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CDC42_CHICK
ID   CDC42_CHICK             Reviewed;         191 AA.
AC   Q90694;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Cell division control protein 42 homolog;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953};
DE   AltName: Full=G25K GTP-binding protein;
DE   Flags: Precursor;
GN   Name=CDC42;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Inner ear;
RX   PubMed=9224952; DOI=10.1016/s0167-4781(97)00027-4;
RA   Gong T.W., Shin J.J., Burmeister M., Lomax M.I.;
RT   "Complete cDNAs for CDC42 from chicken cochlea and mouse liver.";
RL   Biochim. Biophys. Acta 1352:282-292(1997).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC       an active GTP-bound and an inactive GDP-bound state. In active state
CC       binds to a variety of effector proteins to regulate cellular responses.
CC       Involved in epithelial cell polarization processes. Regulates the
CC       bipolar attachment of spindle microtubules to kinetochores before
CC       chromosome congression in metaphase. Regulates cell migration. Plays a
CC       role in the extension and maintenance of the formation of thin, actin-
CC       rich surface projections called filopodia. Also plays a role in
CC       phagocytosis through organization of the F-actin cytoskeleton
CC       associated with forming phagocytic cups. {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000250|UniProtKB:P60953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P60766,
CC         ECO:0000250|UniProtKB:P60953};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P60766,
CC         ECO:0000250|UniProtKB:P60953};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC       activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC       and GDP dissociation inhibitors which inhibit the dissociation of the
CC       nucleotide from the GTPase. {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000250|UniProtKB:P60953}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P60953}. Midbody {ECO:0000250|UniProtKB:P60953}.
CC       Cell projection, dendrite {ECO:0000250|UniProtKB:P60766}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U40848; AAC00027.1; -; mRNA.
DR   RefSeq; NP_990379.1; NM_205048.1.
DR   RefSeq; XP_015152311.1; XM_015296825.1.
DR   RefSeq; XP_015152312.1; XM_015296826.1.
DR   AlphaFoldDB; Q90694; -.
DR   SMR; Q90694; -.
DR   MINT; Q90694; -.
DR   STRING; 9031.ENSGALP00000034254; -.
DR   PaxDb; Q90694; -.
DR   Ensembl; ENSGALT00000034897; ENSGALP00000034254; ENSGALG00000004796.
DR   Ensembl; ENSGALT00000049495; ENSGALP00000050376; ENSGALG00000004796.
DR   GeneID; 395917; -.
DR   KEGG; gga:395917; -.
DR   CTD; 998; -.
DR   VEuPathDB; HostDB:geneid_395917; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00940000153675; -.
DR   HOGENOM; CLU_041217_21_3_1; -.
DR   InParanoid; Q90694; -.
DR   OrthoDB; 1091615at2759; -.
DR   PhylomeDB; Q90694; -.
DR   Reactome; R-GGA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-GGA-182971; EGFR downregulation.
DR   Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-GGA-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-GGA-525793; Myogenesis.
DR   Reactome; R-GGA-5625970; RHO GTPases activate KTN1.
DR   Reactome; R-GGA-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
DR   Reactome; R-GGA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-GGA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-GGA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-GGA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-GGA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-GGA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-GGA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-GGA-9013408; RHOG GTPase cycle.
DR   Reactome; R-GGA-9013409; RHOJ GTPase cycle.
DR   Reactome; R-GGA-9013420; RHOU GTPase cycle.
DR   Reactome; R-GGA-9013423; RAC3 GTPase cycle.
DR   Reactome; R-GGA-9013424; RHOV GTPase cycle.
DR   Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q90694; -.
DR   Proteomes; UP000000539; Chromosome 21.
DR   Bgee; ENSGALG00000004796; Expressed in colon and 12 other tissues.
DR   ExpressionAtlas; Q90694; baseline.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0042995; C:cell projection; ISS:AgBase.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0017119; C:Golgi transport complex; IEA:Ensembl.
DR   GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR   GO; GO:0000322; C:storage vacuole; IEA:Ensembl.
DR   GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0032427; F:GBD domain binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0003924; F:GTPase activity; ISS:AgBase.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0031996; F:thioesterase binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:AgBase.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
DR   GO; GO:0003161; P:cardiac conduction system development; IEA:Ensembl.
DR   GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR   GO; GO:0036336; P:dendritic cell migration; IEA:Ensembl.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0086101; P:endothelin receptor signaling pathway involved in heart process; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0046847; P:filopodium assembly; ISS:AgBase.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0045185; P:maintenance of protein location; ISS:AgBase.
DR   GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR   GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:AgBase.
DR   GO; GO:0048664; P:neuron fate determination; IEA:Ensembl.
DR   GO; GO:0038189; P:neuropilin signaling pathway; IEA:Ensembl.
DR   GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:AgBase.
DR   GO; GO:0048549; P:positive regulation of pinocytosis; IEA:Ensembl.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:AgBase.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISS:AgBase.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR   GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
DR   CDD; cd01874; Cdc42; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR037874; Cdc42.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Differentiation;
KW   GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation; Neurogenesis;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..188
FT                   /note="Cell division control protein 42 homolog"
FT                   /id="PRO_0000198956"
FT   PROPEP          189..191
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281286"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         188
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           188
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  21273 MW;  51A437E22A4D8BEF CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
     DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPKKTRRCVL L
 
 
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