(data stored in ACNUC8465 zone)

SWISSPROT: 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   11-DEC-2019, entry version 150.
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}.
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   SMR; Q90694; -.
DR   MINT; Q90694; -.
DR   STRING; 9031.ENSGALP00000034254; -.
DR   PaxDb; Q90694; -.
DR   PRIDE; Q90694; -.
DR   Ensembl; ENSGALT00000034897; ENSGALP00000034254; ENSGALG00000004796.
DR   Ensembl; ENSGALT00000049495; ENSGALP00000050376; ENSGALG00000004796.
DR   GeneID; 395917; -.
DR   KEGG; gga:395917; -.
DR   CTD; 998; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00940000153675; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; Q90694; -.
DR   KO; K04393; -.
DR   OMA; GYLADHM; -.
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-194840; Rho GTPase cycle.
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-525793; Myogenesis.
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-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q90694; -.
DR   Proteomes; UP000000539; Chromosome 21.
DR   Bgee; ENSGALG00000004796; Expressed in 11 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; Q90694; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; ISS:AgBase.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISS:AgBase.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:AgBase.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
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:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
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:0045185; P:maintenance of protein location; ISS:AgBase.
DR   GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR   GO; GO:0031333; P:negative regulation of protein complex assembly; ISS:AgBase.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:AgBase.
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:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   CDD; cd01874; Cdc42; 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   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q90694.
DR   SWISS-2DPAGE; Q90694.
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   NP_BIND         10..17
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         57..61
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         115..118
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
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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