GGA1_YEAST
ID GGA1_YEAST Reviewed; 557 AA.
AC Q06336; D6VSY7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA1;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 1;
GN Name=GGA1; OrderedLocusNames=YDR358W; ORFNames=D9476.2;
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=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 [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 CHARACTERIZATION.
RX PubMed=10747088; DOI=10.1083/jcb.149.1.67;
RA Hirst J., Lui W.W.Y., Bright N.A., Totty N., Seaman M.N.J., Robinson M.S.;
RT "A family of proteins with gamma-adaptin and VHS domains that facilitate
RT trafficking between the trans-Golgi network and the vacuole/lysosome.";
RL J. Cell Biol. 149:67-80(2000).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11124697;
RX DOI=10.1002/1097-0061(200101)18:1<1::aid-yea644>3.0.co;2-5;
RA Zhdankina O., Strand N.L., Redmond J.M., Boman A.L.;
RT "Yeast GGA proteins interact with GTP-bound Arf and facilitate transport
RT through the Golgi.";
RL Yeast 18:1-18(2001).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348; SER-357 AND SER-378, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-394, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-357 AND SER-378, 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: May play a role in the regulation of membrane traffic through
CC the trans-Golgi network.
CC -!- SUBUNIT: Binds to ARF1 and ARF2.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U28372; AAB64793.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12197.1; -; Genomic_DNA.
DR PIR; S61154; S61154.
DR RefSeq; NP_010645.1; NM_001180666.1.
DR PDB; 5CN1; X-ray; 2.31 A; A/B/C/D=433-557.
DR PDB; 5CN2; X-ray; 2.25 A; A/B=433-557.
DR PDBsum; 5CN1; -.
DR PDBsum; 5CN2; -.
DR AlphaFoldDB; Q06336; -.
DR SMR; Q06336; -.
DR BioGRID; 32414; 127.
DR IntAct; Q06336; 5.
DR MINT; Q06336; -.
DR STRING; 4932.YDR358W; -.
DR iPTMnet; Q06336; -.
DR MaxQB; Q06336; -.
DR PaxDb; Q06336; -.
DR PRIDE; Q06336; -.
DR TopDownProteomics; Q06336; -.
DR EnsemblFungi; YDR358W_mRNA; YDR358W; YDR358W.
DR GeneID; 851960; -.
DR KEGG; sce:YDR358W; -.
DR SGD; S000002766; GGA1.
DR VEuPathDB; FungiDB:YDR358W; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000176423; -.
DR HOGENOM; CLU_017092_0_0_1; -.
DR InParanoid; Q06336; -.
DR OMA; QKWINDA; -.
DR BioCyc; YEAST:G3O-29909-MON; -.
DR PRO; PR:Q06336; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06336; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR008153; GAE_dom.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR041198; GGA_N-GAT.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF18308; GGA_N-GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Golgi apparatus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..557
FT /note="ADP-ribosylation factor-binding protein GGA1"
FT /id="PRO_0000212686"
FT DOMAIN 29..165
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 192..317
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 440..556
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 451..461
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 463..475
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 510..522
FT /evidence="ECO:0007829|PDB:5CN2"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 531..541
FT /evidence="ECO:0007829|PDB:5CN2"
FT STRAND 544..554
FT /evidence="ECO:0007829|PDB:5CN2"
SQ SEQUENCE 557 AA; 62320 MW; DBA76787F998DBD7 CRC64;
MPQRIELTSE PVRKPRSTES SLLRKIQRAC RSTLPEPDLG LNLDVADYIN SKQGATPREA
VLAIEKLVNN GDTQAAVFAL SLLDVLVKNC GYSIHLQISR KEFLNDLVKR FPEQPPLRYS
KVQQMILEAI EEWYQTICKH ASYKDDLQYI NDMHKLLKYK GYTFPKVGSE NLAVLRPNDQ
LRTPSELQEE QERAQAAKLE ELLRSGKPDD LKEANKLMKI MAGFKDDTKV AVKQAINNEL
NKLKRKADLF NEMLTSADEP DLENEAIQEL YGDLKSAQPK FKKLIEEERD DDALVSNLSK
FNDLVIQLLK RYKSIKGMKE EELNVPDTNE PAKELNLIDF DDDTTANTPS VTSPSKSLQP
FDDLLGDFNK VSLSSPKSPQ ENDTVVDILG DAHSKSSGID LLDFDSQPGE SKTALSAYSN
SIVLPNGLLN SSSNSKEITA QSQRHILNQS DHLRIDYELT RESMTKLRLV IFYSNISSDP
ITNFALLVAS PKGTTLSLQP QSGNMLQSNS RDGIKQIASV EGISVNLGKP IKLKWKANYC
TKGDSKEESG TTSLPTI
