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Search results 701 to 800 out of 8285 for C2

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Type Details Score
UniProt Feature
UniProt Feature
Begin: 1
Description: Coiled-coil and C2 domain-containing protein 1A
Type: chain
End: 943
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UniProt Feature
UniProt Feature
Begin: 2
Description: Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Type: chain
End: 1686
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UniProt Feature
UniProt Feature
Begin: 1
Description: NADH dehydrogenase [ubiquinone] 1 subunit C2
Type: chain
End: 120
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UniProt Feature
UniProt Feature
Begin: 1
Description: Coiled-coil and C2 domain-containing protein 1B
Type: chain
End: 848
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UniProt Feature
UniProt Feature
Begin: 1
Description: Coiled-coil and C2 domain-containing protein 2A
Type: chain
End: 1633
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UniProt Feature
UniProt Feature
Begin: 1
Description: Solute carrier family 35 member C2
Type: chain
End: 364
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UniProt Feature
UniProt Feature
Begin: 725
Description: Cartilage intermediate layer protein 1 C2
Type: chain
End: 1184
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UniProt Feature
UniProt Feature
Begin: 716
Description: Cartilage intermediate layer protein 2 C2
Type: chain
End: 1162
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Protein
F8VPL2
Organism: Mus musculus/domesticus
Length: 1686  
Fragment?: false
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HT Sample
GSM2985071
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985091
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985111
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985133
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985153
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985173
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985195
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985215
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985238
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985292
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985297
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985302
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985308
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985314
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985320
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985336
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985342
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985348
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985354
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985360
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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HT Sample
GSM2985366
Organism Name: mouse, laboratory
Sex: Not Specified
Age: embryonic day 7.5
Stage: 11
Structure . Name: embryo
Notes: section from late-gastrulation embryo, region C2
Curation Status: Curated
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Protein
Q61850
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
Q52KB6-3
Organism: Mus musculus/domesticus
Length: 2130  
Fragment?: false
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Protein
Q52KB6-2
Organism: Mus musculus/domesticus
Length: 1943  
Fragment?: false
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Protein
Q9D4D2
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: false
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Protein
Q924P1
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Protein
Q9JHS5
Organism: Mus musculus/domesticus
Length: 41  
Fragment?: true
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Protein
D6RH58
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: false
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Protein
B9EI61
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
V9GXB2
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
E9Q152
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: false
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Protein
Q20BD0
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
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Publication
22073306 | J:180993
First Author: Nielsen GK
Year: 2011
Journal: PLoS One
Title: Protein replacement therapy partially corrects the cholesterol-storage phenotype in a mouse model of Niemann-Pick type C2 disease.
Volume: 6
Issue: 11
Pages: e27287
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EMAPA Term
C2 neural arch transverse process | EMAPA:26675
Starts At: 26
Ends At: 26
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Protein Coding Gene
MGI:1923492 | Rph3al
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q3U7R1
Organism: Mus musculus/domesticus
Length: 1092  
Fragment?: false
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Publication
7697723 | -
First Author: Sutton RB
Year: 1995
Journal: Cell
Title: Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.
Volume: 80
Issue: 6
Pages: 929-38
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Protein Coding Gene
MGI:1915183 | Hcfc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347481 | Foxc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR030542 | Tac2-N
Type: Family
Description: Tac2-N (tandem C2 domains nuclear protein) represents a novel class of C-type tandem C2 proteins. Tac2-N proteins are almost exclusively localised in the nucleus [].
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Protein Coding Gene
MGI:2685505 | C2cd4d
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1919014 | C2cd2l
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
31666192 | J:292159
 
First Author: Gavini CK
Year: 2020
Journal: Metabolism
Title: Hypothalamic C2-domain protein involved in MC4R trafficking and control of energy balance.
Volume: 102
Pages: 153990
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Publication
18513680 | -
First Author: Tallila J
Year: 2008
Journal: Am J Hum Genet
Title: Identification of CC2D2A as a Meckel syndrome gene adds an important piece to the ciliopathy puzzle.
Volume: 82
Issue: 6
Pages: 1361-7
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Publication
10583959 | -
First Author: Stepp SE
Year: 1999
Journal: Science
Title: Perforin gene defects in familial hemophagocytic lymphohistiocytosis.
Volume: 286
Issue: 5446
Pages: 1957-9
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Publication
9058810 | -
First Author: Vergelli M
Year: 1997
Journal: J Immunol
Title: Human autoreactive CD4+ T cell clones use perforin- or Fas/Fas ligand-mediated pathways for target cell lysis.
Volume: 158
Issue: 6
Pages: 2756-61
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Protein Domain
IPR028928 | CC2D2AN-C2
Type: Domain
Description: A C2 domain is usually involved in targeting proteins to cell membranes. Ciliary CC2D2A protein has two C2 domains and an inactive transglutaminase-like peptidase domain (CC2D2A-TGL) []. This entry represents the first C2 domain. CC2D2A (coiled-coil and C2 domain-containing protein 2A) is a component of the tectonic-like complex, a complex localised at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes []. It is required for ciliogenesis and sonic hedgehog/SHH signalling [].
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Protein Domain
IPR037300 | Perforin-1_C2
Type: Domain
Description: Perforin-1 contains a single copy of a C2 domain in its C terminus and plays a role in lymphocyte-mediated cytotoxicity []. Mutations in perforin-1 lead to familial hemophagocytic lymphohistiocytosis type 2, a rare, rapidly fatal, autosomal recessive immune disorder characterized by uncontrolled activation of T cells and macrophages and overproduction of inflammatory cytokines []. The function of perforin-1 is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes []. 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 phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, , , , , , , ].
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Protein Domain
IPR023315 | SynGAP_C2_N
Type: Homologous_superfamily
Description: This entry represents a small structural domain found at the extreme N terminus of the C2 domain of Ras GTPase-activating protein SynGAP [].
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Protein
Q9CQ54
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
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Protein
A0A0U1RPJ5
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
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Protein
Q9D846
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Publication
35592111 | J:325115
 
First Author: Acheta J
Year: 2022
Journal: Front Mol Neurosci
Title: Cc2d1b Contributes to the Regulation of Developmental Myelination in the Central Nervous System.
Volume: 15
Pages: 881571
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Publication
28982981 | J:257163
First Author: Meliambro K
Year: 2017
Journal: J Biol Chem
Title: The Hippo pathway regulator KIBRA promotes podocyte injury by inhibiting YAP signaling and disrupting actin cytoskeletal dynamics.
Volume: 292
Issue: 51
Pages: 21137-21148
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Publication
23843985 | J:204311
First Author: Roszell BR
Year: 2013
Journal: PLoS One
Title: Pulmonary abnormalities in animal models due to Niemann-Pick type C1 (NPC1) or C2 (NPC2) disease.
Volume: 8
Issue: 7
Pages: e67084
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Publication
22179027 | J:185098
First Author: Boadu E
Year: 2012
Journal: Biochim Biophys Acta
Title: ABCA1-dependent mobilization of lysosomal cholesterol requires functional Niemann-Pick C2 but not Niemann-Pick C1 protein.
Volume: 1821
Issue: 3
Pages: 396-404
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Publication
7592870 | J:46046
First Author: Fukuda M
Year: 1995
Journal: J Biol Chem
Title: Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain.
Volume: 270
Issue: 44
Pages: 26523-7
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Publication
24438076 | J:211602
First Author: Adachi T
Year: 2014
Journal: Biochem J
Title: Niemann-Pick disease type C2 protein induces triglyceride accumulation in silkworm and mammalian cell lines.
Volume: 459
Issue: 1
Pages: 137-47
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Publication
27402802 | J:235219
First Author: Guo H
Year: 2016
Journal: J Lipid Res
Title: Niemann-Pick type C2 deficiency impairs autophagy-lysosomal activity, mitochondrial function, and TLR signaling in adipocytes.
Volume: 57
Issue: 9
Pages: 1644-58
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Protein Domain
IPR033884 | C2_Calpain
Type: Domain
Description: A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases.The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes, including phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies of the C1 domain in Protein Kinase C and the protein kinase catalytic domain []. Regions with significant homology []to the C2-domain have been found in many proteins. The C2 domain is thought to be involved in calcium-dependent phospholipid binding []and in membrane targetting processes such as subcellular localisation. The 3D structure of the C2 domain of synaptotagmin has been reported[], the domain forms an eight-stranded β-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 β-sandwich.
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Protein Domain
IPR037301 | Tollip_C2
Type: Domain
Description: Tollip is a part of the Interleukin-1 receptor (IL-1R) signaling pathway. Tollip is proposed to link serine/threonine kinase IRAK to IL-1Rs as well as inhibiting phosphorylation of IRAK []. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates []. There is a single C2 domain present in Tollip. 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 varietyof substances including phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, , , , , , , ].
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Protein Domain
IPR037775 | C2_C2CD3
Type: Domain
Description: C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development []. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others []. It is required for centriole elongation []. Mutations in the human C2cd3 gene cause Orofaciodigital syndrome 14, which is characterised by malformations of the face, oral cavity, and digits []. It plays an important part in centriolar distal appendage assembly and ciliary vesicle docking in mammals []. 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. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, , , ].
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Protein Domain
IPR037772 | C2_Freud
Type: Domain
Description: The cc2d1a gene family consists of two homologues, CC2D1A (Freud-1) and CC2D1B (Freud-2). Freud-1 is a calcium-regulated repressor of serotonine receptor 5-HT1A and dopamine-D2 receptor expression [, ]. Mutations in cc2d1a has been linked to nonsyndromic mental retardation [, ].CC2D1A/freud-1 and CC2D1B/freud-2 share conserved domains, including several DM14 domains that are specific to this protein family, a C-terminal helix-loop-helix domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal []. The Freud-1 C2 domain appears to be essential for its DNA binding and repressor function; it may mediate protein-protein interactions [].
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Protein Coding Gene
MGI:1924487 | Cc2d2a
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
21763481 | J:178421
First Author: Dowdle WE
Year: 2011
Journal: Am J Hum Genet
Title: Disruption of a ciliary B9 protein complex causes Meckel syndrome.
Volume: 89
Issue: 1
Pages: 94-110
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Protein
Q9R1S0
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
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Publication
16415886 | J:105230
First Author: Kyttälä M
Year: 2006
Journal: Nat Genet
Title: MKS1, encoding a component of the flagellar apparatus basal body proteome, is mutated in Meckel syndrome.
Volume: 38
Issue: 2
Pages: 155-7
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Protein
Q5SW45
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
Q3UK10
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q3UUM5
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
B2KGP7
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
A0A0U1RNW5
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
Q5NCM9
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
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Protein
A0A494BB14
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Protein
Q5SS55
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: true
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Protein
Q284W0
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
Q3UWW7
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein
A0A0U1RPE5
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Protein
Q8R212
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
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Publication
17127412 | -
 
First Author: Ponsard C
Year: 2007
Journal: Front Biosci
Title: Identification of ICIS-1, a new protein involved in cilia stability.
Volume: 12
Pages: 1661-9
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Publication
18337471 | -
First Author: Williams CL
Year: 2008
Journal: Mol Biol Cell
Title: Functional redundancy of the B9 proteins and nephrocystins in Caenorhabditis elegans ciliogenesis.
Volume: 19
Issue: 5
Pages: 2154-68
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Publication
27646273 | -
First Author: Vieillard J
Year: 2016
Journal: J Cell Biol
Title: Transition zone assembly and its contribution to axoneme formation in Drosophila male germ cells.
Volume: 214
Issue: 7
Pages: 875-89
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Publication
26490104 | -
First Author: Slaats GG
Year: 2016
Journal: J Med Genet
Title: MKS1 regulates ciliary INPP5E levels in Joubert syndrome.
Volume: 53
Issue: 1
Pages: 62-72
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Publication
27577095 | -
First Author: Pratt MB
Year: 2016
Journal: J Cell Sci
Title: Drosophila sensory cilia lacking MKS proteins exhibit striking defects in development but only subtle defects in adults.
Volume: 129
Issue: 20
Pages: 3732-3743
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Publication
27272733 | -
First Author: Wang P
Year: 2016
Journal: PLoS Genet
Title: RAB-10 Promotes EHBP-1 Bridging of Filamentous Actin and Tubular Recycling Endosomes.
Volume: 12
Issue: 6
Pages: e1006093
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Protein Domain
IPR010796 | C2_B9-type_dom
Type: Family
Description: The C2 domain is one of the most prevalent eukaryotic lipid-binding domains deployed in diverse functional contexts. Distinct versions of the C2 domain have been recognized, the classical C2, the PI3K-type, the tensin-type, the B9-type, the DOCK-type, the NT-type and the Aida-type. Despite their limited sequence similarity, all C2 domains contain at their core a compact β-sandwich composed of two four-stranded β-sheets with highly variable inter-strand regions that might contain one or more α-helices. One feature that is highly conserved in the C2 domains is the pair of hydrophobic residues on the upper part of the β-sheet, which are involved in imparting a curvature of the sheet that allows formation of a concave ligand-binding area [].This entry represents a family of B9-type C2 domain containing proteins, found in ciliary basal body associated proteins. Although its specific function is unknown, a cilia-specific role has been suggested for the poorly characterised B9-type C2 domain [, , ].Some proteins known to contain a B9-type C2 domain are listed below:Mammalian Tectonic-like complex member MKS1 (also known as Meckel syndrome 1 , MKS1). The tectonic-like complex is localised at the transition zone of primary cilia and acts as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. It is involved in centrosome migration to the apical cell surface during early ciliogenesis [, , ]. The homologue in Drosophila melanogaster is required for ciliary structure and function [, ]. Mammalian proteins B9D1 and B9D2. B9D1 is required for ciliogenesis and sonic hedgehog/SHH signaling [, ].
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Protein Domain
IPR019448 | NT-C2
Type: Domain
Description: The C2 domain is one of the most prevalent eukaryotic lipid-binding domainsdeployed in diverse functional contexts. Many C2 domainsbind directly to membrane lipids and display a wide range of lipidselectivity, with preference for anionic phosphatidylserine (PS) andphosphatidylinositol-phosphates (PIPs).Despite their limited sequence similarity, all C2 domains contain at theircore a compact β-sandwich composed of two four-stranded beta sheets withhighly variable inter-strand regions that might contain one or more alpha-helices.The NT-type C2 domain shows a diverse range of domain architectures but it isnearly always found at the N-termini of proteins that contain it. Hence, ithas been named the N-terminal C2 (NT-C2) family. It is typically coupled witha coiled-coil domain, that could mediate di/oligo-merization and the DIL(Dilute) domain. It is also coupled with the Calponinhomology (CH) domain in EHBP1 proteins, Filamin/ABP280repeats and Mg2+ transporter MgtE N-terminal domain inproteins from chlorophyte algae such as Micromonas and Ostreococcus tauri.Thus, a common theme across the NT-type C2 domain proteins is the combinationto several different domains with microfilament-binding or actin-related roles(i.e. such as CH, DIL, and Filamin). Other conserved groups of the NT-type C2proteins prototyped by EEIG1, PMI1, and SYNC1 have their own distinct C-terminal conserved extensions that are restricted to these groups and mightmediate specific interactions. The primary function of the NT-type C2 domainappears to be the linking of actin/microfilament-binding adaptors to themembrane and to act as a link that tethers endosomal vesicles to thecytoskeleton in course of their intracellular trafficking [, ].
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Protein Domain
IPR035892 | C2_domain_sf
Type: Homologous_superfamily
Description: The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes, including phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies of the C1 domain in Protein Kinase C and the protein kinase catalytic domain []. Regions with significant homology []to the C2-domain have been found in many proteins. The C2 domain is thought to be involved in calcium-dependent phospholipid binding []and in membrane targetting processes such as subcellular localisation. The 3D structure of the C2 domain of synaptotagmin has been reported[], the domain forms an eight-stranded β-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 β-sandwich.
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Protein Domain
IPR037785 | C2_C2CD5
Type: Domain
Description: C2CD5, also known as CDP138 or KIAA0528, is a C2 domain-containing phosphoprotein. It is a substrate for protein kinase Akt2, and it may be involved in the regulation of GLUT4 vesicle-plasma membrane fusion in response to insulin. The C2 domain of C2CD5 was shown to be capable of binding Ca(2+) and lipid membranes []. Other studies indicate that C2CD5 is a CDK5- and FIBP-interacting protein, forming a complex with these proteins that is involved in cell proliferation and migration [].This entry represents the C2 domain of C2CD5.
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Publication
20713135 | -
First Author: Zhang D
Year: 2010
Journal: Gene
Title: Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes.
Volume: 469
Issue: 1-2
Pages: 18-30
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Publication
32514154 | J:293759
First Author: Ozkul Y
Year: 2020
Journal: Sci Rep
Title: A heritable profile of six miRNAs in autistic patients and mouse models.
Volume: 10
Issue: 1
Pages: 9011
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