ID CDC42_MACFA Reviewed; 191 AA.
AC Q4R4R6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Cell division control protein 42 homolog;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953};
DE Flags: Precursor;
GN Name=CDC42; ORFNames=QflA-13723;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. In
CC neurons, plays a role in the extension and maintenance of the formation
CC of filopodia, thin and actin-rich surface projections (By similarity).
CC Required for DOCK10-mediated spine formation in Purkinje cells and
CC hippocampal neurons. Facilitates filopodia formation upon DOCK11-
CC activation (By similarity). Upon activation by CaMKII, modulates
CC dendritic spine structural plasticity by relaying CaMKII transient
CC activation to synapse-specific, long-term signaling (By similarity).
CC Also plays a role in phagocytosis through organization of the F-actin
CC cytoskeleton associated with forming phagocytic cups (By similarity).
CC {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953,
CC ECO:0000250|UniProtKB:Q8CFN2}.
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 -!- 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 activates
CC CDC42 by exchanging GDP for GTP. Interacts with DOCK8 (via DHR-2
CC domain); the interaction activates CDC42 by exchanging GDP for GTP.
CC Interacts with IQGAP1. Interacts with NET1 and ARHGAP33/TCGAP. Part of
CC a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. The GTP-
CC bound form interacts with CCPG1. Interacts with USP6. Interacts with
CC NEK6. Part of a collagen stimulated complex involved in cell migration
CC composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with
CC ITGB1BP1. Interacts with ARHGDIA; this interaction inactivates and
CC stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the
CC inactive, GDP-bound form. Interacts in (GTP-bound form) with FNBP1L and
CC ABI1, but only in the presence of FNBP1L. Interacts with MARCKS (By
CC similarity). {ECO:0000250|UniProtKB:P60766,
CC ECO:0000250|UniProtKB:P60953}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P60766};
CC Lipid-anchor {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P60766}. Midbody {ECO:0000250|UniProtKB:P60953}.
CC Cytoplasm, cytoskeleton, 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 membrane
CC {ECO:0000250|UniProtKB:P60766}; Peripheral membrane protein
CC {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 progressed
CC through anaphase to telophase. Localizes at the end of cytokinesis in
CC the intercellular bridge formed between two daughter cells. Its
CC localization is regulated by the activities of guanine nucleotide
CC exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes
CC with NEK6 in the centrosome. In its active GTP-bound form localizes to
CC the leading edge membrane of migrating dendritic cells.
CC {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953}.
CC -!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates
CC the binding of the Rho-GDP dissociation inhibitor RhoGDI.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; AB169828; BAE01909.1; -; mRNA.
DR RefSeq; NP_001270330.1; NM_001283401.1.
DR AlphaFoldDB; Q4R4R6; -.
DR SMR; Q4R4R6; -.
DR STRING; 9541.ENSMFAP00000018965; -.
DR eggNOG; KOG0393; Eukaryota.
DR OrthoDB; 20499at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProt.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24072:SF192; CELL DIVISION CONTROL PROTEIN 42 HOMOLOG; 1.
DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cell division control protein 42 homolog"
FT /id="PRO_0000270825"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000270826"
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 64
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P60953"
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; 21258 MW; BF4079A26AE78FF5 CRC64;
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFNNY AVTVMIGGEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
EPKKSRRCVL L
//
