(data stored in ACNUC8465 zone)

SWISSPROT: CDC42_ANOGA

ID   CDC42_ANOGA             Reviewed;         191 AA.
AC   Q17031; Q7PQZ1; Q93110;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAY-2019, entry version 126.
DE   RecName: Full=Cdc42 homolog;
DE   AltName: Full=25 kDa GTP-binding protein;
DE   Flags: Precursor;
GN   Name=Cdc42; ORFNames=AGAP002440;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B.,
RA   Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P.,
RA   Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V.,
RA   Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S.,
RA   Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M.,
RA   Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I.,
RA   Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z.,
RA   Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R.,
RA   Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E.,
RA   Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F.,
RA   Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R.,
RA   Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C.,
RA   Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V.,
RA   Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D.,
RA   Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H.,
RA   Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A.,
RA   Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F.,
RA   Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S.,
RA   Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C.,
RA   Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-191, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=G3; TISSUE=Midgut;
RX   PubMed=8917545; DOI=10.1073/pnas.93.23.13066;
RA   Dimopoulos G.M., Richman A.M., della Torre A., Kafatos F.C., Louis C.;
RT   "Identification and characterization of differentially expressed cDNAs
RT   of the vector mosquito, Anopheles gambiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13066-13071(1996).
CC   -!- FUNCTION: Regulates mbt kinase activity and is also required to
CC       recruit mbt to adherens junctions. Together with mbt, regulates
CC       photoreceptor cell morphogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the adult unfed gut,
CC       expression drops after feeding. {ECO:0000269|PubMed:8917545}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development with highest
CC       levels in early embryo and pupae and lowest levels in late pupae
CC       and adults. {ECO:0000269|PubMed:8917545}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       CDC42 subfamily. {ECO:0000305}.
DR   EMBL; AAAB01008859; EAA08093.4; -; Genomic_DNA.
DR   EMBL; Z69980; CAA93820.1; -; mRNA.
DR   RefSeq; XP_003436126.1; XM_003436078.1.
DR   RefSeq; XP_003436127.1; XM_003436079.1.
DR   RefSeq; XP_312505.3; XM_312505.5.
DR   SMR; Q17031; -.
DR   STRING; 7165.AGAP002440-PC; -.
DR   PaxDb; Q17031; -.
DR   PRIDE; Q17031; -.
DR   EnsemblMetazoa; AGAP002440-RA; AGAP002440-PA; AGAP002440.
DR   EnsemblMetazoa; AGAP002440-RB; AGAP002440-PB; AGAP002440.
DR   EnsemblMetazoa; AGAP002440-RC; AGAP002440-PC; AGAP002440.
DR   GeneID; 1273521; -.
DR   KEGG; aga:AgaP_AGAP002440; -.
DR   VectorBase; AGAP002440-RA; AGAP002440-PA; AGAP002440.
DR   VectorBase; AGAP002440-RB; AGAP002440-PB; AGAP002440.
DR   VectorBase; AGAP002440-RC; AGAP002440-PC; AGAP002440.
DR   CTD; 1273521; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; Q17031; -.
DR   KO; K04393; -.
DR   OMA; HEQGERL; -.
DR   OrthoDB; 1091615at2759; -.
DR   PhylomeDB; Q17031; -.
DR   Proteomes; UP000007062; Chromosome 2R.
DR   Proteomes; UP000007062; Unassembled WGS sequence.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
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; Q17031.
DR   SWISS-2DPAGE; Q17031.
KW   Cell junction; Cell membrane; Complete proteome;
KW   Developmental protein; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN         1    188       Cdc42 homolog.
FT                                /FTId=PRO_0000198957.
FT   PROPEP      189    191       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000281287.
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     188    188       Cysteine methyl ester. {ECO:0000250}.
FT   LIPID       188    188       S-geranylgeranyl cysteine. {ECO:0000250}.
FT   CONFLICT     58     58       T -> S (in Ref. 2; CAA93820).
FT                                {ECO:0000305}.
FT   CONFLICT    171    171       E -> V (in Ref. 2; CAA93820).
FT                                {ECO:0000305}.
SQ   SEQUENCE   191 AA;  21413 MW;  4BB97244AC0E3B8F CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCQKTPF LLVGTQIDLR
     DENSTLEKLA KNKQKPITLE QGEKLAKELK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPTKKRKCRF L
//

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