GYP5_YEAST
ID GYP5_YEAST Reviewed; 894 AA.
AC Q12344; D6W3C2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=GTPase-activating protein GYP5;
GN Name=GYP5; OrderedLocusNames=YPL249C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP FUNCTION.
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-496.
RX PubMed=12189143; DOI=10.1074/jbc.m205783200;
RA De Antoni A., Schmitzova J., Trepte H.-H., Gallwitz D., Albert S.;
RT "Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to
RT Golgi transport revealed by the analysis of two novel Ypt1-GAPs.";
RL J. Biol. Chem. 277:41023-41031(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH GYL1, AND
RP IDENTIFICATION IN SEC4-CONTAINING COMPLEXES.
RX PubMed=15331637; DOI=10.1242/jcs.01349;
RA Chesneau L., Dupre S., Burdina A., Roger J., Le Panse S., Jacquet M.,
RA Cuif M.-H.;
RT "Gyp5p and Gyl1p are involved in the control of polarized exocytosis in
RT budding yeast.";
RL J. Cell Sci. 117:4757-4767(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH GYL1 AND RVS167.
RX PubMed=15802519; DOI=10.1534/genetics.104.040063;
RA Friesen H., Colwill K., Robertson K., Schub O., Andrews B.;
RT "Interaction of the Saccharomyces cerevisiae cortical actin patch protein
RT Rvs167p with proteins involved in ER to Golgi vesicle trafficking.";
RL Genetics 170:555-568(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-389, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND THR-89, 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: GTPase-activating protein which accelerates the GTP
CC hydrolysis rate of YPT1 and SEC4. Involved in ER to Golgi trafficking
CC and polarized exocytosis. {ECO:0000269|PubMed:10679030,
CC ECO:0000269|PubMed:12189143, ECO:0000269|PubMed:15331637,
CC ECO:0000269|PubMed:15802519}.
CC -!- SUBUNIT: Interacts with GYL1 and RVS167; and is part of SEC4-containing
CC complexes. {ECO:0000269|PubMed:15331637, ECO:0000269|PubMed:15802519}.
CC -!- INTERACTION:
CC Q12344; P43603: LSB3; NbExp=3; IntAct=EBI-38508, EBI-22980;
CC Q12344; P39743: RVS167; NbExp=6; IntAct=EBI-38508, EBI-14500;
CC Q12344; P32793: YSC84; NbExp=2; IntAct=EBI-38508, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Bud neck.
CC -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GYP5 family. {ECO:0000305}.
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DR EMBL; Z73605; CAA97970.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91595.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11188.1; -; Genomic_DNA.
DR PIR; S61015; S61015.
DR RefSeq; NP_015075.1; NM_001184063.1.
DR AlphaFoldDB; Q12344; -.
DR SMR; Q12344; -.
DR BioGRID; 35914; 91.
DR DIP; DIP-8946N; -.
DR IntAct; Q12344; 7.
DR MINT; Q12344; -.
DR STRING; 4932.YPL249C; -.
DR iPTMnet; Q12344; -.
DR MaxQB; Q12344; -.
DR PaxDb; Q12344; -.
DR PRIDE; Q12344; -.
DR EnsemblFungi; YPL249C_mRNA; YPL249C; YPL249C.
DR GeneID; 855827; -.
DR KEGG; sce:YPL249C; -.
DR SGD; S000006170; GYP5.
DR VEuPathDB; FungiDB:YPL249C; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000168693; -.
DR HOGENOM; CLU_005350_11_0_1; -.
DR InParanoid; Q12344; -.
DR OMA; LFVHDAM; -.
DR BioCyc; YEAST:G3O-34135-MON; -.
DR Reactome; R-SCE-8854214; TBC/RABGAPs.
DR PRO; PR:Q12344; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12344; protein.
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:0005798; C:Golgi-associated vesicle; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IMP:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; ER-Golgi transport; Exocytosis; GTPase activation;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..894
FT /note="GTPase-activating protein GYP5"
FT /id="PRO_0000240365"
FT DOMAIN 451..630
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 732..872
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 496
FT /note="R->A,K: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:12189143"
SQ SEQUENCE 894 AA; 101800 MW; 67BAAC39B2A51859 CRC64;
MSSDKSIEKN TDTIASEVHE GDNHSNNLGS MEEEIKSTPS DQYEEIAIIP TEPLHSDKEL
NDKQQSLGHE APTNVSREEP IGISGDEDTQ ITEQNVNEQR QETREPSSEI DLNEPLDVEK
DVTTDVQAPN GLNIEKEYDA VKENEKVYAD TKEVVSSPEN REVTGKNSGG EKSSSSKFLD
DESGTTTAAN ANDISISSEV TPERSSENDN NQIHITNEVA AGINLNENKE QKAAIEDGPV
TAENLSSETA RKVPPIPTQI INEKGDNSSE NEVSAIPTTS SPPLPPRQNV ATSTSPKLPP
RGKQREQPPK TKNAVPPPLE EEMKSEKFRK NFEETKRNSY HHVPLTGSKT AQLESTAEIN
LIASRYRKTS HHLNKEGEET RESLQEGQSF LKSTFTSFLE NLSEYNEVEN VNEEDREMFK
IDWSFWTQVV NDYATVASNE PENLEAHVTN GIPPQIRGII WQLMANSKSR EMEDIYETLL
DTECLHEATI RRDLRRTKFV AEDKMESLYK VIKVYSVYDP DVGYTQGMGF IAAPLLINCE
NEAESFGLLV GLMKNYGLRE LFLPGMPGLM LMLYQFDRLL EEHSPSLYNR LIREGISSTM
YATQWFLTFF AYKFPLEFVL RIFDIVFVEG IEVLLKFAVN LMLKNEETLV KLRFDELLDF
LKDELFNYYL MGNQDDASVV QMGLSNGNSF KGNDDGTFSY NVDLFVHDAM TGVYITPLTL
RRYRGEYVEI HEKEQKKEDH YESLRIQNHQ LQREAQKLEH DYSILNKENI SAANELIQNR
LNMEMLLDEK NDLINTITDI KSQIEEEIRK QNLPNPDASL PKADLREDLE RTISRNNEVM
RENGQLEERI TELQAEIDEL ININKEQVST ASLLERDSKA KGRKGWTGFK KVFK
