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Database: UniProt
Entry: Q7YT81_CIOIN
LinkDB: Q7YT81_CIOIN
Original site: Q7YT81_CIOIN 
ID   Q7YT81_CIOIN            Unreviewed;       191 AA.
AC   Q7YT81; A0A1W2VN78;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Cell division control protein 42 homolog {ECO:0000256|ARBA:ARBA00016061, ECO:0000256|RuleBase:RU367141};
DE            EC=3.6.5.2 {ECO:0000256|RuleBase:RU367141};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:CAD48472.1};
RN   [1] {ECO:0000313|EMBL:CAD48472.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed tissue {ECO:0000313|EMBL:CAD48472.1};
RA   Fort P.P.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD48472.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed tissue {ECO:0000313|EMBL:CAD48472.1};
RX   PubMed=12941527; DOI=10.1016/S0248-4900(03)00052-2;
RA   Philips A., Blein M., Robert A., Chambon J.P., Baghdiguian S., Weill M.,
RA   Fort P.;
RT   "Ascidians as a vertebrate-like model organism for physiological studies of
RT   Rho GTPase signaling.";
RL   Biol. Cell 95:295-302(2003).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC       an active GTP-bound and an inactive GDP-bound state.
CC       {ECO:0000256|RuleBase:RU367141}.
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:0000256|RuleBase:RU367141};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367141};
CC       Lipid-anchor {ECO:0000256|RuleBase:RU367141}. Midbody
CC       {ECO:0000256|ARBA:ARBA00004214}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC       subfamily. {ECO:0000256|ARBA:ARBA00008112,
CC       ECO:0000256|RuleBase:RU367141}.
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DR   EMBL; AJ508665; CAD48472.1; -; mRNA.
DR   RefSeq; NP_001027691.1; NM_001032519.1.
DR   AlphaFoldDB; Q7YT81; -.
DR   GeneID; 445701; -.
DR   KEGG; cin:445701; -.
DR   CTD; 998; -.
DR   OrthoDB; 20499at2759; -.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProt.
DR   GO; GO:0051130; P:positive regulation of cellular component organization; IEA:UniProt.
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; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367141};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU367141};
KW   Hydrolase {ECO:0000313|EMBL:CAD48472.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU367141};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367141};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367141};
KW   Prenylation {ECO:0000256|ARBA:ARBA00023289, ECO:0000256|RuleBase:RU367141}.
SQ   SEQUENCE   191 AA;  21409 MW;  14A4A34CDEA32D9B CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPQ EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSY ENIKEKWVPE ITHHCPKTPF LLVGTQVDLR
     DDAATIEKLS KNKQKAITQD MGDKLARELK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPKRRRRCQV L
//
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