GGA2_YEAST
ID GGA2_YEAST Reviewed; 585 AA.
AC P38817; D3DL58;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA2;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 2;
GN Name=GGA2; OrderedLocusNames=YHR108W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION.
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 FUNCTION, AND SUBUNIT.
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 INTERACTION WITH ENT3 AND ENT5, AND MUTAGENESIS OF LYS-560; TRP-563 AND
RP LYS-564.
RX PubMed=12483220; DOI=10.1038/ncb901;
RA Duncan M.C., Costaguta G., Payne G.S.;
RT "Yeast epsin-related proteins required for Golgi-endosome traffic define a
RT gamma-adaptin ear-binding motif.";
RL Nat. Cell Biol. 5:77-81(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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-180 AND LYS-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: May play a role in the regulation of membrane traffic through
CC the trans-Golgi network. {ECO:0000269|PubMed:10747088,
CC ECO:0000269|PubMed:11124697}.
CC -!- SUBUNIT: Binds to ARF1 and ARF2. {ECO:0000269|PubMed:11124697}.
CC -!- INTERACTION:
CC P38817; P48563: MON2; NbExp=3; IntAct=EBI-7569, EBI-28333;
CC P38817; P39104: PIK1; NbExp=3; IntAct=EBI-7569, EBI-13423;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network.
CC -!- MISCELLANEOUS: Present with 2270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U00059; AAB68854.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06802.1; -; Genomic_DNA.
DR PIR; S48950; S48950.
DR RefSeq; NP_011976.1; NM_001179238.1.
DR PDB; 3MNM; X-ray; 1.73 A; A/B/C=465-585.
DR PDBsum; 3MNM; -.
DR AlphaFoldDB; P38817; -.
DR SMR; P38817; -.
DR BioGRID; 36541; 170.
DR DIP; DIP-2971N; -.
DR IntAct; P38817; 22.
DR MINT; P38817; -.
DR STRING; 4932.YHR108W; -.
DR iPTMnet; P38817; -.
DR MaxQB; P38817; -.
DR PaxDb; P38817; -.
DR PRIDE; P38817; -.
DR EnsemblFungi; YHR108W_mRNA; YHR108W; YHR108W.
DR GeneID; 856508; -.
DR KEGG; sce:YHR108W; -.
DR SGD; S000001150; GGA2.
DR VEuPathDB; FungiDB:YHR108W; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000176423; -.
DR HOGENOM; CLU_017092_0_0_1; -.
DR InParanoid; P38817; -.
DR OMA; DEWNFAS; -.
DR BioCyc; YEAST:G3O-31151-MON; -.
DR PRO; PR:P38817; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38817; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
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; IPR002014; VHS_dom.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF03127; 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; Isopeptide bond;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..585
FT /note="ADP-ribosylation factor-binding protein GGA2"
FT /id="PRO_0000212687"
FT DOMAIN 33..169
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 196..321
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 466..581
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 358..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 560
FT /note="K->Q: Reduced binding to ENT3."
FT /evidence="ECO:0000269|PubMed:12483220"
FT MUTAGEN 563
FT /note="W->A: Reduced binding to ENT3 and ENT5."
FT /evidence="ECO:0000269|PubMed:12483220"
FT MUTAGEN 564
FT /note="K->Q: Reduced binding to ENT3 and ENT5."
FT /evidence="ECO:0000269|PubMed:12483220"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 479..489
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 509..517
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 560..569
FT /evidence="ECO:0007829|PDB:3MNM"
FT STRAND 572..581
FT /evidence="ECO:0007829|PDB:3MNM"
SQ SEQUENCE 585 AA; 64347 MW; 7AC3A317AEE302E2 CRC64;
MSHPHSHSIY LSELPVRKPQ ALGNPLLRKI QRACRMSLAE PDLALNLDIA DYINEKQGAA
PRDAAIALAK LINNRESHVA IFALSLLDVL VKNCGYPFHL QISRKEFLNE LVKRFPGHPP
LRYSKIQRLI LTAIEEWYQT ICKHSSYKND MGYIRDMHRL LKYKGYAFPK ISESDLAVLK
PSNQLKTASE IQKEQEIAQA AKLEELIRRG KPEDLREANK LMKIMAGFKE DNAVQAKQAI
SSELNKLKRK ADLLNEMLES PDSQNWDNET TQELHSALKV AQPKFQKIIE EEQEDDALVQ
DLLKFNDTVN QLLEKFNLLK NGDSNAASQI HPSHVSAPLQ QSSGALTNEI NLIDFNDLDE
APSQGNNNTN GTGTPAAAET SVNDLLGDLT DLSISNPSTA NQASFGLGGD IVLGSSQPAP
PVTTTNNSNN TLDLLGLSTP QSPTNSQAVN SSGFDLLMGF NPTTGTTTAP ARTLVNQSPN
LKIEFEISRE SNSVIRIKSF FTNLSSSPIS NLVFLLAVPK SMSLKLQPQS SNFMIGNAKD
GISQEGTIEN APANPSKALK VKWKVNYSVN STQAEETAVF TLPNV
