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GDP-mannose transporter 1 (GMT 1) (Low dye-binding protein 3) (Morphogenesis checkpoint-dependent protein 3) (Vanadate resistance glycosylation protein 4)

 GMT1_YEAST              Reviewed;         337 AA.
P40107; D6VVB0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
12-SEP-2018, entry version 154.
RecName: Full=GDP-mannose transporter 1;
Short=GMT 1;
AltName: Full=Low dye-binding protein 3;
AltName: Full=Morphogenesis checkpoint-dependent protein 3;
AltName: Full=Vanadate resistance glycosylation protein 4;
Name=VRG4; Synonyms=GOG5, LDB3, MCD3, VAN2, VIG4;
OrderedLocusNames=YGL225W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=8632002; DOI=10.1074/jbc.271.7.3837;
Poster J.B., Dean N.;
"The yeast VRG4 gene is required for normal Golgi functions and
defines a new family of related genes.";
J. Biol. Chem. 271:3837-3845(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=7672592;
Kanik-Ennulat C., Montalvo E., Neff N.;
"Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae
show defects in Golgi-mediated protein glycosylation, sporulation and
detergent resistance.";
Genetics 140:933-943(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9290212;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P;
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
chromosome VII.";
Yeast 13:1077-1090(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
FUNCTION.
PubMed=2137555; DOI=10.1128/MCB.10.3.898;
Kanik-Ennulat C., Neff N.;
"Vanadate-resistant mutants of Saccharomyces cerevisiae show
alterations in protein phosphorylation and growth control.";
Mol. Cell. Biol. 10:898-909(1990).
[7]
FUNCTION.
PubMed=2014241; DOI=10.1073/pnas.88.8.3209;
Ballou L., Hitzeman R.A., Lewis M.S., Ballou C.E.;
"Vanadate-resistant yeast mutants are defective in protein
glycosylation.";
Proc. Natl. Acad. Sci. U.S.A. 88:3209-3212(1991).
[8]
FUNCTION.
PubMed=7877969; DOI=10.1073/pnas.92.5.1287;
Dean N.;
"Yeast glycosylation mutants are sensitive to aminoglycosides.";
Proc. Natl. Acad. Sci. U.S.A. 92:1287-1291(1995).
[9]
FUNCTION.
PubMed=9335583;
Mondesert G., Clarke D.J., Reed S.I.;
"Identification of genes controlling growth polarity in the budding
yeast Saccharomyces cerevisiae: a possible role of N-glycosylation and
involvement of the exocyst complex.";
Genetics 147:421-434(1997).
[10]
FUNCTION.
PubMed=9184829; DOI=10.1093/glycob/7.4.487;
Manas P., Olivero I., Avalos M., Hernandez L.M.;
"Isolation of new nonconditional Saccharomyces cerevisiae mutants
defective in asparagine-linked glycosylation.";
Glycobiology 7:487-497(1997).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9395539; DOI=10.1074/jbc.272.50.31908;
Dean N., Zhang Y.B., Poster J.B.;
"The VRG4 gene is required for GDP-mannose transport into the lumen of
the Golgi in the yeast, Saccharomyces cerevisiae.";
J. Biol. Chem. 272:31908-31914(1997).
[12]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF SER-278
AND ALA-286.
PubMed=10570930; DOI=10.1016/S0014-5793(99)01177-1;
Abe M., Hashimoto H., Yoda K.;
"Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of
the yeast Saccharomyces cerevisiae.";
FEBS Lett. 458:309-312(1999).
[13]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
THR-280; SER-282; GLY-285; ALA-286; LEU-287; ASN-288; LYS-289 AND
PRO-291.
PubMed=11067855; DOI=10.1074/jbc.M009114200;
Gao X.-D., Nishikawa A., Dean N.;
"Identification of a conserved motif in the yeast Golgi GDP-mannose
transporter required for binding to nucleotide sugar.";
J. Biol. Chem. 276:4424-4432(2001).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12478588; DOI=10.1002/yea.925;
Hashimoto H., Abe M., Hirata A., Noda Y., Adachi H., Yoda K.;
"Progression of the stacked Golgi compartments in the yeast
Saccharomyces cerevisiae by overproduction of GDP-mannose
transporter.";
Yeast 19:1413-1424(2002).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[16]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[17]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH RET2.
PubMed=15494368; DOI=10.1242/jcs.01491;
Abe M., Noda Y., Adachi H., Yoda K.;
"Localization of GDP-mannose transporter in the Golgi requires
retrieval to the endoplasmic reticulum depending on its cytoplasmic
tail and coatomer.";
J. Cell Sci. 117:5687-5696(2004).
[18]
SUBCELLULAR LOCATION.
PubMed=16699524; DOI=10.1038/nature04717;
Losev E., Reinke C.A., Jellen J., Strongin D.E., Bevis B.J.,
Glick B.S.;
"Golgi maturation visualized in living yeast.";
Nature 441:1002-1006(2006).
[19]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
-!- FUNCTION: Involved in the import of GDP-mannose from the cytoplasm
into the Golgi lumen. Defective copy causes severe glycosylation
defect and abnormal retention of soluble endoplasmic reticulum
proteins. Involved in vanadate sensitivity.
{ECO:0000269|PubMed:10570930, ECO:0000269|PubMed:11067855,
ECO:0000269|PubMed:12478588, ECO:0000269|PubMed:15494368,
ECO:0000269|PubMed:2014241, ECO:0000269|PubMed:2137555,
ECO:0000269|PubMed:7672592, ECO:0000269|PubMed:7877969,
ECO:0000269|PubMed:8632002, ECO:0000269|PubMed:9184829,
ECO:0000269|PubMed:9335583, ECO:0000269|PubMed:9395539}.
-!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:10570930,
ECO:0000269|PubMed:11067855}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass
membrane protein. Cytoplasmic vesicle membrane; Multi-pass
membrane protein. Endoplasmic reticulum membrane; Multi-pass
membrane protein. Note=Recycles between the Golgi apparatus and
the endoplasmic reticulum.
-!- MISCELLANEOUS: Present with 31900 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TPT transporter family. SLC35D
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L33915; AAC37468.1; -; Genomic_DNA.
EMBL; U15599; AAA81537.1; -; Genomic_DNA.
EMBL; Z72747; CAA96941.1; -; Genomic_DNA.
EMBL; BK006941; DAA07894.1; -; Genomic_DNA.
PIR; S50238; S50238.
RefSeq; NP_011290.1; NM_001181090.1.
PDB; 5OGE; X-ray; 3.22 A; A/B/C/D/E/F/G/H=1-337.
PDB; 5OGK; X-ray; 3.60 A; A/B/C/D/E/F/G/H=1-337.
PDBsum; 5OGE; -.
PDBsum; 5OGK; -.
ProteinModelPortal; P40107; -.
SMR; P40107; -.
BioGrid; 33034; 127.
DIP; DIP-5108N; -.
IntAct; P40107; 6.
STRING; 4932.YGL225W; -.
TCDB; 2.A.7.13.1; the drug/metabolite transporter (dmt) superfamily.
MaxQB; P40107; -.
PaxDb; P40107; -.
PRIDE; P40107; -.
EnsemblFungi; YGL225W; YGL225W; YGL225W.
GeneID; 852647; -.
KEGG; sce:YGL225W; -.
EuPathDB; FungiDB:YGL225W; -.
SGD; S000003193; VRG4.
GeneTree; ENSGT00510000053739; -.
HOGENOM; HOG000031183; -.
InParanoid; P40107; -.
KO; K15356; -.
OMA; TRSFCVD; -.
OrthoDB; EOG092C3KEZ; -.
BioCyc; YEAST:G3O-30699-MONOMER; -.
PRO; PR:P40107; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IDA:SGD.
GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
GO; GO:1990570; P:GDP-mannose transmembrane transport; IMP:SGD.
InterPro; IPR038736; Vrg4-like.
PANTHER; PTHR44752; PTHR44752; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasmic vesicle;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
Reference proteome; Sugar transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 337 GDP-mannose transporter 1.
/FTId=PRO_0000213398.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 51 Lumenal. {ECO:0000255}.
TRANSMEM 52 72 Helical. {ECO:0000255}.
TOPO_DOM 73 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 113 Helical. {ECO:0000255}.
TOPO_DOM 114 119 Lumenal. {ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TOPO_DOM 141 144 Cytoplasmic. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TOPO_DOM 166 180 Lumenal. {ECO:0000255}.
TRANSMEM 181 201 Helical. {ECO:0000255}.
TOPO_DOM 202 215 Cytoplasmic. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TOPO_DOM 237 252 Lumenal. {ECO:0000255}.
TRANSMEM 253 273 Helical. {ECO:0000255}.
TOPO_DOM 274 279 Cytoplasmic. {ECO:0000255}.
TRANSMEM 280 300 Helical. {ECO:0000255}.
TOPO_DOM 301 304 Lumenal. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TOPO_DOM 326 337 Cytoplasmic. {ECO:0000255}.
REGION 279 291 GDP-mannose-binding.
REGION 326 337 RET2-binding.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 278 278 S->C: In VIG4-2; increases drug
sensitivity and decreases protein
glycolysis.
{ECO:0000269|PubMed:10570930}.
MUTAGEN 280 280 T->A: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 282 282 S->A: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 285 285 G->A,D: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 286 286 A->V: In VIG4-1; increases drug
sensitivity and decreases protein
glycolysis. {ECO:0000269|PubMed:10570930,
ECO:0000269|PubMed:11067855}.
MUTAGEN 287 287 L->A: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 288 288 N->A: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 289 289 K->A,D: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
MUTAGEN 291 291 P->A: Decreases transport activity and
GDP-mannose-binding.
{ECO:0000269|PubMed:11067855}.
STRAND 18 20 {ECO:0000244|PDB:5OGE}.
HELIX 23 41 {ECO:0000244|PDB:5OGE}.
HELIX 51 70 {ECO:0000244|PDB:5OGE}.
HELIX 83 108 {ECO:0000244|PDB:5OGE}.
HELIX 111 132 {ECO:0000244|PDB:5OGE}.
HELIX 139 157 {ECO:0000244|PDB:5OGE}.
HELIX 178 208 {ECO:0000244|PDB:5OGE}.
HELIX 215 222 {ECO:0000244|PDB:5OGE}.
HELIX 224 235 {ECO:0000244|PDB:5OGE}.
HELIX 240 244 {ECO:0000244|PDB:5OGE}.
HELIX 249 275 {ECO:0000244|PDB:5OGE}.
HELIX 278 287 {ECO:0000244|PDB:5OGE}.
HELIX 289 299 {ECO:0000244|PDB:5OGE}.
HELIX 306 332 {ECO:0000244|PDB:5OGE}.
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


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