GDP-mannose transporter 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P40107 (GMT1_YEAST)

Last modified July 22, 2008. Version 66. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    GDP-mannose transporter 1
      Short name(s)=GMT 1
Alternative name(s):
    Vanadate resistance glycosylation protein 4
    Low dye-binding protein 3
    Morphogenesis checkpoint-dependent protein 3

Gene names

Name:	VRG4
Synonyms:	GOG5, LDB3, MCD3, VAN2, VIG4
Ordered Locus Names:	YGL225W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Subunit structure	Homooligomer.
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.
Sequence similarities	Belongs to the TPT transporter family. SLC35D subfamily.

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Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane
Domain	Transmembrane
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid glycosylation Ref.10 Inferred from mutant phenotype. Source: SGD nucleotide-sugar transport Ref.10 Inferred from direct assay. Source: SGD protein amino acid N-linked glycosylation Ref.10 Inferred from mutant phenotype. Source: SGD
Cellular component	Golgi apparatus Ref.10 Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	nucleotide-sugar transmembrane transporter activity Ref.10 Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BZZ1	P38822	1	EBI-7764,EBI-3889

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 337

337

GDP-mannose transporter 1

Regions

Topological domain

1 – 16

Cytoplasmic Potential

Transmembrane

17 – 37

Potential

Topological domain

38 – 51

Lumenal Potential

Transmembrane

52 – 72

Potential

Topological domain

73 – 92

Cytoplasmic Potential

Transmembrane

93 – 113

Potential

Topological domain

114 – 119

Lumenal Potential

Transmembrane

120 – 140

Potential

Topological domain

141 – 144

Cytoplasmic Potential

Transmembrane

145 – 165

Potential

Topological domain

166 – 180

Lumenal Potential

Transmembrane

181 – 201

Potential

Topological domain

202 – 215

Cytoplasmic Potential

Transmembrane

216 – 236

Potential

Topological domain

237 – 252

Lumenal Potential

Transmembrane

253 – 273

Potential

Topological domain

274 – 279

Cytoplasmic Potential

Transmembrane

280 – 300

Potential

Topological domain

301 – 304

Lumenal Potential

Transmembrane

305 – 325

Potential

Topological domain

326 – 337

Cytoplasmic Potential

Region

279 – 291

GDP-mannose-binding

Region

326 – 337

RET2-binding

Amino acid modifications

Glycosylation

119

N-linked (GlcNAc...) Potential

Glycosylation

242

N-linked (GlcNAc...) Potential

Glycosylation

246

N-linked (GlcNAc...) Potential

Glycosylation

249

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

278

S → C in VIG4-2; increases drug sensitivity and decreases protein glycolysis

Mutagenesis

280

T → A: Decreases transport activity and GDP-mannose-binding

Mutagenesis

282

S → A: Decreases transport activity and GDP-mannose-binding

Mutagenesis

285

G → A or D: Decreases transport activity and GDP-mannose-binding

Mutagenesis

286

A → V in VIG4-1; increases drug sensitivity and decreases protein glycolysis

Mutagenesis

287

L → A: Decreases transport activity and GDP-mannose-binding

Mutagenesis

288

N → A: Decreases transport activity and GDP-mannose-binding

Mutagenesis

289

K → A or D: Decreases transport activity and GDP-mannose-binding

Mutagenesis

291

P → A: Decreases transport activity and GDP-mannose-binding

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Sequences

Sequence

Length

Mass (Da)

Tools

P40107-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5C7EE07B05DA8E61
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FASTA

337

37,019

        10         20         30         40         50         60 
MSELKTGHAG HNPWASVANS GPISILSYCG SSILMTVTNK FVVNLKDFNM NFVMLFVQSL 

        70         80         90        100        110        120 
VCTITLIILR ILGYAKFRSL NKTDAKNWFP ISFLLVLMIY TSSKALQYLA VPIYTIFKNL 

       130        140        150        160        170        180 
TIILIAYGEV LFFGGSVTSM ELSSFLLMVL SSVVATWGDQ QAVAAKAASL AEGAAGAVAS 

       190        200        210        220        230        240 
FNPGYFWMFT NCITSALFVL IMRKRIKLTN FKDFDTMFYN NVLALPILLL FSFCVEDWSS 

       250        260        270        280        290        300 
VNLTNNFSND SLTAMIISGV ASVGISYCSG WCVRVTSSTT YSMVGALNKL PIALSGLIFF 

       310        320        330 
DAPRNFLSIL SIFIGFLSGI IYAVAKQKKQ QAQPLRK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast VRG4 gene is required for normal Golgi functions and defines a new family of related genes." Poster J.B., Dean N. J. Biol. Chem. 271:3837-3845(1996) [PubMed: 8632002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c.
[2]	"Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae show defects in Golgi-mediated protein glycosylation, sporulation and detergent resistance." Kanik-Ennulat C., Montalvo E., Neff N. Genetics 140:933-943(1995) [PubMed: 7672592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c.
[3]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed: 9290212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." 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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Vanadate-resistant mutants of Saccharomyces cerevisiae show alterations in protein phosphorylation and growth control." Kanik-Ennulat C., Neff N. Mol. Cell. Biol. 10:898-909(1990) [PubMed: 2137555] [Abstract] Cited for: FUNCTION.
[6]	"Vanadate-resistant yeast mutants are defective in protein glycosylation." Ballou L., Hitzeman R.A., Lewis M.S., Ballou C.E. Proc. Natl. Acad. Sci. U.S.A. 88:3209-3212(1991) [PubMed: 2014241] [Abstract] Cited for: FUNCTION.
[7]	"Yeast glycosylation mutants are sensitive to aminoglycosides." Dean N. Proc. Natl. Acad. Sci. U.S.A. 92:1287-1291(1995) [PubMed: 7877969] [Abstract] Cited for: FUNCTION.
[8]	"Identification of genes controlling growth polarity in the budding yeast Saccharomyces cerevisiae: a possible role of N-glycosylation and involvement of the exocyst complex." Mondesert G., Clarke D.J., Reed S.I. Genetics 147:421-434(1997) [PubMed: 9335583] [Abstract] Cited for: FUNCTION.
[9]	"Isolation of new nonconditional Saccharomyces cerevisiae mutants defective in asparagine-linked glycosylation." Manas P., Olivero I., Avalos M., Hernandez L.M. Glycobiology 7:487-497(1997) [PubMed: 9184829] [Abstract] Cited for: FUNCTION.
[10]	"The VRG4 gene is required for GDP-mannose transport into the lumen of the Golgi in the yeast, Saccharomyces cerevisiae." Dean N., Zhang Y.B., Poster J.B. J. Biol. Chem. 272:31908-31914(1997) [PubMed: 9395539] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of the yeast Saccharomyces cerevisiae." Abe M., Hashimoto H., Yoda K. FEBS Lett. 458:309-312(1999) [PubMed: 10570930] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF SER-278 AND ALA-286.
[12]	"Identification of a conserved motif in the yeast golgi GDP-mannose transporter required for binding to nucleotide sugar." Gao X.-D., Nishikawa A., Dean N. J. Biol. Chem. 276:4424-4432(2001) [PubMed: 11067855] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, MUTAGENESIS OF THR-280; SER-282; GLY-285; ALA-286; LEU-287; ASN-288; LYS-289 AND PRO-291.
[13]	"Progression of the stacked Golgi compartments in the yeast Saccharomyces cerevisiae by overproduction of GDP-mannose transporter." Hashimoto H., Abe M., Hirata A., Noda Y., Adachi H., Yoda K. Yeast 19:1413-1424(2002) [PubMed: 12478588] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]	"Localization of GDP-mannose transporter in the Golgi requires retrieval to the endoplasmic reticulum depending on its cytoplasmic tail and coatomer." Abe M., Noda Y., Adachi H., Yoda K. J. Cell Sci. 117:5687-5696(2004) [PubMed: 15494368] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH RET2.
[17]	"Golgi maturation visualized in living yeast." Losev E., Reinke C.A., Jellen J., Strongin D.E., Bevis B.J., Glick B.S. Nature 441:1002-1006(2006) [PubMed: 16699524] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].

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Cross-references

Sequence databases
	L33915 Genomic DNA. Translation: AAC37468.1. U15599 Genomic DNA. Translation: AAA81537.1. Z72747 Genomic DNA. Translation: CAA96941.1.
PIR	S50238.
RefSeq	NP_011290.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5108N.
IntAct	P40107.
Genome annotation databases
Ensembl	YGL225W. Saccharomyces cerevisiae. [Contig view]
GeneID	852647.
GenomeReviews	Gene locus YGL225W in contig Y13135_GR.
KEGG	sce:YGL225W.
NMPDR	fig\|4932.3.peg.2393.
Organism-specific databases
CYGD	YGL225w.
SGD	S000003193. VRG4.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P40107.
Gene expression databases
ArrayExpress	P40107.
GermOnline	YGL225W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004853. DUF250. IPR004689. UDPgal_transpt. [Graphical view]
Pfam	PF03151. TPT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00803. nst. 1 hit.
ProDom	P40107. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P40107.
ProtoNet	Search...

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Entry information

Entry name

GMT1_YEAST

Accession

Primary (citable) accession number: P40107

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	July 22, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents