GYP1_YEAST
ID GYP1_YEAST Reviewed; 637 AA.
AC Q08484; D6W2D3; O00028;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=GTPase-activating protein GYP1;
DE AltName: Full=GAP for YPT1;
GN Name=GYP1; OrderedLocusNames=YOR070C; ORFNames=YOR29-21;
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].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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-343.
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=11118206; DOI=10.1093/emboj/19.24.6713;
RA Eitzen G., Will E., Gallwitz D., Haas A., Wickner W.;
RT "Sequential action of two GTPases to promote vacuole docking and fusion.";
RL EMBO J. 19:6713-6720(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11359917; DOI=10.1091/mbc.12.5.1215;
RA Du L.-L., Novick P.;
RT "Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus
RT and is a negative regulator of Ypt1p.";
RL Mol. Biol. Cell 12:1215-1226(2001).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP 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 FUNCTION.
RX PubMed=19386605; DOI=10.1074/jbc.m109.000737;
RA Hickey C.M., Stroupe C., Wickner W.;
RT "The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS
RT membrane association.";
RL J. Biol. Chem. 284:16118-16125(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-250, 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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF RAB-GAP TBC DOMAIN.
RX PubMed=11013213; DOI=10.1093/emboj/19.19.5105;
RA Rak A., Fedorov R., Alexandrov K., Albert S., Goody R.S., Gallwitz D.,
RA Scheidig A.J.;
RT "Crystal structure of the GAP domain of Gyp1p: first insights into
RT interaction with Ypt/Rab proteins.";
RL EMBO J. 19:5105-5113(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 244-637, FUNCTION, AND
RP MUTAGENESIS OF GLN-378.
RX PubMed=16855591; DOI=10.1038/nature04847;
RA Pan X., Eathiraj S., Munson M., Lambright D.G.;
RT "TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger
RT mechanism.";
RL Nature 442:303-306(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) that stimulates specifically
CC the intrinsic GTPase activity of Ypt/Rab-type GTPases YPT1 and YPT7
CC (PubMed:11359917, PubMed:19386605). Functions on the Golgi as a
CC negative regulator of YPT1 (PubMed:11359917). Functions on the vacuole
CC as a negative regulator of YPT7 (PubMed:11118206, PubMed:19386605). It
CC is also active on SEC4 and YPT51 (PubMed:10508155). Provides a
CC catalytic arginine (arginine finger) and glutamine (glutamine finger)
CC in trans to accelerate the GTP hydrolysis rate of the substrate GTPase
CC (Probable) (PubMed:16855591). {ECO:0000269|PubMed:10508155,
CC ECO:0000269|PubMed:11118206, ECO:0000269|PubMed:11359917,
CC ECO:0000269|PubMed:16855591, ECO:0000269|PubMed:19386605,
CC ECO:0000305|PubMed:10508155}.
CC -!- INTERACTION:
CC Q08484; P51996: YPT32; NbExp=3; IntAct=EBI-8005, EBI-29384;
CC Q08484; O35963: Rab33b; Xeno; NbExp=3; IntAct=EBI-8005, EBI-6379521;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:11359917}.
CC -!- MISCELLANEOUS: Present with 206 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z70678; CAA94555.1; -; Genomic_DNA.
DR EMBL; Z74978; CAA99263.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10849.1; -; Genomic_DNA.
DR PIR; S66953; S66953.
DR RefSeq; NP_014713.1; NM_001183489.1.
DR PDB; 1FKM; X-ray; 1.90 A; A=249-637.
DR PDB; 2G77; X-ray; 2.26 A; A=244-637.
DR PDBsum; 1FKM; -.
DR PDBsum; 2G77; -.
DR AlphaFoldDB; Q08484; -.
DR SMR; Q08484; -.
DR BioGRID; 34469; 528.
DR DIP; DIP-1258N; -.
DR IntAct; Q08484; 29.
DR MINT; Q08484; -.
DR STRING; 4932.YOR070C; -.
DR iPTMnet; Q08484; -.
DR MaxQB; Q08484; -.
DR PaxDb; Q08484; -.
DR PRIDE; Q08484; -.
DR EnsemblFungi; YOR070C_mRNA; YOR070C; YOR070C.
DR GeneID; 854236; -.
DR KEGG; sce:YOR070C; -.
DR SGD; S000005596; GYP1.
DR VEuPathDB; FungiDB:YOR070C; -.
DR eggNOG; KOG1092; Eukaryota.
DR GeneTree; ENSGT00940000170594; -.
DR HOGENOM; CLU_018687_4_1_1; -.
DR InParanoid; Q08484; -.
DR OMA; FHVFVCA; -.
DR BioCyc; YEAST:G3O-33609-MON; -.
DR EvolutionaryTrace; Q08484; -.
DR PRO; PR:Q08484; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08484; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; 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: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 3D-structure; Golgi apparatus; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..637
FT /note="GTPase-activating protein GYP1"
FT /id="PRO_0000208010"
FT DOMAIN 280..508
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 343
FT /note="Arginine finger"
FT /evidence="ECO:0000269|PubMed:16855591,
FT ECO:0000305|PubMed:10508155"
FT SITE 378
FT /note="Glutamin finger"
FT /evidence="ECO:0000269|PubMed:16855591"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 343
FT /note="R->A,K: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:10508155,
FT ECO:0000269|PubMed:16855591"
FT MUTAGEN 378
FT /note="Q->A: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:16855591"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 304..321
FT /evidence="ECO:0007829|PDB:1FKM"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 354..370
FT /evidence="ECO:0007829|PDB:1FKM"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:1FKM"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 415..433
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 445..461
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:1FKM"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 494..508
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 571..585
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:1FKM"
FT HELIX 612..629
FT /evidence="ECO:0007829|PDB:1FKM"
SQ SEQUENCE 637 AA; 73289 MW; 08C1A26B6ED37E13 CRC64;
MGVRSAAKEM HERDHNSDSS SLVTSLMKSW RISSASSSKK PSLYKMNTTE STSLPSGYAS
SADRDRRTSD GNFEAMAKQQ ASTRRTSNSY SPLRYVNPTL STASNESPRP ALLLRQHHQR
HHHHQQPRHS SSGSVGNNCS NSTEPNKKGD RYFKDLDEDW SAVIDDYNMP IPILTNGGFG
TPVAPTRTLS RKSTSSSINS ISNMGTSAVR NSSSSFTYPQ LPQLQKEKTN DSKKTQLEIE
NERDVQELNS IIQRISKFDN ILKDKTIINQ QDLRQISWNG IPKIHRPVVW KLLIGYLPVN
TKRQEGFLQR KRKEYRDSLK HTFSDQHSRD IPTWHQIEID IPRTNPHIPL YQFKSVQNSL
QRILYLWAIR HPASGYVQGI NDLVTPFFET FLTEYLPPSQ IDDVEIKDPS TYMVDEQITD
LEADTFWCLT KLLEQITDNY IHGQPGILRQ VKNLSQLVKR IDADLYNHFQ NEHVEFIQFA
FRWMNCLLMR EFQMGTVIRM WDTYLSETSQ EVTSSYSMSS NDIKPPVTPT EPRVASFVTP
TKDFQSPTTA LSNMTPNNAV EDSGKMRQSS LNEFHVFVCA AFLIKWSDQL MEMDFQETIT
FLQNPPTKDW TETDIEMLLS EAFIWQSLYK DATSHWL
