GLO3_YEAST
ID GLO3_YEAST Reviewed; 493 AA.
AC P38682; D3DM28;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein GLO3;
DE Short=ARF GAP GLO3;
GN Name=GLO3; OrderedLocusNames=YER122C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP 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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-398, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-306; SER-389 AND
RP SER-398, AND 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC (ARF) family. Involved in retrograde vesicular transport from the Golgi
CC to the endoplasmic reticulum. {ECO:0000269|PubMed:9927415}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X79514; CAA56046.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03220.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07782.1; -; Genomic_DNA.
DR PIR; S50625; S50625.
DR RefSeq; NP_011048.1; NM_001179012.1.
DR PDB; 7JTZ; X-ray; 2.07 A; A/B/C/D=1-150.
DR PDBsum; 7JTZ; -.
DR AlphaFoldDB; P38682; -.
DR SMR; P38682; -.
DR BioGRID; 36866; 528.
DR DIP; DIP-2740N; -.
DR IntAct; P38682; 11.
DR MINT; P38682; -.
DR STRING; 4932.YER122C; -.
DR iPTMnet; P38682; -.
DR MaxQB; P38682; -.
DR PaxDb; P38682; -.
DR PRIDE; P38682; -.
DR EnsemblFungi; YER122C_mRNA; YER122C; YER122C.
DR GeneID; 856859; -.
DR KEGG; sce:YER122C; -.
DR SGD; S000000924; GLO3.
DR VEuPathDB; FungiDB:YER122C; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000173235; -.
DR HOGENOM; CLU_023062_7_0_1; -.
DR InParanoid; P38682; -.
DR OMA; QNVGESI; -.
DR BioCyc; YEAST:G3O-30286-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:P38682; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P38682; protein.
DR GO; GO:0030126; C:COPI vesicle coat; IPI:SGD.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Golgi apparatus; GTPase activation; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..493
FT /note="ADP-ribosylation factor GTPase-activating protein
FT GLO3"
FT /id="PRO_0000074225"
FT DOMAIN 16..137
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 31..54
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 145..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 222
FT /note="S -> C (in Ref. 1; CAA56046)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..493
FT /note="EAHDKLKTFDNATSISSSSYFGEDKEVDEFGNPINSSGSGAGNFDGRNSNNG
FT FIDFNASADDELQMLRDVVEQGAEKLGSYLRDYLRK -> GSA (in Ref. 1;
FT CAA56046)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:7JTZ"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:7JTZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7JTZ"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:7JTZ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:7JTZ"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:7JTZ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7JTZ"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7JTZ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7JTZ"
FT HELIX 119..138
FT /evidence="ECO:0007829|PDB:7JTZ"
SQ SEQUENCE 493 AA; 55094 MW; CDB588BF1351A042 CRC64;
MSNDEGETFA TEQTTQQVFQ KLGSNMENRV CFDCGNKNPT WTSVPFGVML CIQCSAVHRN
MGVHITFVKS STLDKWTINN LRRFKLGGNH KARDFFLKNN GKQLLNTANV DAKTKYTSPV
AKKYKIHLDK KVQKDMELYP SELVLNGQDS SDSPLDTDSD ASRSTSKENS VDDFFSNWQK
PSSNSSSKLN VNTGSLAPKN NTTGSTPKTT VTKTRSSILT ASRKKPVLNS QDKKKHSILS
SSRKPTRLTA KKVDKSQAED LFDQFKKEAQ QEKEDEFTNS SSSTKIRQND YDSQFMNNSK
GNNNNSIDDI NTQPDEFNDF LNDTSNSFDT TRKEQQDTLT PKFAKLGFGM TMNDANDLAK
QQKESQKIAQ GPRYTGRIAE RYGTQKAISS DQLFGRGSFD EAANREAHDK LKTFDNATSI
SSSSYFGEDK EVDEFGNPIN SSGSGAGNFD GRNSNNGFID FNASADDELQ MLRDVVEQGA
EKLGSYLRDY LRK
