GCS1_YEAST
ID GCS1_YEAST Reviewed; 352 AA.
AC P35197; D6VRC9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein GCS1;
DE Short=ARF GAP GCS1;
GN Name=GCS1; OrderedLocusNames=YDL226C;
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=8070409; DOI=10.1002/j.1460-2075.1994.tb06692.x;
RA Ireland L.S., Johnston G.C., Drebot M.A., Dhillon N., Demaggio A.J.,
RA Hoekstra M.F., Singer R.A.;
RT "A member of a novel family of yeast 'Zn-finger' proteins mediates the
RT transition from stationary phase to cell proliferation.";
RL EMBO J. 13:3812-3821(1994).
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.
RX PubMed=9927415; DOI=10.1093/emboj/18.3.555;
RA Poon P.P., Cassel D., Spang A., Rotman M., Pick E., Singer R.A.,
RA Johnston G.C.;
RT "Retrograde transport from the yeast Golgi is mediated by two ARF GAP
RT proteins with overlapping function.";
RL EMBO J. 18:555-564(1999).
RN [5]
RP FUNCTION.
RX PubMed=11756474; DOI=10.1083/jcb.200108075;
RA Poon P.P., Nothwehr S.F., Singer R.A., Johnston G.C.;
RT "The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function
RT for transport from the yeast trans-Golgi network.";
RL J. Cell Biol. 155:1239-1250(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11839779; DOI=10.1242/jcs.115.2.275;
RA Huang C.F., Chen C.C., Tung L., Buu L.M., Lee F.J.-S.;
RT "The yeast ADP-ribosylation factor GAP, Gcs1p, is involved in maintenance
RT of mitochondrial morphology.";
RL J. Cell Sci. 115:275-282(2002).
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-157 AND THR-161, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-260, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; SER-157; THR-161;
RP SER-168 AND THR-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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) for ARF1 and ARF2. Involved
CC in intracellular vesicular transport. Required for transport from the
CC trans-Golgi network. Implicated in the regulation of retrograde
CC transport from the Golgi to the ER and in actin cytoskeletal
CC organization. May be involved in the maintenance of mitochondrial
CC morphology, possibly through organizing the actin cytoskeleton in
CC Saccharomyces. {ECO:0000269|PubMed:11756474,
CC ECO:0000269|PubMed:11839779, ECO:0000269|PubMed:9927415}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11839779}.
CC Mitochondrion {ECO:0000269|PubMed:11839779}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:11839779}. Golgi apparatus
CC {ECO:0000305|PubMed:11839779}. Note=Found also in the mitochondria and
CC in the perinuclear region.
CC -!- MISCELLANEOUS: Present with 9560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L24125; AAA50389.1; -; Genomic_DNA.
DR EMBL; Z74274; CAA98805.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11639.1; -; Genomic_DNA.
DR PIR; S47006; S47006.
DR RefSeq; NP_010055.1; NM_001180286.1.
DR PDB; 5FJX; X-ray; 2.45 A; D/E=345-352.
DR PDBsum; 5FJX; -.
DR AlphaFoldDB; P35197; -.
DR SMR; P35197; -.
DR BioGRID; 31884; 260.
DR DIP; DIP-809N; -.
DR IntAct; P35197; 17.
DR MINT; P35197; -.
DR STRING; 4932.YDL226C; -.
DR iPTMnet; P35197; -.
DR MaxQB; P35197; -.
DR PaxDb; P35197; -.
DR PRIDE; P35197; -.
DR EnsemblFungi; YDL226C_mRNA; YDL226C; YDL226C.
DR GeneID; 851372; -.
DR KEGG; sce:YDL226C; -.
DR SGD; S000002385; GCS1.
DR VEuPathDB; FungiDB:YDL226C; -.
DR eggNOG; KOG0704; Eukaryota.
DR HOGENOM; CLU_044516_2_0_1; -.
DR InParanoid; P35197; -.
DR OMA; NVCCDCN; -.
DR BioCyc; YEAST:G3O-29606-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P35197; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P35197; protein.
DR GO; GO:0005856; C:cytoskeleton; IMP:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030037; P:actin filament reorganization involved in cell cycle; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:SGD.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Golgi apparatus; GTPase activation; Metal-binding;
KW Mitochondrion; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..352
FT /note="ADP-ribosylation factor GTPase-activating protein
FT GCS1"
FT /id="PRO_0000074224"
FT DOMAIN 11..127
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 26..49
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 138..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VARIANT 27
FT /note="M -> I"
FT MUTAGEN 29
FT /note="C->Y: In GCS1-1; severely affect the function."
SQ SEQUENCE 352 AA; 39296 MW; 3215525F3EF9CF17 CRC64;
MSDWKVDPDT RRRLLQLQKI GANKKCMDCG APNPQWATPK FGAFICLECA GIHRGLGVHI
SFVRSITMDQ FKPEELLRME KGGNEPLTEW FKSHNIDLSL PQKVKYDNPV AEDYKEKLTC
LCEDRVFEER EHLDFDASKL SATSQTAASA TPGVAQSREG TPLENRRSAT PANSSNGANF
QKEKNEAYFA ELGKKNQSRP DHLPPSQGGK YQGFGSTPAK PPQERSAGSS NTLSLENFQA
DPLGTLSRGW GLFSSAVTKS FEDVNETVIK PHVQQWQSGE LSEETKRAAA QFGQKFQETS
SYGFQAFSNF TKNFNGNAED SSTAGNTTHT EYQKIDNNDK KNEQDEDKWD DF
