GDA1_YEAST
ID GDA1_YEAST Reviewed; 518 AA.
AC P32621; D3DLK7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Guanosine-diphosphatase;
DE Short=GDPase;
DE EC=3.6.1.42;
GN Name=GDA1; OrderedLocusNames=YEL042W; ORFNames=SYGP-ORF16;
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], PROTEIN SEQUENCE OF 125-144; 238-257;
RP 276-281; 366-374 AND 399-412, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=G2-9;
RX PubMed=8391537; DOI=10.1083/jcb.122.2.307;
RA Abeijon C., Yanagisawa K., Mandon E.C., Haeusler A., Moremen K.,
RA Hirschberg C.B., Robbins P.W.;
RT "Guanosine diphosphatase is required for protein and sphingolipid
RT glycosylation in the Golgi lumen of Saccharomyces cerevisiae.";
RL J. Cell Biol. 122:307-323(1993).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBUNIT.
RX PubMed=7540172; DOI=10.1074/jbc.270.24.14564;
RA Berninsone P., Lin Z.-Y., Kempner E., Hirschberg C.B.;
RT "Regulation of yeast Golgi glycosylation. Guanosine diphosphatase functions
RT as a homodimer in the membrane.";
RL J. Biol. Chem. 270:14564-14567(1995).
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).
CC -!- FUNCTION: After transfer of sugars to endogenous macromolecular
CC acceptors, the enzyme converts nucleoside diphosphates to nucleoside
CC monophosphates which in turn exit the Golgi lumen in a coupled
CC antiporter reaction, allowing entry of additional nucleotide sugar from
CC the cytosol. {ECO:0000269|PubMed:8391537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.42;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7540172}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:8391537}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:8391537}.
CC -!- MISCELLANEOUS: Present with 8680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; L19560; AAA34656.1; -; Genomic_DNA.
DR EMBL; U18779; AAB65000.1; -; Genomic_DNA.
DR EMBL; AY723798; AAU09715.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07611.1; -; Genomic_DNA.
DR PIR; A40732; A40732.
DR RefSeq; NP_010872.1; NM_001178857.1.
DR AlphaFoldDB; P32621; -.
DR SMR; P32621; -.
DR BioGRID; 36687; 190.
DR DIP; DIP-5284N; -.
DR IntAct; P32621; 12.
DR MINT; P32621; -.
DR STRING; 4932.YEL042W; -.
DR iPTMnet; P32621; -.
DR MaxQB; P32621; -.
DR PaxDb; P32621; -.
DR PRIDE; P32621; -.
DR DNASU; 856669; -.
DR EnsemblFungi; YEL042W_mRNA; YEL042W; YEL042W.
DR GeneID; 856669; -.
DR KEGG; sce:YEL042W; -.
DR SGD; S000000768; GDA1.
DR VEuPathDB; FungiDB:YEL042W; -.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_4_1_1; -.
DR InParanoid; P32621; -.
DR OMA; DKPIVQY; -.
DR BioCyc; YEAST:YEL042W-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P32621; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32621; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:SGD.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:SGD.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..518
FT /note="Guanosine-diphosphatase"
FT /id="PRO_0000209919"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..518
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 56822 MW; 9A61182D5ED22ADF CRC64;
MAPIFRNYRF AIGAFAVIML ILLIKTSSIG PPSIARTVTP NASIPKTPED ISILPVNDEP
GYLQDSKTEQ NYPELADAVK SQTSQTCSEE HKYVIMIDAG STGSRVHIYK FDVCTSPPTL
LDEKFDMLEP GLSSFDTDSV GAANSLDPLL KVAMNYVPIK ARSCTPVAVK ATAGLRLLGD
AKSSKILSAV RDHLEKDYPF PVVEGDGVSI MGGDEEGVFA WITTNYLLGN IGANGPKLPT
AAVFDLGGGS TQIVFEPTFP INEKMVDGEH KFDLKFGDEN YTLYQFSHLG YGLKEGRNKV
NSVLVENALK DGKILKGDNT KTHQLSSPCL PPKVNATNEK VTLESKETYT IDFIGPDEPS
GAQCRFLTDE ILNKDAQCQS PPCSFNGVHQ PSLVRTFKES NDIYIFSYFY DRTRPLGMPL
SFTLNELNDL ARIVCKGEET WNSVFSGIAG SLDELESDSH FCLDLSFQVS LLHTGYDIPL
QRELRTGKKI ANKEIGWCLG ASLPLLKADN WKCKIQSA
