GMT1_YEAS1
ID GMT1_YEAS1 Reviewed; 337 AA.
AC B3LHR7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 52.
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; ORFNames=SCRG_01209;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Recycles between the Golgi apparatus and the
CC endoplasmic reticulum. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC {ECO:0000305}.
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DR EMBL; CH408044; EDV10425.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LHR7; -.
DR SMR; B3LHR7; -.
DR EnsemblFungi; EDV10425; EDV10425; SCRG_01209.
DR HOGENOM; CLU_025360_1_2_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..337
FT /note="GDP-mannose transporter 1"
FT /id="PRO_0000391672"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..51
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..119
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..180
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..252
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..304
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
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"
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
