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 03-AUG-2022, entry version 137.
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC 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., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., 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., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA 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 DEVELOPMENTAL
RP 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 of
RT 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 recruit
CC mbt to adherens junctions. Together with mbt, regulates photoreceptor
CC cell morphogenesis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the adult unfed gut, expression
CC 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 and
CC adults. {ECO:0000269|PubMed:8917545}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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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 AlphaFoldDB; Q17031; -.
DR SMR; Q17031; -.
DR STRING; 7165.AGAP002440-PC; -.
DR PaxDb; Q17031; -.
DR GeneID; 1273521; -.
DR KEGG; aga:AgaP_AGAP002440; -.
DR CTD; 1273521; -.
DR VEuPathDB; VectorBase:AGAP002440; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q17031; -.
DR OMA; ITHHQQK; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q17031; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; 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:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; 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:0035099; P:hemocyte migration; IEA:UniProt.
DR GO; GO:0035006; P:melanization defense response; IEA:UniProt.
DR GO; GO:0030707; P:ovarian follicle cell development; IEA:UniProt.
DR GO; GO:0051130; P:positive regulation of cellular component organization; IEA:UniProt.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Developmental protein; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Cdc42 homolog"
FT /id="PRO_0000198957"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281287"
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 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="T -> S (in Ref. 2; CAA93820)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> V (in Ref. 2; CAA93820)"
FT /evidence="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
