CDC42_SCHPO
ID CDC42_SCHPO Reviewed; 192 AA.
AC Q01112;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Cell division control protein 42 homolog;
DE AltName: Full=CDC42Sp;
DE Flags: Precursor;
GN Name=cdc42; ORFNames=SPAC110.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1587480; DOI=10.1016/0378-1119(92)90724-4;
RA Fawell E., Bowden S., Armstrong J.;
RT "A homologue of the ras-related CDC42 gene from Schizosaccharomyces
RT pombe.";
RL Gene 114:153-154(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ED665;
RX PubMed=8289788; DOI=10.1128/mcb.14.2.1075-1083.1994;
RA Miller P.J., Johnson D.I.;
RT "Cdc42p GTPase is involved in controlling polarized cell growth in
RT Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 14:1075-1083(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP INTERACTION WITH GEF1.
RX PubMed=12529446; DOI=10.1091/mbc.e02-07-0400;
RA Coll P.M., Trillo Y., Ametzazurra A., Perez P.;
RT "Gef1p, a new guanine nucleotide exchange factor for Cdc42p, regulates
RT polarity in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 14:313-323(2003).
RN [5]
RP INTERACTION WITH SCD1.
RX PubMed=12972551; DOI=10.1091/mbc.e02-10-0665;
RA Hirota K., Tanaka K., Ohta K., Yamamoto M.;
RT "Gef1p and Scd1p, the Two GDP-GTP exchange factors for Cdc42p, form a ring
RT structure that shrinks during cytokinesis in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 14:3617-3627(2003).
CC -!- FUNCTION: Involved in development of cell polarity during the cell
CC division cycle.
CC -!- SUBUNIT: Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act
CC cooperatively to form a protein complex. Interacts with gef1 and scd1.
CC {ECO:0000269|PubMed:12529446, ECO:0000269|PubMed:12972551}.
CC -!- INTERACTION:
CC Q01112; Q09763: gef1; NbExp=7; IntAct=EBI-767502, EBI-1556299;
CC Q01112; Q9UUM7: hob3; NbExp=2; IntAct=EBI-767502, EBI-1556284;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; M83650; AAA35298.1; -; mRNA.
DR EMBL; L25677; AAA16472.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC08561.1; -; Genomic_DNA.
DR PIR; A55924; A55924.
DR RefSeq; NP_593536.1; NM_001018970.2.
DR AlphaFoldDB; Q01112; -.
DR SMR; Q01112; -.
DR BioGRID; 279463; 44.
DR DIP; DIP-275N; -.
DR IntAct; Q01112; 3.
DR MINT; Q01112; -.
DR STRING; 4896.SPAC110.03.1; -.
DR MaxQB; Q01112; -.
DR PaxDb; Q01112; -.
DR PRIDE; Q01112; -.
DR EnsemblFungi; SPAC110.03.1; SPAC110.03.1:pep; SPAC110.03.
DR GeneID; 2543027; -.
DR KEGG; spo:SPAC110.03; -.
DR PomBase; SPAC110.03; cdc42.
DR VEuPathDB; FungiDB:SPAC110.03; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q01112; -.
DR OMA; ITHHQQK; -.
DR PhylomeDB; Q01112; -.
DR Reactome; R-SPO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SPO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-SPO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SPO-5627123; RHO GTPases activate PAKs.
DR Reactome; R-SPO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SPO-9013148; CDC42 GTPase cycle.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q01112; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071521; C:Cdc42 GTPase complex; IPI:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:PomBase.
DR GO; GO:0012505; C:endomembrane system; IDA:PomBase.
DR GO; GO:0070382; C:exocytic vesicle; IDA:PomBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; EXP:PomBase.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0042815; P:bipolar cell growth; EXP:PomBase.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0101026; P:mitotic nuclear membrane biogenesis; ISO:PomBase.
DR GO; GO:1902917; P:positive regulation of mating projection assembly; IMP:PomBase.
DR GO; GO:0032951; P:regulation of beta-glucan biosynthetic process; IGI:PomBase.
DR GO; GO:0032955; P:regulation of division septum assembly; IMP:PomBase.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:PomBase.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:PomBase.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:PomBase.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:PomBase.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Cell division control protein 42 homolog"
FT /id="PRO_0000198954"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281284"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000250"
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 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 192 AA; 21330 MW; EDBC8DA3F3E89301 CRC64;
MPTIKCVVVG DGAVGKTCLL ISYTTNKFPS DYVPTVFDNY AVTVMIGDEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVTSPASF ENVKEKWFPE VHHHCPGVPC LIVGTQIDLR
DDPSVQQKLA RQHQHPLTHE QGERLARELG AVKYVECSAL TQKGLKNVFD EAIVAALDPP
VPHKKKSKCL VL
