which are thought to mediate transport glycerolipids between the two bilayers [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry contains the fourth C2 repeat of tricalbins, C2D, and has a type-II topology []. The C2 domains of tricalbins 1 and 3 are calcium-dependent lipid-binding units comparable to mammalian synaptotagmin C2 domains, while tricalbin 2 does not seem to bind lipids in response to calcium signaling [].

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Protein Domain

IPR037761 | C2A_Tricalbin

Type:

Domain

Description:

Tricalbins (Tcb1/2/3) are yeast orthologues of the extended synaptotagmins. Tricalbins contain a transmembrane domain in their N-termini and lipid-binding C2 domains in their long cytoplasmic carboxyl-termini. As extended synaptotagmins, tricalbins also possess a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that is found in proteins localized to ER-organelle contact sites []. The ER-plasma membrane tethering function of tricalbins mediates the formation of ER-PM contacts sites []which are thought to mediate transport glycerolipids between the two bilayers [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry contains the first C2 repeat of tricalbins, C2A, and has a type-II topology []. The C2 domains of tricalbins 1 and 3 are calcium-dependent lipid-binding units comparable to mammalian synaptotagmin C2 domains, while tricalbin 2 does not seem to bind lipids in response to calcium signaling [].

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Protein Domain

IPR037762 | C2C_Tricalbin

Type:

Domain

Description:

Tricalbins (Tcb1/2/3) are yeast orthologues of the extended synaptotagmins. Tricalbins contain a transmembrane domain in their N-termini and lipid-binding C2 domains in their long cytoplasmic carboxyl-termini. As extended synaptotagmins, tricalbins also possess a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that is found in proteins localized to ER-organelle contact sites []. The ER-plasma membrane tethering function of tricalbins mediates the formation of ER-PM contacts sites []which are thought to mediate transport glycerolipids between the two bilayers [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry contains the third C2 repeat of tricalbins, C2C, and has a type-II topology []. The C2 domains of tricalbins 1 and 3 are calcium-dependent lipid-binding units comparable to mammalian synaptotagmin C2 domains, while tricalbin 2 does not seem to bind lipids in response to calcium signaling [].

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Protein Domain

IPR037765 | C2B_Tricalbin

Type:

Domain

Description:

Tricalbins (Tcb1/2/3) are yeast orthologues of the extended synaptotagmins. Tricalbins contain a transmembrane domain in their N-termini and lipid-binding C2 domains in their long cytoplasmic carboxyl-termini. As extended synaptotagmins, tricalbins also possess a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that is found in proteins localized to ER-organelle contact sites []. The ER-plasma membrane tethering function of tricalbins mediates the formation of ER-PM contacts sites []which are thought to mediate transport glycerolipids between the two bilayers [].C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry contains the second C2 repeat of tricalbins, C2B, and has a type-II topology []. The C2 domains of tricalbins 1 and 3 are calcium-dependent lipid-binding units comparable to mammalian synaptotagmin C2 domains, while tricalbin 2 does not seem to bind lipids in response to calcium signaling [].

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Publication

23237950 | -

First Author:	Manford AG
Year:	2012
Journal:	Dev Cell
Title:	ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology.
Volume:	23
Issue:	6
Pages:	1129-40

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Publication

37797615 | J:341577

First Author:	Durfee C
Year:	2023
Journal:	Cell Rep Med
Title:	Human APOBEC3B promotes tumor development in vivo including signature mutations and metastases.
Volume:	4
Issue:	10
Pages:	101211

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Publication

24743474 | J:215194

First Author:	Dow LE
Year:	2014
Journal:	PLoS One
Title:	Conditional reverse tet-transactivator mouse strains for the efficient induction of TRE-regulated transgenes in mice.
Volume:	9
Issue:	4
Pages:	e95236

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Publication

11034339 | J:64314

First Author:	Linares JL
Year:	2000
Journal:	FEBS Lett
Title:	C2PA, a new protein expressed during mouse spermatogenesis.
Volume:	480
Issue:	2-3
Pages:	249-54

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Publication

10871871 | J:63109

First Author:	Yung Yu C
Year:	2000
Journal:	Immunol Today
Title:	The human and mouse MHC class III region: a parade of 21 genes at the centromeric segment.
Volume:	21
Issue:	7
Pages:	320-8

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Publication

8824158 | J:36503

First Author:	Kuroda N
Year:	1996
Journal:	Immunogenetics
Title:	Molecular cloning and linkage analysis of the Japanese medaka fish complement Bf/C2 gene.
Volume:	44
Issue:	6
Pages:	459-67

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Protein Coding Gene

MGI:1916622 | Mocs3

Type:	protein_coding_gene
Organism:	mouse, laboratory

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Protein Domain

IPR029023 | Tensin_phosphatase

Type:

Domain

Description:

Tensins constitute an eukaryotic family of lipid phosphatases that are definedby the presence of two adjacent domains: a lipid phosphatase domain and aC2-like domain. The tensin-type C2 lacks the canonical Ca(2+) ligands found inclassical C2 domains, and in this respect it is similar tothe C2 domains of PKC-type [, ]. The tensin-type C2 domain can bindphospholipid membranes in a Ca(2+) independent manner []. In the tumorsuppressor protein PTEN, the best characterized member of the family, thelipid phosphatase domain was shown to specifically dephosphorylate the D3position of the inositol ring of the lipid second messenger,phosphatydilinositol-3-4-5-triphosphate (PIP3). The lipid phosphatase domaincontains the signature motif HCXXGXXR present in the active sites of proteintyrosine phosphatases (PTPs) and dual specificity phosphatases (DSPs).Furthermore, two invariant lysines are found only in the tensin-typephosphatase motif (HCKXGKXR) and are suspected to interact with the phosphategroup at position D1 and D5 of the inositol ring [, ].The crystal structure of the PTEN tumor suppressor has been solved []. The lipid phosphatase domain has a structure similar to thedual specificity phosphatase. However, PTEN has a largeractive site pocket that could be important to accomodate PI(3,4,5)P3. Thetensin-type C2 domain has a structure similar to the classical C2 domain thatmediates the Ca2+ dependent membrane recruitment of several signalingproteins. However the tensin-type C2 domain lacks two of the three conservedloops that bind Ca2+.Proteins known to contain a phosphatase and a C2 tensin-type domain are listed below:Tensin, a focal-adhesion molecule that binds to actin filaments. It may beinvolved in cell migration, cartilage development and in linking signaltransduction pathways to the cytoskeleton.Phosphatase and tensin homologue deleted on chromosome 10 protein (PTEN).It antagonizes PI 3-kinase signalling by dephosphorylating the 3-positionof the inositol ring of PI(3,4,5)P3 and thus inactivates downstreamsignalling. It plays major roles both during development and in the adultto control cell size, growth, and survival.Auxilin. It binds clathrin heavy chain and promotes its assembly intoregular cages.Cyclin G-associated kinase or auxilin-2. It is a potential regulator ofclathrin-mediated membrane trafficking.PTEN homologues in fungi have the tensin phosphatase domain, but they lack the C2 domain. .This entry represents the phosphatase domain.

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Protein Coding Gene

MGI:1921765 | Cdkal1

Type:	protein_coding_gene
Organism:	mouse, laboratory

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Publication

26175110 | -

First Author:	Perestenko P
Year:	2015
Journal:	FEBS J
Title:	The second C2-domain of copine-2, copine-6 and copine-7 is responsible for their calcium-dependent membrane association.
Volume:	282
Issue:	19
Pages:	3722-36

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Protein Domain

IPR043541 | SYT14/14L/16

Type:

Family

Description:

This entry includes Synaptotagmin-14/14L/16 proteins. They belong to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). The C2 domain is a Ca2-dependent membrane-targeting module. Most of the synaptotagmins have a unique N-terminal domain (transmembrane region) that is involved in membrane anchoring or specific ligand binding [].The 3D structure of the C2 domain of synaptotagmin has been reported []. The domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif, designated a C2 key []. Calcium binds in a cup-shaped depression formed by the N- and C-terminal loops of the C2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.In mammals Synaptotagmin-14 (SYT14) is expressed in brain (especially in the cerebellum) []. Mutations in SYT14 gene cause spinocerebellar ataxia, autosomal recessive, 11 (SCAR11), which is a clinically and genetically heterogeneous group of cerebellar disorders [].This entry also includes synaptotagmin-14-like protein (SYT14L, also known as sytdep) from human, which is highly expressed in mature peripheral blood neutrophils [].SYT16 is Ca2-independent and may be involved in membrane trafficking in specific tissues outside the brain [].

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Protein Domain

IPR037768 | C2B_Copine

Type:

Domain

Description:

Copines are a widely distributed class of Ca2+-dependent lipid-binding proteins. Most have a characteristic domain structure: two C2 domains in the N-terminal region and a von Willebrand A (VWA) domain in the C-terminal region. They are potentially involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth [, ]. In plants, they are known as BONZAI proteins []. The copine family in plants may have effects in promoting growth and development in addition to repressing cell death [, ]. Caenorhabditis elegans copine, also known as Nra1, is Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and levamisole []. C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements: type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This entry represents the second C2 repeat of copines, C2B, and has a type-I topology. The C2B domains of copine-2, copine-6 and copine-7 have been shown to be responsible for the protein calcium-dependent membrane association [].

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Protein Domain

IPR001565 | Synaptotagmin

Type:

Domain

Description:

Synaptotagmins are synaptic vesicle membrane proteins found in abundance in nerve cells and some endocrine cells [, ]. The amino acid sequence of synaptotagmin comprises a single transmembrane region with a short vesicular N-terminal region, and a cytoplasmic C-terminal region containing 2 internal repeats similar to the C2 regulatory domain of protein kinase C. The protein is believed to be important in the docking and fusion of synaptic vesicles with the plasma membrane, i.e. with neurotransmitter release [, ].The 2 synaptotagmin C2 domains have been shown to have different functions: C2A binds phospholipid in a calcium-dependent manner, while C2B binds inositol polyphosphate and phospholipid irrespective of the presence of Ca2+[]. The structure of C2 domains in synaptotagmin I has been deduced: the C2 polypeptide forms an 8-stranded β-sandwich constructed around a conserved 4-stranded motif, designated a C2 key []. The calcium binding region is a cup-shaped depression formed by the N- and C-terminal loops of the C2-key motif, while the site of phospholipid interaction is thought to be a polybasic sequence on the hairpin loop connecting strands 3 and 4 [].

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Publication

17548353 | J:161112

First Author:	Ke B
Year:	2007
Journal:	J Biol Chem
Title:	Doc2beta is a novel Munc18c-interacting partner and positive effector of syntaxin 4-mediated exocytosis.
Volume:	282
Issue:	30
Pages:	21786-97

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Publication

27002738 | J:231949

First Author:	San Agustin JT
Year:	2016
Journal:	Nat Commun
Title:	Genetic link between renal birth defects and congenital heart disease.
Volume:	7

Pages:	11103

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Allele

Enpp1<ttw-Ham> | MGI:6402836

Name:	ectonucleotide pyrophosphatase/phosphodiesterase 1; tiptoe walking Hamamatsu University School of Medicine
Allele Type:	Spontaneous
Attribute String:	Null/knockout

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Publication

33753311 | J:317639

First Author:	Bourgeois-Jaarsma Q
Year:	2021
Journal:	Mol Cell Neurosci
Title:	Ca²⁺ sensor proteins in spontaneous release and synaptic plasticity: Limited contribution of Doc2c, rabphilin-3a and synaptotagmin 7 in hippocampal glutamatergic neurons.
Volume:	112

Pages:	103613

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Protein

D3YVX0

Organism:	Mus musculus/domesticus
Length:	69
Fragment?:	true

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Protein

F6UNQ3

Organism:	Mus musculus/domesticus
Length:	140
Fragment?:	true

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Protein

D6RGS5

Organism:	Mus musculus/domesticus
Length:	186
Fragment?:	false

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Protein

A0A0J9YV12

Organism:	Mus musculus/domesticus
Length:	49
Fragment?:	true

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Protein

F6YZT0

Organism:	Mus musculus/domesticus
Length:	67
Fragment?:	true

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Publication

15141306 | -

First Author:	Creutz CE
Year:	2004
Journal:	Cell Mol Life Sci
Title:	Characterization of the yeast tricalbins: membrane-bound multi-C2-domain proteins that form complexes involved in membrane trafficking.
Volume:	61
Issue:	10
Pages:	1208-20

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Publication

14983047 | -

First Author:	Shin OH
Year:	2004
Journal:	Proc Natl Acad Sci U S A
Title:	Unexpected Ca2+-binding properties of synaptotagmin 9.
Volume:	101
Issue:	8
Pages:	2554-9

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Publication

17263688 | -

First Author:	Grise F
Year:	2007
Journal:	Biochem J
Title:	Distinct roles of the C2A and the C2B domain of the vesicular Ca2+ sensor synaptotagmin 9 in endocrine beta-cells.
Volume:	403
Issue:	3
Pages:	483-92

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Publication

9382842 | -

First Author:	Lockyer PJ
Year:	1997
Journal:	Curr Biol
Title:	Distinct subcellular localisations of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m result from the GAP1IP4BP PH domain directing plasma membrane targeting.
Volume:	7
Issue:	12
Pages:	1007-10

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Publication

25294679 | J:305893

First Author:	Schurmans S
Year:	2015
Journal:	Adv Biol Regul
Title:	The Ras/Rap GTPase activating protein RASA3: from gene structure to in vivo functions.
Volume:	57

Pages:	153-61

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Protein Domain

IPR041108 | PP_kinase_C_1

Type:

Domain

Description:

Polyphosphate kinase (Ppk) catalyses the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules. This C1-terminal domain has a structure similar to phospholipase D. It is one of two closely related carboxy-terminal domains (C1 and C2 domains). Both the C1 and C2 domains (residues 322-502 and 503-687, respectively) consist of a sevenstranded mixed β-sheet flanked by five α-helices. However, the structural topology and relative orientations of the helices to the β-sheet in these two domains are different. The C1 and C2 domains are highly conserved in the PPK family. Some of the residues previously shown to be crucial for the enzyme catalytic activity are located in these two domains [].

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Protein Domain

IPR028691 | SYT9

Type:

Family

Description:

Synaptotagmin-9 (SYT9) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains (known as C2A and C2B domains). Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding.Synaptotagmin 1 (originally called p65) was the first member of the synaptotagmin family identified [, ]. It has been shown to function as a Ca2+ sensor on the synaptic vesicle surface, therefore to regulate Ca2+ dependent neurotransmitter release [, ]. SYT9 shares high degree of protein sequence similarity with SYT1. However, unlike SYT1, the C2 domain of SYT9 does not form Ca2+/phospholipid complexes and the endogenous SYT9 does not associate with SNARE complexes in the absence or presence of Ca2+. The C2 domain of SYT9 has low Ca2+ affinity and may have a modulatory Ca2+-dependent function []. SYT9 is involved in endocrine secretion such as insulin release from large dense core vesicles in pancreatic beta-cells [].

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Protein Domain

IPR017147 | Tricalbin

Type:

Family

Description:

Tricalbins constitute a synaptotagmin-like yeast protein family. Tricalbins contain several copies of C2 domains and are thought to be involved in membrane traffic [, , ]. As extended synaptotagmins, tricalbins also possess a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that is found in proteins localized to ER-organelle contact sites []. The ER-plasma membrane tethering function of tricalbins mediates the formation of ER-PM contacts sites []which are thought to mediate transport glycerolipids between the two bilayers []. The family consists of three members: tricalbin 1-3. The C2 domains of tricalbins 1 and 3 are calcium-dependent lipid-binding units comparable to mammalian synaptotagmin C2 domains, while tricalbin 2 does not seem to bind lipids in response to calcium signaling [].

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Protein Domain

IPR037721 | Ferlin

Type:

Family

Description:

Ferlins are involved in vesicle fusion events []. Ferlins and other proteins, such as synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1).Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF [].

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Protein Domain

IPR025200 | PPK_C_dom2

Type:

Domain

Description:

Polyphosphate kinase (Ppk) catalyses the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules. This C2-terminal domain has a structure similar to phospholipase D. It is one of two closely related carboxy-terminal domains (C1 and C2 domains). Both the C1 and C2 domains (residues 322-502 and 503-687, respectively) consist of a sevenstranded mixed β-sheet flanked by five α-helices. However, the structural topology and relative orientations of the helices to the β-sheet in these two domains are different. The C1 and C2 domains are highly conserved in the PPK family. Some of the residues previously shown to be crucial for the enzyme catalytic activity are located in these two domains [].

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Protein Domain

IPR037773 | RASA2_PH

Type:

Domain

Description:

GAP1 (GTPase-activating protein 1) family members include RASA2 (GAP1m), RASAL (RASAL1), GAP1(IP4BP or RASA3), and CAPRI (RASA4). They all display Ras GAP activity. With the exception of RASA2, they all possess an arginine finger-dependent GAP activity on Rap1 [, ]. They contain N-terminal tandem C2 domain repeats, a centrally located Ras-GAP domain, and a PH (pleckstrin homology) domain containing a Btk motif [].This entry represents the PH domain of Ras GTPase-activating protein 2 (RASA2, also known as GAP1m). The tandem C2 domains of RASA2, like those of GAP1IP4BP, do not contain the conserved C2 motif that is known to be required for calcium-dependent phospholipid binding. RASA2 is regulated by the binding of its PH domains to phophoinositides, PIP3 (phosphatidylinositol 3,4,5-trisphosphate) []. It suppresses RAS, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation []. RASA2 also binds to inositol 1,3,4,5-tetrakisphosphate (IP4) [].

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Protein Domain

IPR037774 | RASA3_PH

Type:

Domain

Description:

GAP1 (GTPase-activating protein 1) family members include RASA2 (GAP1m), RASAL (RASAL1), GAP1(IP4BP or RASA3), and CAPRI (RASA4). They all display Ras GAP activity. With the exception of RASA2, they all possess an arginine finger-dependent GAP activity on Rap1 [, ]. They contain N-terminal tandem C2 domain repeats, a centrally located Ras-GAP domain, and a PH (pleckstrin homology) domain containing a Btk motif [].This entry represents the PH domain of Ras GTPase-activating protein 3 (RASA3, also known as GAP1 or IP4BP). The RASA3 PH domain binds to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) and I(1,3,4,5)P4 []. Its C2 domains, like those of RASA2 (GAP1M), do not contain the C2 motif that is known to be required for calcium-dependent phospholipid binding [].

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Protein Domain

IPR037777 | RASA4_PH

Type:

Domain

Description:

GAP1 (GTPase-activating protein 1) family members include RASA2 (GAP1m), RASAL (RASAL1), GAP1(IP4BP or RASA3), and CAPRI (RASA4). They all display Ras GAP activity. With the exception of RASA2, they all possess an arginine finger-dependent GAP activity on Rap1 [, ]. They contain N-terminal tandem C2 domain repeats, a centrally located Ras-GAP domain, and a PH (pleckstrin homology) domain containing a Btk motif [].This entry represents the PH domain of Ras GTPase-activating protein 4 (RASA4, also known as CAPRI). Both CAPRI and RASAL are calcium-activated RasGAPs that inactivate Ras at the plasma membrane. Its tandem C2 domains bind phospholipids upon an elevation in the intracellular free Ca2+ concentration ([Ca2+]i). CAPRI and RASAL differ in that CAPRI is an amplitude sensor while RASAL senses calcium oscillations [, ]. This difference between them resides not in their C2 domains, but in their PH domains leading to speculation that this might reflect an association with either phosphoinositides and/or proteins [].

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Protein Domain

IPR025939 | Aida_C

Type:

Domain

Description:

The axin interaction dorsalization-associated (Aida) protein was characterised in zebrafish as a protein that utilizes its C-terminal region to interact with axis formation inhibitor (Axin), which is a microtubule-interacting scaffold protein for several distinct signalling proteins in the Wnt cascade. The C-terminal region of the Aida protein is a distinct version of the C2 domain. This Aida-type C2 domain is found in the C-terminal region of the proteins and it is critical for interactions with cytoskeletal in the context of cellular adhesion points, thus, it is combined with diverse domains related to cytoskeletal functions, e.g. EF hands, coiled coils, IQ calmodulin-binding motifs, ankyrin repeats and myosin head motor domain, or with a second lipid-binding domain, e.g. the PH domain. The Aida-type C2 domain is found only in the metazoan, choanoflagellate, chromist and chlorophyte lineages [, ].This domain has predominantly a β-strand globular fold composed of an antiparallel β-sandwich with two β-sheets, and three short α-helices to stabilize the conformation [].

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Publication

7683413 | J:20863

First Author:	Clevidence DE
Year:	1993
Journal:	Proc Natl Acad Sci U S A
Title:	Identification of nine tissue-specific transcription factors of the hepatocyte nuclear factor 3/forkhead DNA-binding-domain family.
Volume:	90
Issue:	9
Pages:	3948-52

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Publication

21095589 | J:166998

First Author:	Miller SA
Year:	2010
Journal:	Mol Cell
Title:	Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression.
Volume:	40
Issue:	4
Pages:	594-605

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