GYP3_YEAST
ID GYP3_YEAST Reviewed; 633 AA.
AC P48566; D6W0Q0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=GTPase-activating protein GYP3;
DE AltName: Full=Multicopy suppressor of bud emergence 3;
DE AltName: Full=Protein MSB3;
GN Name=MSB3; Synonyms=GYP3; OrderedLocusNames=YNL293W; ORFNames=N0470;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10679030; DOI=10.1091/mbc.11.2.773;
RA Bi E., Chiavetta J.B., Chen H., Chen G.-C., Chan C.S.M., Pringle J.R.;
RT "Identification of novel, evolutionarily conserved Cdc42p-interacting
RT proteins and of redundant pathways linking Cdc24p and Cdc42p to actin
RT polarization in yeast.";
RL Mol. Biol. Cell 11:773-793(2000).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ARG-282.
RX PubMed=12913108; DOI=10.1083/jcb.200302038;
RA Gao X.D., Albert S., Tcheperegine S.E., Burd C.G., Gallwitz D., Bi E.;
RT "The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required
RT for efficient exocytosis and actin organization.";
RL J. Cell Biol. 162:635-646(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Regulates exocytosis by functioning as a GAP for SEC4.
CC Stimulates specifically the GTPase activity of YPT6. Also required for
CC efficient polarization of the actin patches.
CC {ECO:0000269|PubMed:10679030, ECO:0000269|PubMed:12913108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10679030}. Bud
CC {ECO:0000269|PubMed:10679030}. Bud neck {ECO:0000269|PubMed:10679030}.
CC Note=Localizes to the presumptive bud site, the bud tip and the mother-
CC bud neck.
CC -!- MISCELLANEOUS: Present with 178 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U23084; AAC49106.1; -; Genomic_DNA.
DR EMBL; Z71569; CAA96211.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10266.1; -; Genomic_DNA.
DR PIR; S60408; S60408.
DR RefSeq; NP_014106.1; NM_001183131.1.
DR AlphaFoldDB; P48566; -.
DR SMR; P48566; -.
DR BioGRID; 35544; 112.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-2783N; -.
DR IntAct; P48566; 7.
DR MINT; P48566; -.
DR STRING; 4932.YNL293W; -.
DR CarbonylDB; P48566; -.
DR iPTMnet; P48566; -.
DR MaxQB; P48566; -.
DR PaxDb; P48566; -.
DR PRIDE; P48566; -.
DR EnsemblFungi; YNL293W_mRNA; YNL293W; YNL293W.
DR GeneID; 855423; -.
DR KEGG; sce:YNL293W; -.
DR SGD; S000005237; MSB3.
DR VEuPathDB; FungiDB:YNL293W; -.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000176552; -.
DR HOGENOM; CLU_005350_12_2_1; -.
DR InParanoid; P48566; -.
DR OMA; GVHWNNS; -.
DR BioCyc; YEAST:G3O-33282-MON; -.
DR PRO; PR:P48566; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48566; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IC:ComplexPortal.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IGI:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..633
FT /note="GTPase-activating protein GYP3"
FT /id="PRO_0000208012"
FT DOMAIN 223..456
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 26..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 282
FT /note="R->F,K: Reduced GAP activity."
FT /evidence="ECO:0000269|PubMed:12913108"
SQ SEQUENCE 633 AA; 72999 MW; 5F62607B95BBAFB9 CRC64;
MQNDQQRFSL QNRTVLAHPY KRLGGAFTVK SPSVPNFHDK MHSDHSSSDS ALVNGSFRAN
DHRSVEPSCL GQASPSEHDG NLSVIDLYGD EVESQRAEGE DDDDNNGDNG NEDLEEVHSD
DLDLVPDDDN RQRVELEGAA SATSANSNGI NNTHFDRYGF KKQNNYISEA EYDKWWVEYS
QYCVRRKHKW QLLLEKSGLP VTDDSPSRFP SKSERLKRYV RKGIPAEWRG NAWWHFARGQ
EKLNKNKGVY SQLLRKMKQI KKQNPNEKQV QDLDIIERDL NRTFPDNIHF QSSLHNKEGP
PIIKSLRRVL VAFSLYNPKI GYCQSMNFLA GLLLLFLDEE RAFWMLVIIT SRYLPGVHNI
NLEGVNIDQG VLMLCVKEYI PEVWSYIKPS IDHHQKNNKT FSPSNKKVLF NMQKNEFLYR
LPPITLCTAS WFMSCFVGVV PIETTLRIWD CLFYEESHFL FKVSLAVLKL SEHDLSKIKP
RNNSLNYSWG SNLNQRGGSM GQEDSDMEIF QVIQTFPKTL LNPNEIFEKI IFKRRFNLNR
LDQDEIDRCR KFVAAQRLKF KTYGELLGNS TSEADLPIND NTDNKGIHIT SDAVNEALSS
EVYGFKKSLA GVHWNNSIKE KVKQMRKKKD KGD
