GMT1_VANPO
ID GMT1_VANPO Reviewed; 332 AA.
AC A7TR80;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=GDP-mannose transporter 1;
DE Short=GMT 1;
GN Name=VRG4-1; ORFNames=Kpol_423p1;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: Involved in the import of GDP-mannose from the cytoplasm into
CC the Golgi lumen. {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}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC {ECO:0000305}.
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DR EMBL; DS480472; EDO15213.1; -; Genomic_DNA.
DR RefSeq; XP_001643071.1; XM_001643021.1.
DR AlphaFoldDB; A7TR80; -.
DR SMR; A7TR80; -.
DR STRING; 436907.A7TR80; -.
DR EnsemblFungi; EDO15213; EDO15213; Kpol_423p1.
DR GeneID; 5543294; -.
DR KEGG; vpo:Kpol_423p1; -.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; A7TR80; -.
DR OMA; IQSTVCV; -.
DR OrthoDB; 1093260at2759; -.
DR PhylomeDB; A7TR80; -.
DR Proteomes; UP000000267; 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; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..332
FT /note="GDP-mannose transporter 1"
FT /id="PRO_0000333538"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..49
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..110
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..177
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..248
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..301
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 36913 MW; D89C90E7D87C701A CRC64;
MSDLKLAENN FWGNVANSGP ISIFSYCASS ILMTVTNKFV VNLKDFNMNF VMLFVQSFVC
TLLLVILKTL GYAKFRPFNK TDAKNWFPIS VLLVIMIYTS SKALQFLAVP IYTIFKNLTI
ILIAYGEVIY FGGKVTSMEL SSFILMVLSS VVATWGDKQA MQAKSLVESD VTVPVVPFNV
GYLWMFANCI SSAAFVLIMR KRIKLTNFKD FDTMFYNNVL ALPILLLFSF CIEDWSSTNL
STSFTANSFT AMIISGMASV GISYCSGWCV RVTSSTTYSM VGALNKLPIA LSGLIFFDAP
KNFLSIFSIF LGFLAGIVYA VAKQKKNQNP EK