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Search results 7501 to 7600 out of 8285 for C2

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Type Details Score
Publication
1970334 | J:10447
First Author: Cameron PU
Year: 1990
Journal: Immunogenetics
Title: Conservation of the central MHC genome: PFGE mapping and RFLP analysis of complement, HSP70, and TNF genes in the goat.
Volume: 31
Issue: 4
Pages: 253-64
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Publication
17559643 | J:125838
 
First Author: Merrick D
Year: 2007
Journal: BMC Dev Biol
Title: A role for Insulin-like growth factor 2 in specification of the fast skeletal muscle fibre.
Volume: 7
Pages: 65
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Publication
3405222 | J:218154
First Author: Sternberg EA
Year: 1988
Journal: Mol Cell Biol
Title: Identification of upstream and intragenic regulatory elements that confer cell-type-restricted and differentiation-specific expression on the muscle creatine kinase gene.
Volume: 8
Issue: 7
Pages: 2896-909
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Publication
18547526 | -
First Author: Vakonakis I
Year: 2008
Journal: Structure
Title: Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain.
Volume: 16
Issue: 6
Pages: 944-53
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Publication
23326475 | J:195873
First Author: Qiao S
Year: 2013
Journal: PLoS One
Title: Dab2IP GTPase activating protein regulates dendrite development and synapse number in cerebellum.
Volume: 8
Issue: 1
Pages: e53635
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Publication
19033661 | J:144734
First Author: Zhang H
Year: 2008
Journal: J Clin Invest
Title: AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice.
Volume: 118
Issue: 12
Pages: 3904-16
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Protein
Q9D9R7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
Q6ZPJ0
Organism: Mus musculus/domesticus
Length: 1128  
Fragment?: false
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Publication
16647110 | -
First Author: Knight ZA
Year: 2006
Journal: Cell
Title: A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling.
Volume: 125
Issue: 4
Pages: 733-47
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Protein
Q9D410
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: false
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Protein
Q3U806
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: true
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Protein
Q2PMX7
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
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Protein
A2AI93
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
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Protein
A0A3P9AQ15
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
Q3TPL1
Organism: Mus musculus/domesticus
Length: 560  
Fragment?: true
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Protein
Q7TPP0
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: true
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Protein
A0A140LHL8
Organism: Mus musculus/domesticus
Length: 629  
Fragment?: true
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Publication
11810268 | J:73952
First Author: Guipponi M
Year: 2001
Journal: Hum Genet
Title: The murine orthologue of the Golgi-localized TPTE protein provides clues to the evolutionary history of the human TPTE gene family.
Volume: 109
Issue: 6
Pages: 569-75
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Protein
A0A0J9YUZ5
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Protein
Q2PMX8
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
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Protein
A0A0J9YU69
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
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Protein
B1AX33
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
Q3UM85
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: true
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Protein
Q3UYH1
Organism: Mus musculus/domesticus
Length: 279  
Fragment?: true
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Protein
Q6KAN5
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
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Protein
Q6PFV2
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: false
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Protein
A0A0J9YUZ2
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
A0A494B9C1
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: true
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Protein
A0A0J9YV63
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
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Protein
Q9JM87
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
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Protein
Q6P8L2
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: true
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Protein
G3UW57
Organism: Mus musculus/domesticus
Length: 370  
Fragment?: false
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Protein
F7BFL8
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: true
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Protein
Q2PMX6
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: false
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Protein
B1AX34
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
Q14AJ8
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Publication
16303567 | -
First Author: Martín-Castellanos C
Year: 2005
Journal: Curr Biol
Title: A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events.
Volume: 15
Issue: 22
Pages: 2056-62
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Publication
16414073 | -
First Author: Williams P
Year: 2006
Journal: J Mol Biol
Title: The 1.6A X-ray structure of the unusual c-type cytochrome, cytochrome cL, from the methylotrophic bacterium Methylobacterium extorquens.
Volume: 357
Issue: 1
Pages: 151-62
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Publication
12082105 | -
First Author: Arcus VL
Year: 2002
Journal: J Biol Chem
Title: The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome.
Volume: 277
Issue: 35
Pages: 32274-81
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Publication
15213171 | -
First Author: Al-Shangiti AM
Year: 2004
Journal: Infect Immun
Title: Structural relationships and cellular tropism of staphylococcal superantigen-like proteins.
Volume: 72
Issue: 7
Pages: 4261-70
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Publication
7479985 | -
First Author: Martin KC
Year: 1995
Journal: Proc Natl Acad Sci U S A
Title: Evidence for synaptotagmin as an inhibitory clamp on synaptic vesicle release in Aplysia neurons.
Volume: 92
Issue: 24
Pages: 11307-11
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Publication
12867508 | -
First Author: Nakhost A
Year: 2003
Journal: J Neurosci
Title: Differential regulation of transmitter release by alternatively spliced forms of synaptotagmin I.
Volume: 23
Issue: 15
Pages: 6238-44
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Publication
15056279 | -
First Author: Nakhost A
Year: 2004
Journal: J Neurochem
Title: Identification and characterization of a novel C2B splice variant of synaptotagmin I.
Volume: 89
Issue: 2
Pages: 354-63
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Publication
15094469 | -
First Author: Lindholm T
Year: 2004
Journal: Neuroreport
Title: Semaphorin and neuropilin expression in motoneurons after intraspinal motoneuron axotomy.
Volume: 15
Issue: 4
Pages: 649-54
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Publication
12213213 | -
First Author: Steinbach K
Year: 2002
Journal: Exp Cell Res
Title: Semaphorin 3E/collapsin-5 inhibits growing retinal axons.
Volume: 279
Issue: 1
Pages: 52-61
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Publication
15051154 | J:91290
First Author: Lillesaar C
Year: 2004
Journal: Neuroscience
Title: Neurites from trigeminal ganglion explants grown in vitro are repelled or attracted by tooth-related tissues depending on developmental stage.
Volume: 125
Issue: 1
Pages: 149-61
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Publication
16202999 | -
First Author: Ozeki-Miyawaki C
Year: 2005
Journal: Exp Cell Res
Title: Identification of functional domains of Mid1, a stretch-activated channel component, necessary for localization to the plasma membrane and Ca2+ permeation.
Volume: 311
Issue: 1
Pages: 84-95
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Publication
11796727 | -
First Author: Maruoka T
Year: 2002
Journal: J Biol Chem
Title: Essential hydrophilic carboxyl-terminal regions including cysteine residues of the yeast stretch-activated calcium-permeable channel Mid1.
Volume: 277
Issue: 14
Pages: 11645-52
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Publication
14697255 | -
First Author: Tada T
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Phe356 in the yeast Ca2+ channel component Mid1 is a key residue for viability after exposure to alpha-factor.
Volume: 313
Issue: 3
Pages: 752-7
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Publication
11016847 | -
First Author: Carnero E
Year: 2000
Journal: Mol Gen Genet
Title: Schizosaccharomyces pombe ehs1p is involved in maintaining cell wall integrity and in calcium uptake.
Volume: 264
Issue: 1-2
Pages: 173-83
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Publication
20403080 | -
First Author: Sato M
Year: 2010
Journal: J Neurochem
Title: Role of the polybasic sequence in the Doc2alpha C2B domain in dense-core vesicle exocytosis in PC12 cells.
Volume: 114
Issue: 1
Pages: 171-81
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Publication
26686281 | -
First Author: Reinisch KM
Year: 2016
Journal: Biochim Biophys Acta
Title: SMP-domain proteins at membrane contact sites: Structure and function.
Volume: 1861
Issue: 8 Pt B
Pages: 924-927
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Publication
28479252 | -
First Author: AhYoung AP
Year: 2017
Journal: Biochem Biophys Res Commun
Title: Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies.
Volume: 488
Issue: 1
Pages: 129-135
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Publication
21787343 | -
First Author: Kopec KO
Year: 2011
Journal: Biochem Soc Trans
Title: Bioinformatics of the TULIP domain superfamily.
Volume: 39
Issue: 4
Pages: 1033-8
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Publication
24965341 | -
 
First Author: Khafif M
Year: 2014
Journal: BMC Bioinformatics
Title: Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.
Volume: 15
Pages: 222
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Publication
17544292 | -
First Author: Hayashi K
Year: 2007
Journal: Pharmacol Res
Title: Protein kinase C theta (PKCtheta): a key player in T cell life and death.
Volume: 55
Issue: 6
Pages: 537-44
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Publication
16978534 | -
First Author: Manicassamy S
Year: 2006
Journal: Cell Mol Immunol
Title: Selective function of PKC-theta in T cells.
Volume: 3
Issue: 4
Pages: 263-70
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Publication
23433459 | -
 
First Author: Zhang EY
Year: 2013
Journal: Adv Pharmacol
Title: The yin and yang of protein kinase C-theta (PKCθ): a novel drug target for selective immunosuppression.
Volume: 66
Pages: 267-312
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Publication
17576073 | -
First Author: Budas GR
Year: 2007
Journal: Pharmacol Res
Title: Cardioprotective mechanisms of PKC isozyme-selective activators and inhibitors in the treatment of ischemia-reperfusion injury.
Volume: 55
Issue: 6
Pages: 523-36
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Publication
14654063 | -
First Author: Murriel CL
Year: 2003
Journal: Arch Biochem Biophys
Title: Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: targeting the apoptotic machinery.
Volume: 420
Issue: 2
Pages: 246-54
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Publication
12359065 | -
First Author: Shieh BH
Year: 2002
Journal: J Biochem
Title: Protein kinase C (PKC) isoforms in Drosophila.
Volume: 132
Issue: 4
Pages: 523-7
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Publication
18637120 | -
First Author: Akita Y
Year: 2008
Journal: FEBS J
Title: Protein kinase Cepsilon: multiple roles in the function of, and signaling mediated by, the cytoskeleton.
Volume: 275
Issue: 16
Pages: 3995-4004
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Publication
21406403 | J:169919
First Author: Hafeez BB
Year: 2011
Journal: Cancer Res
Title: Genetic ablation of PKC epsilon inhibits prostate cancer development and metastasis in transgenic mouse model of prostate adenocarcinoma.
Volume: 71
Issue: 6
Pages: 2318-27
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Publication
26023164 | -
First Author: Gutierrez-Uzquiza A
Year: 2015
Journal: Mol Cancer Res
Title: PKCε Is an Essential Mediator of Prostate Cancer Bone Metastasis.
Volume: 13
Issue: 9
Pages: 1336-46
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Publication
10999941 | -
First Author: Scheschonka A
Year: 2000
Journal: Mol Pharmacol
Title: RGS3 is a GTPase-activating protein for g(ialpha) and g(qalpha) and a potent inhibitor of signaling by GTPase-deficient forms of g(qalpha) and g(11alpha).
Volume: 58
Issue: 4
Pages: 719-28
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Publication
12036301 | J:77362
First Author: Kehrl JH
Year: 2002
Journal: Genomics
Title: Additional 5' exons in the RGS3 locus generate multiple mRNA transcripts, one of which accounts for the origin of human PDZ-RGS3.
Volume: 79
Issue: 6
Pages: 860-8
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Publication
10749886 | -
First Author: Dulin NO
Year: 2000
Journal: J Biol Chem
Title: Regulator of G protein signaling RGS3T is localized to the nucleus and induces apoptosis.
Volume: 275
Issue: 28
Pages: 21317-23
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Publication
15488174 | -
 
First Author: Lu Q
Year: 2004
Journal: Methods Enzymol
Title: Analysis of PDZ-RGS3 function in ephrin-B reverse signaling.
Volume: 390
Pages: 120-8
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Publication
11985497 | -
First Author: Niu J
Year: 2002
Journal: Biochem J
Title: RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain.
Volume: 365
Issue: Pt 3
Pages: 677-84
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Publication
15458844 | -
First Author: Meyer G
Year: 2004
Journal: Neuropharmacology
Title: The complexity of PDZ domain-mediated interactions at glutamatergic synapses: a case study on neuroligin.
Volume: 47
Issue: 5
Pages: 724-33
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Publication
11595167 | -
First Author: Ikeda M
Year: 2001
Journal: Gene
Title: Molecular cloning and characterization of a steroid receptor-binding regulator of G-protein signaling protein cDNA.
Volume: 273
Issue: 2
Pages: 207-14
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Publication
27470558 | -
 
First Author: Gao T
Year: 2016
Journal: Biomed Pharmacother
Title: The association of Phosphatase and tensin homolog (PTEN) deletion and prostate cancer risk: A meta-analysis.
Volume: 83
Pages: 114-121
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Publication
17188236 | -
First Author: Ross B
Year: 2007
Journal: Biochem Biophys Res Commun
Title: High resolution crystal structures of the p120 RasGAP SH3 domain.
Volume: 353
Issue: 2
Pages: 463-8
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Publication
23051731 | J:200258
First Author: Silió V
Year: 2012
Journal: Mol Biol Cell
Title: Phosphoinositide 3-kinase β regulates chromosome segregation in mitosis.
Volume: 23
Issue: 23
Pages: 4526-42
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Publication
17371229 | -
First Author: Patton DT
Year: 2007
Journal: Biochem Soc Trans
Title: The PI3K p110delta controls T-cell development, differentiation and regulation.
Volume: 35
Issue: Pt 2
Pages: 167-71
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Publication
17202264 | J:119070
First Author: McMullen JR
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Protective effects of exercise and phosphoinositide 3-kinase(p110alpha) signaling in dilated and hypertrophic cardiomyopathy.
Volume: 104
Issue: 2
Pages: 612-7
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Publication
16627990 | -
First Author: Liu Z
Year: 2006
Journal: Cell Cycle
Title: Human tumor mutants in the p110alpha subunit of PI3K.
Volume: 5
Issue: 7
Pages: 675-7
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Publication
21543329 | -
First Author: Matsuda M
Year: 2011
Journal: J Biol Chem
Title: Crystal structure of the cytoplasmic phosphatase and tensin homolog (PTEN)-like region of Ciona intestinalis voltage-sensing phosphatase provides insight into substrate specificity and redox regulation of the phosphoinositide phosphatase activity.
Volume: 286
Issue: 26
Pages: 23368-77
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Publication
14659893 | -
 
First Author: Tapparel C
Year: 2003
Journal: Gene
Title: The TPTE gene family: cellular expression, subcellular localization and alternative splicing.
Volume: 323
Pages: 189-99
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Publication
22396523 | -
First Author: Sutton KA
Year: 2012
Journal: Mol Biol Evol
Title: Evolution of the voltage sensor domain of the voltage-sensitive phosphoinositide phosphatase VSP/TPTE suggests a role as a proton channel in eutherian mammals.
Volume: 29
Issue: 9
Pages: 2147-55
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Protein Domain
IPR031468 | SMP_LBD
Type: Domain
Description: Membrane contacts sites (MCSs), regions where two organelles come in closeproximity to one another, act as molecular hubs for the exchange of smallmolecules (e.g. lipids) and signals (e.g. calcium ions). Synaptotagmin-likeMitochondrial lipid-binding Proteins (SMP) domains are exclusively found atMCSs between different organelles such as endoplasmic reticulum (ER)-Mitochondrion, ER-Plasma membrane (PM) and Nucleus-Vacuole junctions. The SMPdomain is able to homo- or heterodimerize, harbors lipids in a hydrophobiccavity and mediates lipid transfer between the two adjacent bilayersindependently of membrane fusion and fission reactions. SMP proteins arewidespread amongst eukaryotic species with a particular enrichment in plantsand features suggestive of species-specific functional variations. SMP domain-containing proteins have been classified into four broad groups: C2 domainsynaptotagmin-like, PH domain-containing HT-008, PDZK8 and mitochondrialprotein families [, , , , , ].The SMP domain consists of 6 β-strands and 3 helices arranged to form abarrel whose interior is lined almost exclusively by hydrophobic residues. The resulting elongated barrel-shaped cylindrical structureharbors a lateral opening and a central hydrophobic cavity where phospholipidscan bind. It dimerizes in an anti-parallel fashion to form a cylindertraversed by a deep hydrophobic groove [, , ]. The SMP domain belongs to theTULIP (for TUbular LIPid-binding) protein superfamily of lipid transferproteins [].
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Protein Domain
IPR034951 | RGS_RGS3
Type: Domain
Description: RGS3 is a member of R4 subfamily of RGS family, a diverse group of multifunctional proteins that regulate cellular signalling events downstream of G-protein coupled receptors (GPCRs) []. Signalling is initiated when GPCRs bind to their ligands, triggering the replacement of GDP bound to the G-alpha subunits of heterotrimeric G proteins with GTP. RGSs inhibit signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. This activity defines them as GTPase activating proteins (GAPs).Regulator of G protein signaling 3 (RGS3) contains a membrane-targeting C2 domain, one PDZ domain, and an RGS (Regulator of G-protein Signalling) domain. RGS3 has been identified to inhibit Galpha-q and Galpha-i-mediated signaling by acting as a GTPase-activating protein []. RGS3 exits as several splice isoforms []. A short form, RGS3S, induced apoptosis when overexpressed [], whereas PDZ-RGS3 has been linked to cell migration through interaction with Ephrin receptors []. RGS3 interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways [, , ].This entry represents the RGS domain of RGS3.
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Protein Domain
IPR016013 | Binary_toxinA_clost-typ
Type: Family
Description: A large group of bacterial exotoxins are referred to as "A/B toxins", essentially because they are formed from two subunits. The "A"subunitpossesses enzyme activity, and is transferred to the host cell followinga conformational change in the membrane-bound transport "B"subunit [].Clostridial species are one of the major causes of food poisoning/gastro-intestinal illnesses. They are Gram-positive, spore-forming rods that occurnaturally in the soil []. Included in the family are: Clostridium botulinum, which produces one of the most potent toxins in existence; Clostridium tetani, causative agent of tetanus; and Clostridium perfringens, commonly found in wound infections and diarrhoea cases. Among the toxins produced by certain Clostridium spp. are the binary exotoxins. These proteins consist of two independent polypeptides, whichcorrespond to the A/B subunit moieties. The enzyme component (A) enters the cell through endosomes produced by the oligomeric binding/translocationprotein (B), and prevents actin polymerisation through ADP-ribosylation of monomeric G-actin [, , ].Members of the "A"binary toxin family include C. perfringens iota toxin Ia[], C. botulinum C2 toxin CI [], and Clostridium difficile ADP-ribosyltransferase []. Other homologous proteins have been found in Clostridium spiroforme [, ], and related bacteria such as Bacillus species.
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Protein Domain
IPR031968 | VASt
Type: Domain
Description: The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The ~190-amino acid VASt domain is predominantly associated with lipid bindingdomains such as GRAM, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol [, ].The predicted structure of the VASt domain is a two-layer sandwich α/β fold, also called "helix grip fold", containing three α-helices (α1 to3), six β-sheets (β1 to 6) and two loops (ω1 and 2) numbered from N to C terminus [].Some proteins known to contain a VASt domain are listed below:Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain.Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes.Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes.Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation. May be involved in sterol transfer between intracellular membranes.Human GramD1a-c.
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Protein Domain
IPR028406 | PLC-delta3
Type: Family
Description: Phosphoinositide-specific phospholipase C (PI-PLC), also known as 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase, plays a role in the inositol phospholipid signaling by hydrolysing phosphatidylinositol-4,5-bisphosphate to produce the second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). These cause the increase of intracellular calcium concentration and the activation of protein kinase C (PKC), respectively.The PLC family in murine or human species is comprised of multiple subtypes. On the basis of their structure, they have been divided into five classes, beta (beta-1, 2, 3 and 4), gamma (gamma-1 and 2), delta (delta-1, 3 and 4), epsilon, zeta, and eta types [, ].PLC-delta-3 is essential for trophoblast and placental development []. It locates at the cleavage furrow where it may participate in cytokinesis []. PI-PLC-delta3 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus [].
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Protein Domain
IPR030535 | Doc2a/b
Type: Family
Description: Doc2a (double C2-like domain-containing protein alpha) and Doc2b (double C2-like domain-containing protein beta) are members of the double C2 domain protein family. Doc2a is expressed in neuronal cells and has been implicated in Ca2+-dependent neurotransmitter release [, ]. Doc2a exhibits Ca2+-dependent phospholipid-binding activity through its C2A domain, which is thought to be important for the regulation of Ca2+-dependent exocytosis. The C2B domain is required for binding of syntaxin-1a/synaptosome-associated protein of 25kDa (SNAP-25) heterodimer []. Doc2a is also expressed in pancreatic islets, and has been implicated together with Doc2b in the synergistic regulation of glucose-stimulated insulin secretion [].Doc2b contains two calcium and phospholipid binding domains in its C terminus []. It interacts with the SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) complex composed of SNAP25, STX1A and VAMP2. Doc2b regulates SNARE-dependent fusion of vesicles with membranes in a calcium-dependent manner. It is involved in calcium-dependent spontaneous release of neurotransmitter, with a function analogous to synaptotagmin-1, but with a higher Ca2+ sensitivity []. Doc2b is a positive SNARE regulator for glucose transporter GLUT4 vesicle fusion and mediates insulin-stimulated glucose transport in adipocytes []. It is involved in both insulin-stimulated glucose uptake in adipocytes and glucose-stimulated insulin secretion in pancreatic cells, as well as insulin responsiveness in skeletal muscle [, ].
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Protein Domain
IPR024338 | Mid1/Ehs1
Type: Family
Description: In Saccharomyces cerevisiae, Mid1 is a yeast plasma membrane protein required for Ca2+ influx induced by the mating pheromone alpha-factor during the mating process [, , ]. The protein is composed of 548-amino-acid residues, contains four hydrophobic regions (H1, H2, H3 and H4) and two cysteine-rich regions (C1 and C2) at the C terminus. H1 appears to be a signal sequence necessary for the alpha-factor-induced delivery to the plasma membrane. The region from H1 to H3 is required for the localisation of Mid1 in the plasma and ER membranes. C1 and C2 are thought to be involved in oligomerisation via the formation of disulphide bonds. Trafficking of Mid1-GFP to the plasma membrane is dependent on the N-glycosylation of Mid1 and the transporter protein Sec12. This suggests that the trafficking of Mid1-GFP to the plasma membrane requires a Sec12-dependent pathway from the ER to the Golgi, and that Mid1 is recruited via a Sec6- and Sec7-independent pathway from the Golgi to the plasma membrane.This entry also includes Ehs1 from Schizosaccharomyces pombe. Ehs1 is required for Ca2+ influx and for vitality of cells in a late, pheromone-induced event of the mating process requiring calcium-induced signaling [].
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Protein Domain
IPR037702 | PI3Kbeta_dom
Type: Domain
Description: This entry represents the catalytic domain of PI3Kbeta (also known as p110beta), which is a Class IA phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). It has been shown to regulate chromosome segregation in mitosis [].PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (p110alpha, beta, gamma or delta) and one of several regulatory subunits (p85alpha, beta or gamma). They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors [].
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Protein Domain
IPR037703 | PI3Kdelta_dom
Type: Domain
Description: This entry represents the catalytic domain of PI3Kdelta (also known as p110delta), which is a Class IA phosphoinositide-3-kinase (PI3K) that that phosphorylates PftdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PI3Kdelta is mainly expressed in immune cells and plays an important role in cellular and humoral immunity. It plays a major role in antigen receptor signaling in B-cells, T-cells, and mast cells. It regulates the differentiation of peripheral helper T-cells and controls the development and function of regulatory T-cells [].PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (p110alpha, beta, gamma or delta) and one of several regulatory subunits (p85alpha, beta or gamma). They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors [].
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Protein Domain
IPR037704 | PI3Kalpha_dom
Type: Domain
Description: This entry represents the catalytic domain of PI3Kalpha (also known as p110alpha), which is a Class IA phosphoinositide-3-kinase (PI3K) that that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PI3Kalpha plays an important role in insulin signaling []. It also mediates cardiac growth induced by exercise training []. Mutations in the PI3Kalpha gene have been linked to various cancers []. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (p110alpha, beta, gamma or delta) and one of several regulatory subunits (p85alpha, beta or gamma). They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors [].
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Protein Domain
IPR034668 | nPKC_theta
Type: Domain
Description: Protein kinases C (PKCs) constitute a family of Ser/Thr kinases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain [, ]. Novel PKCs (nPKCs) comprise delta, epsilon, eta, and theta isoforms, which have tandem C1 domains and a C2 domain that does not bind calcium []. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology []. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation []. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases [].
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Protein Domain
IPR009153 | Cyt_cL
Type: Family
Description: In Gram-negative bacteria, growth on methanol is dependent on the soluble, periplasmic quinoprotein methanol dehydrogenase, which oxidises methanol to formaldehyde. The electrons generated by this reaction are transferred from the reduced enzyme to the unusual cytochrome cL, which is subsequently oxidised itself by cytochrome c2 (also known as cytochrome cH), which then transfers the electrons to a membrane-bound cytochrome oxidase [].This entry represents cytochrome cL (also known as cytochrome C551i in some species), whose amino acid sequence is distinct from that of other c-type cytochromes and does not fit into any established amino acid sequence class. Despite its lack of homology to other proteins, many of its properties, eg the low-spin haem prosthetic group, are similar to those of class 1 cytochrome c proteins. Other properties, such as its large size and acidic nature are distinct to cytochrome cL. The core of this protein has a structure typical of class I cytochrome c proteins, consisting of compact alpha helices enclosing the haem c prosthetic group with one edge of the haem exposed []. Unusually, there is a tightly bound calcium close to the haem group which is thought to help stabilise redox potential and may be involved in the transfer of electrons from methanol dehydrogenase to the haem group.
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Protein Domain
IPR035012 | Tensin-like_SH2
Type: Domain
Description: This entry represents the SH2 domain found in tensin-like proteins. The tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: tensin1, tensin2 (TENC1, C1-TEN), tensin3 and tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of tensin2 and tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein [].PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway []. Because of their PTEN-like domains, the tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only tensin2 and tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [, , ].
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Protein Domain
IPR000922 | Lectin_gal-bd_dom
Type: Domain
Description: The D-galactoside binding lectin purified from sea urchin (Anthocidaris crassispina) eggs exists as a disulphide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity []. The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galactoside binding lectin, it was latter shown that it bind to L-rhamnose preferentially [, ]. L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure.A cysteine-rich domain homologous to the SUEL protein has been identified in the following proteins [, , ]:Plant beta-galactosidases () (lactases).Mammalian latrophilin, the calcium independent receptor of alpha-latrotoxin (CIRL). The galactose-binding lectin domain is not required for alpha-latratoxin binding [].Human lectomedin-1.Rhamnose-binding lectin (SAL) from catfish (Silurus asotus, Namazu) eggs. This protein is composed of three tandem repeat domains homologous to the SUEL lectin domain. All cysteine positions of each domain are completely conserved [].The hypothetical B0457.1, F32A7.3A and F32A7.3B proteins from Caenorhabditis elegans.The human KIAA0821 protein.
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Protein Domain
IPR046770 | DOCKER_Lobe_B
Type: Domain
Description: This entry represents a conserved region within a number of eukaryotic dedicator of cytokinesis proteins (DOCK), which are guanine nucleotide exchange factors (GEFs) [, , ], that activate some small GTPases by exchanging bound GDP for free GTP such as Rac. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis []. These proteins have a DOCK-homology region 1 (DHR-1, also known as DOCK-type C2 domain) at the N-terminal and a DHR-2 (also known as DOCKER domain) at the C-terminal. The DOCKER domain () is a GEF catalytic domain organised into three lobes, A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe B, which adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement. This lobe changes its position relative to lobe C and the bound GTPase, which suggests that lobe B distinguishes between the switch 1 conformations of the small GTPases Rac1 and Cdc42 [, ].
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Protein Domain
IPR034669 | nPKC_epsilon
Type: Domain
Description: Protein kinases C (PKCs) constitute a family of Ser/Thr kinases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain [, ]. Novel PKCs (nPKCs) comprise delta, epsilon, eta, and theta isoforms, which have tandem C1 domains and a C2 domain that does not bind calcium []. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein [, ]. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumour invasion and metastasis[, ]. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage [, ]. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility [].This entry also includes PKCs from invertebrates, such as Pkc98E from Drosophila, which exhibits sequence identity to PKC-epsilon [].
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Protein Domain
IPR045102 | PTP_VSP_TPTE
Type: Domain
Description: Proteins containing this domain are a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis []. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity [, ]. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain [].
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Protein Domain
IPR015512 | Semaphorin_4F
Type: Family
Description: Semaphorins were first cloned as recognised mediators of cellular guidance, and consist of a large family of phylogenetically conserved secreted and transmembrane signalling proteins. Among the best-characterised vertebrate Semaphorins are the five secreted Class 3 members that contain an approximately 500 amino acid N-terminal Semaphorin domain, a C2 type immunoglobulin domain, and a highly basic C-terminal tail []. Two receptor families have been implicated in mediating the actions of class 3 semaphorins: the Neuropilins and Plexins. The nine known vertebrate Plexins are divided into four subfamilies (A through D) based on structure []. Several Plexins have been shown to interact directly with some class 4, 7 and V Semaphorins, but class 3 Semaphorins, however, do not appear to bind Plexins directly. Rather, the functional receptors for these Semaphorins are complexes of Neuropilins and A-type Plexins, with the former serving as the ligand-binding moiety and the latter the signal-transducing component [, ]. There are two Neuropilins (NP-1 and NP-2) that bind the five class 3 Semaphorins preferentially. In particular, Sema3A binds NP-1, whereas Sema3F utilises NP-2, while NP-1 and NP-2 heterodimers are thought to serve as functional receptors for Sema3C [].Semaphorin 4F may be involved in the injury response of intramedullary axotomized motoneurons [].
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Protein Domain
IPR015513 | Semaphorin_3E
Type: Family
Description: Semaphorins were first cloned as recognised mediators of cellular guidance, and consist of a large family of phylogenetically conserved secreted and transmembrane signalling proteins. Among the best-characterised vertebrate Semaphorins are the five secreted Class 3 members that contain an approximately 500 amino acid N-terminal Semaphorin domain, a C2 type immunoglobulin domain, and a highly basic C-terminal tail []. Two receptor families have been implicated in mediating the actions of class 3 semaphorins: the Neuropilins and Plexins. The nine known vertebrate Plexins are divided into four subfamilies (A through D) based on structure []. Several Plexins have been shown to interact directly with some class 4, 7 and V Semaphorins, but class 3 Semaphorins, however, do not appear to bind Plexins directly. Rather, the functional receptors for these Semaphorins are complexes of Neuropilins and A-type Plexins, with the former serving as the ligand-binding moiety and the latter the signal-transducing component [, ]. There are two Neuropilins (NP-1 and NP-2), which bind the five class 3 Semaphorins preferentially. In particular, Sema3A binds NP-1, whereas Sema3F utilises NP-2, while NP-1 and NP-2 heterodimers are thought to serve as functional receptors for Sema3C [].Recent work suggests a possible role of Gallus gallus (Chicken) Sema3E/collapsin-5 in restricting growth of retinal ganglion cell axons to the optic fibre layer [].
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Protein Domain
IPR015514 | Semaphorin_6C
Type: Family
Description: Semaphorins were first cloned as recognised mediators of cellular guidance, and consist of a large family of phylogenetically conserved secreted and transmembrane signalling proteins. Among the best-characterised vertebrate Semaphorins are the five secreted Class 3 members that contain an approximately 500 amino acid N-terminal Semaphorin domain, a C2 type immunoglobulin domain, and a highly basic C-terminal tail []. Two receptor families have been implicated in mediating the actions of class 3 semaphorins: the Neuropilins and Plexins. The nine known vertebrate Plexins are divided into four subfamilies (A through D) based on structure []. Several Plexins have been shown to interact directly with some class 4, 7 and V Semaphorins, but class 3 Semaphorins, however, do not appear to bind Plexins directly. Rather, the functional receptors for these Semaphorins are complexes of Neuropilins and A-type Plexins, with the former serving as the ligand-binding moiety and the latter the signal-transducing component [, ]. There are two Neuropilins (NP-1 and NP-2) that bind the five class 3 Semaphorins preferentially. In particular, Sema3A binds NP-1, whereas Sema3F utilises NP-2, while NP-1 and NP-2 heterodimers are thought to serve as functional receptors for Sema3C [].Recent microarray studies have suggested a role for Sema 6C in dental mesenchyme-induced neurite repulsion [].
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