ID   GMT2_YEAS1              Reviewed;         249 AA.
AC   B3LS51;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Probable GDP-mannose transporter 2;
DE            Short=GMT 2;
GN   Name=HVG1; Synonyms=YEM9; ORFNames=SCRG_04508;
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. {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}.
CC   -!- CAUTION: This is a truncated version of GDP-mannose transporter 2. This
CC       strain has a stop codon in position 73, which disrupts the gene coding
CC       for this protein and produces two ORFs. A contiguous sequence for GDP-
CC       mannose transporter 2 can be found in strain Lalvin EC1118 (AC C8Z742).
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408052; EDV08867.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LS51; -.
DR   SMR; B3LS51; -.
DR   EnsemblFungi; EDV08867; EDV08867; SCRG_04508.
DR   HOGENOM; CLU_025360_1_1_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; IPR000620; EamA_dom.
DR   InterPro; IPR038736; Vrg4-like.
DR   PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR   Pfam; PF00892; EamA; 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..249
FT                   /note="Probable GDP-mannose transporter 2"
FT                   /id="PRO_0000391669"
FT   TOPO_DOM        1..15
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..84
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..159
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..211
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   249 AA;  27688 MW;  53A0FB1F5049A6BC CRC64;
     MIYTSSKSLQ YLAVPIYTIF KNLTIILIAY GEVLFFGGKV TSMELTSFIM MVLSSVVATW
     GDQQAIAIKA SSLEDLDQEL VESTIFVLNP GYLWMFTNCI SSALFVLIMR KRIRLTNFKD
     YDTMFYNNVL ALPLLLVFSF IMEDWSTKNL SVNLSADSLA AMVISGLMSV GISYCSGWCV
     RVTSSTTYSM VGALNKLPIA LAGLVFFDAP KNFLSFFSIF LGFLSGLLYA VAKQKKIQQQ
     KVLAATLEK