GYP7_YEAST
ID GYP7_YEAST Reviewed; 746 AA.
AC P48365; D6VRC2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=GTPase-activating protein GYP7;
DE AltName: Full=GAP for YPT7;
GN Name=GYP7; OrderedLocusNames=YDL234C;
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], AND FUNCTION.
RC STRAIN=AG430;
RX PubMed=10091609; DOI=10.1046/j.1432-1327.1999.00192.x;
RA Vollmer P., Will E., Scheglmann D., Strom M., Gallwitz D.;
RT "Primary structure and biochemical characterization of yeast GTPase-
RT activating proteins with substrate preference for the transport GTPase
RT Ypt7p.";
RL Eur. J. Biochem. 260:284-290(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 MUTAGENESIS OF ARG-458.
RX PubMed=10508155; DOI=10.1093/emboj/18.19.5216;
RA Albert S., Will E., Gallwitz D.;
RT "Identification of the catalytic domains and their functionally critical
RT arginine residues of two yeast GTPase-activating proteins specific for
RT Ypt/Rab transport GTPases.";
RL EMBO J. 18:5216-5225(1999).
RN [5]
RP FUNCTION.
RX PubMed=11210571; DOI=10.1016/s0076-6879(01)29065-x;
RA Will E., Albert S., Gallwitz D.;
RT "Expression, purification, and biochemical properties of Ypt/Rab GTPase-
RT activating proteins of Gyp family.";
RL Methods Enzymol. 329:50-58(2001).
RN [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-339, 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 (GAP) that most effectively
CC accelerates the intrinsic GTPase activity of Ypt/Rab-type GTPase YPT7
CC involved in vacuole docking and fusion (PubMed:10091609,
CC PubMed:11210571). It is also active, but to a lesser extent, on YPT31,
CC YPT32, YPT1, YPT6 and SEC4 (PubMed:10091609, PubMed:11210571). Provides
CC a catalytic arginine (arginine finger) in trans to accelerate the GTP
CC hydrolysis rate of the substrate GTPase (Probable).
CC {ECO:0000269|PubMed:10091609, ECO:0000269|PubMed:11210571,
CC ECO:0000305|PubMed:10508155}.
CC -!- INTERACTION:
CC P48365; P0CG63: UBI4; NbExp=2; IntAct=EBI-8018, EBI-7000452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X79552; CAA56095.1; -; Genomic_DNA.
DR EMBL; Z74281; CAA98813.1; -; Genomic_DNA.
DR EMBL; Z74282; CAA98814.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11632.1; -; Genomic_DNA.
DR PIR; S61057; S61057.
DR RefSeq; NP_010047.1; NM_001180294.1.
DR AlphaFoldDB; P48365; -.
DR SMR; P48365; -.
DR BioGRID; 31877; 66.
DR DIP; DIP-6769N; -.
DR IntAct; P48365; 7.
DR MINT; P48365; -.
DR STRING; 4932.YDL234C; -.
DR iPTMnet; P48365; -.
DR MaxQB; P48365; -.
DR PaxDb; P48365; -.
DR PRIDE; P48365; -.
DR EnsemblFungi; YDL234C_mRNA; YDL234C; YDL234C.
DR GeneID; 851364; -.
DR KEGG; sce:YDL234C; -.
DR SGD; S000002393; GYP7.
DR VEuPathDB; FungiDB:YDL234C; -.
DR eggNOG; KOG2197; Eukaryota.
DR GeneTree; ENSGT00940000169893; -.
DR HOGENOM; CLU_004457_0_1_1; -.
DR InParanoid; P48365; -.
DR OMA; ERNQRIW; -.
DR BioCyc; YEAST:G3O-29612-MON; -.
DR Reactome; R-SCE-8854214; TBC/RABGAPs.
DR PRO; PR:P48365; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P48365; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA: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 Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..746
FT /note="GTPase-activating protein GYP7"
FT /id="PRO_0000208017"
FT DOMAIN 385..633
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 470..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 458
FT /note="Arginine finger"
FT /evidence="ECO:0000305|PubMed:10508155"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 458
FT /note="R->A,K: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:10508155"
SQ SEQUENCE 746 AA; 87306 MW; 10F0F2B11A9993A6 CRC64;
MSKILFCKSK VFLHPTSDAR DNIAGFLLLT LEANKLSHQA ILQYIPESGL STLEISKLLK
HEAKVGTCPT STPFVIENSI NFSNLVNTSL GQAFEISLSQ IYCIQFRPPS PNGWYVGSLV
IYPLTEQFTG FQPPVLFFHD QLCPSTTDKL KRLRKSMNPF DDSDELYWGG VDLRNKINEL
MELKKSNLEP EFWLVNPSLN DLRNFVSKDL LESYNNSKKD TTELATAGVK LNEKFQEWKW
NVMSKIADVT TKSTNFIDSW LTNNSPIQKS QIDNEYLQKL LNNEKVKQIE QDYDSARVYL
ANWSLGVKQE AERYQKQNKL FDSYRNNIFN DLNLTDELSD TEINNALQRQ FPLTEAKWNS
LWDENDGRLR VTVNEVKDFI FHGGLENDSL RGKVWGFLLE IYPWDSSQDE RVQIDQTLAA
EYDQLKLTWS KDFLQFDDED EEEYWNDQLF RISKDVRRCD RNLEIFQYNT IDGLPPPPQQ
LPANENNSTS PESANDESDD ADDGVRNPHL IHLQNILITY NVYNTNLGYV QGMTDLLSPI
YVIMKEEWKT FWCFTHFMDI MERNFLRDQS GIHEQMLTLV ELVQLMLPEL SEHLNKCDSG
NLFFCFRMLL VWFKREFEME DIMHIWENFW TFYYSSQFQL FFMLAILQKN SQAILQHLNQ
FDQILKFFNE LNGKLDWNDL MVRAELLFKK FEKMMHVMER DLQNVSSSSS SSSTGVLPCQ
SERLTLLLSK KPIIRHEGQR SKNSVK
