(data stored in ACNUC8465 zone)

SWISSPROT: CDC42_CANLF

ID   CDC42_CANLF             Reviewed;         191 AA.
AC   P60952; P21181; P25763;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   08-MAY-2019, entry version 145.
DE   RecName: Full=Cell division control protein 42 homolog;
DE   AltName: Full=G25K GTP-binding protein;
DE   Flags: Precursor;
GN   Name=CDC42;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RA   Dutartre H., Davoust J., Gorvel J., Chavrier P.;
RT   "Cytokinesis arrest and redistribution of actin-cytoskeleton
RT   regulatory components induced by the Rho GTPase CDC42Hs.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and an inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses. Involved in epithelial cell polarization
CC       processes. Regulates the bipolar attachment of spindle
CC       microtubules to kinetochores before chromosome congression in
CC       metaphase. Plays a role in the extension and maintenance of the
CC       formation of thin, actin-rich surface projections called
CC       filopodia. Mediates CDC42-dependent cell migration. Required for
CC       DOCK10-mediated spine formation in Purkinje cells and hippocampal
CC       neurons. Facilitates filopodia formation upon DOCK11-activation.
CC       Also plays a role in phagocytosis through organization of the F-
CC       actin cytoskeleton associated with forming phagocytic cups.
CC       {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953}.
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC       {ECO:0000250|UniProtKB:P60766}.
CC   -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CC       CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
CC       dependent manner). Interacts with activated CSPG4 and with BAIAP2.
CC       Interacts with DOCK11/Zizimin2; the interaction activates CDC42 by
CC       exchanging GDP for GTP. Interacts with DOCK9; the interaction
CC       activates CDC42 by exchanging GDP for GTP. Interacts with DOCK8
CC       (via DHR-2 domain); the interaction activates CDC42 by exchanging
CC       GDP for GTP. Interacts with IQGAP1. Interacts with NET1 and
CC       ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and
CC       PRKCI or PRKCZ. The GTP-bound form interacts with CCPG1. Interacts
CC       with USP6. Interacts with NEK6. Part of a collagen stimulated
CC       complex involved in cell migration composed of CDC42, CRK, TNK2
CC       and BCAR1/p130cas. Interacts with ITGB1BP1. Interacts with
CC       ARHGDIA; this interaction inactivates and stabilizes CDC42.
CC       Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-
CC       bound form. Interacts in (GTP-bound form) with FNBP1L and ABI1,
CC       but only in the presence of FNBP1L. {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000250|UniProtKB:P60953}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P60766}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P60766}. Midbody
CC       {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P60953}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P60766}. Cell projection, lamellipodium
CC       membrane {ECO:0000250|UniProtKB:P60766}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P60766}. Note=Localizes to spindle during
CC       prometaphase cells. Moves to the central spindle as cells
CC       progressed through anaphase to telophase. Localizes at the end of
CC       cytokinesis in the intercellular bridge formed between two
CC       daughter cells. Its localization is regulated by the activities of
CC       guanine nucleotide exchange factor ECT2 and GTPase activating
CC       protein RACGAP1. Colocalizes with NEK6 in the centrosome. In its
CC       active GTP-bound form localizes to the leading edge membrane of
CC       migrating dendritic cells. {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000250|UniProtKB:P60953}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Placental;
CC         IsoId=P60952-2, P21181-4;
CC         Sequence=Displayed;
CC       Name=2; Synonyms=Brain;
CC         IsoId=P60952-1, P21181-1;
CC         Sequence=VSP_010078, VSP_010079;
CC   -!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this
CC       stimulates the binding of the Rho-GDP dissociation inhibitor
CC       RhoGDI. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       CDC42 subfamily. {ECO:0000305}.
DR   EMBL; Z49944; CAA90215.1; -; mRNA.
DR   PIR; S57563; S57563.
DR   RefSeq; NP_001003254.1; NM_001003254.2. [P60952-2]
DR   SMR; P60952; -.
DR   CORUM; P60952; -.
DR   STRING; 9612.ENSCAFP00000021683; -.
DR   PaxDb; P60952; -.
DR   PRIDE; P60952; -.
DR   Ensembl; ENSCAFT00000023350; ENSCAFP00000021683; ENSCAFG00000014707. [P60952-2]
DR   Ensembl; ENSCAFT00000023351; ENSCAFP00000021684; ENSCAFG00000014707. [P60952-1]
DR   GeneID; 403934; -.
DR   KEGG; cfa:403934; -.
DR   CTD; 998; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00940000153675; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; P60952; -.
DR   KO; K04393; -.
DR   OMA; HEQGERL; -.
DR   OrthoDB; 1091615at2759; -.
DR   TreeFam; TF101109; -.
DR   Reactome; R-CFA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-CFA-182971; EGFR downregulation.
DR   Reactome; R-CFA-194840; Rho GTPase cycle.
DR   Reactome; R-CFA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-CFA-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-CFA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-CFA-418885; DCC mediated attractive signaling.
DR   Reactome; R-CFA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CFA-525793; Myogenesis.
DR   Reactome; R-CFA-5625970; RHO GTPases activate KTN1.
DR   Reactome; R-CFA-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-CFA-5627123; RHO GTPases activate PAKs.
DR   Reactome; R-CFA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-CFA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-CFA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-CFA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-CFA-983231; Factors involved in megakaryocyte development and platelet production.
DR   Proteomes; UP000002254; Chromosome 2.
DR   Bgee; ENSCAFG00000014707; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
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:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR   GO; GO:0000322; C:storage vacuole; 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; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
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: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:0034613; P:cellular protein localization; IEA:Ensembl.
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: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; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR   GO; GO:0048664; P:neuron fate determination; IEA:Ensembl.
DR   GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
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:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR   GO; GO:0043497; P:regulation of protein heterodimerization activity; IEA:Ensembl.
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; P60952.
DR   SWISS-2DPAGE; P60952.
KW   Alternative splicing; Cell membrane; Cell projection;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT   CHAIN         1    188       Cell division control protein 42 homolog.
FT                                /FTId=PRO_0000030423.
FT   PROPEP      189    191       Removed in mature form.
FT                                /FTId=PRO_0000030424.
FT   NP_BIND      10     17       GTP. {ECO:0000250}.
FT   NP_BIND      57     61       GTP. {ECO:0000250}.
FT   NP_BIND     115    118       GTP. {ECO:0000250}.
FT   MOTIF        32     40       Effector region. {ECO:0000255}.
FT   MOD_RES      64     64       Phosphotyrosine; by SRC.
FT                                {ECO:0000250|UniProtKB:P60953}.
FT   MOD_RES     188    188       Cysteine methyl ester. {ECO:0000250}.
FT   LIPID       188    188       S-geranylgeranyl cysteine. {ECO:0000250}.
FT   VAR_SEQ     163    163       K -> R (in isoform 2).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_010078.
FT   VAR_SEQ     182    191       PKKSRRCVLL -> TQPKRKCCIF (in isoform 2).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_010079.
SQ   SEQUENCE   191 AA;  21259 MW;  51A437E22A4D8FFF CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
     DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPKKSRRCVL L
//

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