GMT1_YEAST
ID GMT1_YEAST Reviewed; 337 AA.
AC P40107; D6VVB0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=GDP-mannose transporter 1;
DE Short=GMT 1;
DE AltName: Full=Low dye-binding protein 3;
DE AltName: Full=Morphogenesis checkpoint-dependent protein 3;
DE AltName: Full=Vanadate resistance glycosylation protein 4;
GN Name=VRG4; Synonyms=GOG5, LDB3, MCD3, VAN2, VIG4;
GN OrderedLocusNames=YGL225W;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8632002; DOI=10.1074/jbc.271.7.3837;
RA Poster J.B., Dean N.;
RT "The yeast VRG4 gene is required for normal Golgi functions and defines a
RT new family of related genes.";
RL J. Biol. Chem. 271:3837-3845(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7672592; DOI=10.1093/genetics/140.3.933;
RA Kanik-Ennulat C., Montalvo E., Neff N.;
RT "Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae show
RT defects in Golgi-mediated protein glycosylation, sporulation and detergent
RT resistance.";
RL Genetics 140:933-943(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=2137555; DOI=10.1128/mcb.10.3.898-909.1990;
RA Kanik-Ennulat C., Neff N.;
RT "Vanadate-resistant mutants of Saccharomyces cerevisiae show alterations in
RT protein phosphorylation and growth control.";
RL Mol. Cell. Biol. 10:898-909(1990).
RN [7]
RP FUNCTION.
RX PubMed=2014241; DOI=10.1073/pnas.88.8.3209;
RA Ballou L., Hitzeman R.A., Lewis M.S., Ballou C.E.;
RT "Vanadate-resistant yeast mutants are defective in protein glycosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3209-3212(1991).
RN [8]
RP FUNCTION.
RX PubMed=7877969; DOI=10.1073/pnas.92.5.1287;
RA Dean N.;
RT "Yeast glycosylation mutants are sensitive to aminoglycosides.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1287-1291(1995).
RN [9]
RP FUNCTION.
RX PubMed=9335583; DOI=10.1093/genetics/147.2.421;
RA Mondesert G., Clarke D.J., Reed S.I.;
RT "Identification of genes controlling growth polarity in the budding yeast
RT Saccharomyces cerevisiae: a possible role of N-glycosylation and
RT involvement of the exocyst complex.";
RL Genetics 147:421-434(1997).
RN [10]
RP FUNCTION.
RX PubMed=9184829; DOI=10.1093/glycob/7.4.487;
RA Manas P., Olivero I., Avalos M., Hernandez L.M.;
RT "Isolation of new nonconditional Saccharomyces cerevisiae mutants defective
RT in asparagine-linked glycosylation.";
RL Glycobiology 7:487-497(1997).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9395539; DOI=10.1074/jbc.272.50.31908;
RA Dean N., Zhang Y.B., Poster J.B.;
RT "The VRG4 gene is required for GDP-mannose transport into the lumen of the
RT Golgi in the yeast, Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:31908-31914(1997).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF SER-278 AND
RP ALA-286.
RX PubMed=10570930; DOI=10.1016/s0014-5793(99)01177-1;
RA Abe M., Hashimoto H., Yoda K.;
RT "Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of the
RT yeast Saccharomyces cerevisiae.";
RL FEBS Lett. 458:309-312(1999).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP THR-280; SER-282; GLY-285; ALA-286; LEU-287; ASN-288; LYS-289 AND PRO-291.
RX PubMed=11067855; DOI=10.1074/jbc.m009114200;
RA Gao X.-D., Nishikawa A., Dean N.;
RT "Identification of a conserved motif in the yeast Golgi GDP-mannose
RT transporter required for binding to nucleotide sugar.";
RL J. Biol. Chem. 276:4424-4432(2001).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12478588; DOI=10.1002/yea.925;
RA Hashimoto H., Abe M., Hirata A., Noda Y., Adachi H., Yoda K.;
RT "Progression of the stacked Golgi compartments in the yeast Saccharomyces
RT cerevisiae by overproduction of GDP-mannose transporter.";
RL Yeast 19:1413-1424(2002).
RN [15]
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 [16]
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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH RET2.
RX PubMed=15494368; DOI=10.1242/jcs.01491;
RA Abe M., Noda Y., Adachi H., Yoda K.;
RT "Localization of GDP-mannose transporter in the Golgi requires retrieval to
RT the endoplasmic reticulum depending on its cytoplasmic tail and coatomer.";
RL J. Cell Sci. 117:5687-5696(2004).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=16699524; DOI=10.1038/nature04717;
RA Losev E., Reinke C.A., Jellen J., Strongin D.E., Bevis B.J., Glick B.S.;
RT "Golgi maturation visualized in living yeast.";
RL Nature 441:1002-1006(2006).
RN [19]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Involved in the import of GDP-mannose from the cytoplasm into
CC the Golgi lumen. Defective copy causes severe glycosylation defect and
CC abnormal retention of soluble endoplasmic reticulum proteins. Involved
CC in vanadate sensitivity. {ECO:0000269|PubMed:10570930,
CC ECO:0000269|PubMed:11067855, ECO:0000269|PubMed:12478588,
CC ECO:0000269|PubMed:15494368, ECO:0000269|PubMed:2014241,
CC ECO:0000269|PubMed:2137555, ECO:0000269|PubMed:7672592,
CC ECO:0000269|PubMed:7877969, ECO:0000269|PubMed:8632002,
CC ECO:0000269|PubMed:9184829, ECO:0000269|PubMed:9335583,
CC ECO:0000269|PubMed:9395539}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:10570930,
CC ECO:0000269|PubMed:11067855}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC Note=Recycles between the Golgi apparatus and the endoplasmic
CC reticulum.
CC -!- MISCELLANEOUS: Present with 31900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC {ECO:0000305}.
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DR EMBL; L33915; AAC37468.1; -; Genomic_DNA.
DR EMBL; U15599; AAA81537.1; -; Genomic_DNA.
DR EMBL; Z72747; CAA96941.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07894.1; -; Genomic_DNA.
DR PIR; S50238; S50238.
DR RefSeq; NP_011290.1; NM_001181090.1.
DR PDB; 5OGE; X-ray; 3.22 A; A/B/C/D/E/F/G/H=1-337.
DR PDB; 5OGK; X-ray; 3.60 A; A/B/C/D/E/F/G/H=1-337.
DR PDB; 6QSK; X-ray; 3.39 A; A/B/C/D/E/F/G/H=1-337.
DR PDBsum; 5OGE; -.
DR PDBsum; 5OGK; -.
DR PDBsum; 6QSK; -.
DR AlphaFoldDB; P40107; -.
DR SMR; P40107; -.
DR BioGRID; 33034; 130.
DR DIP; DIP-5108N; -.
DR IntAct; P40107; 6.
DR STRING; 4932.YGL225W; -.
DR TCDB; 2.A.7.13.1; the drug/metabolite transporter (dmt) superfamily.
DR MaxQB; P40107; -.
DR PaxDb; P40107; -.
DR PRIDE; P40107; -.
DR EnsemblFungi; YGL225W_mRNA; YGL225W; YGL225W.
DR GeneID; 852647; -.
DR KEGG; sce:YGL225W; -.
DR SGD; S000003193; VRG4.
DR VEuPathDB; FungiDB:YGL225W; -.
DR eggNOG; KOG1444; Eukaryota.
DR GeneTree; ENSGT00510000048348; -.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; P40107; -.
DR OMA; IRVWIPV; -.
DR BioCyc; YEAST:G3O-30699-MON; -.
DR PRO; PR:P40107; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P40107; protein.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:1990570; P:GDP-mannose transmembrane transport; IMP:SGD.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..337
FT /note="GDP-mannose transporter 1"
FT /id="PRO_0000213398"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..119
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..180
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..252
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..304
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 326..337
FT /note="RET2-binding"
FT BINDING 279..291
FT /ligand="GDP-alpha-D-mannose"
FT /ligand_id="ChEBI:CHEBI:57527"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 278
FT /note="S->C: In VIG4-2; increases drug sensitivity and
FT decreases protein glycolysis."
FT /evidence="ECO:0000269|PubMed:10570930"
FT MUTAGEN 280
FT /note="T->A: Decreases transport activity and GDP-mannose-
FT binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 282
FT /note="S->A: Decreases transport activity and GDP-mannose-
FT binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 285
FT /note="G->A,D: Decreases transport activity and GDP-
FT mannose-binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 286
FT /note="A->V: In VIG4-1; increases drug sensitivity and
FT decreases protein glycolysis."
FT /evidence="ECO:0000269|PubMed:10570930,
FT ECO:0000269|PubMed:11067855"
FT MUTAGEN 287
FT /note="L->A: Decreases transport activity and GDP-mannose-
FT binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 288
FT /note="N->A: Decreases transport activity and GDP-mannose-
FT binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 289
FT /note="K->A,D: Decreases transport activity and GDP-
FT mannose-binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT MUTAGEN 291
FT /note="P->A: Decreases transport activity and GDP-mannose-
FT binding."
FT /evidence="ECO:0000269|PubMed:11067855"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 23..41
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 83..108
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 111..132
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 139..157
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 178..208
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 249..275
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:5OGE"
FT HELIX 306..332
FT /evidence="ECO:0007829|PDB:5OGE"
SQ SEQUENCE 337 AA; 37019 MW; 5C7EE07B05DA8E61 CRC64;
MSELKTGHAG HNPWASVANS GPISILSYCG SSILMTVTNK FVVNLKDFNM NFVMLFVQSL
VCTITLIILR ILGYAKFRSL NKTDAKNWFP ISFLLVLMIY TSSKALQYLA VPIYTIFKNL
TIILIAYGEV LFFGGSVTSM ELSSFLLMVL SSVVATWGDQ QAVAAKAASL AEGAAGAVAS
FNPGYFWMFT NCITSALFVL IMRKRIKLTN FKDFDTMFYN NVLALPILLL FSFCVEDWSS
VNLTNNFSND SLTAMIISGV ASVGISYCSG WCVRVTSSTT YSMVGALNKL PIALSGLIFF
DAPRNFLSIL SIFIGFLSGI IYAVAKQKKQ QAQPLRK
