GMT2_VANPO
ID GMT2_VANPO Reviewed; 332 AA.
AC A7TES5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=GDP-mannose transporter 2;
DE Short=GMT 2;
GN Name=VRG4-2; ORFNames=Kpol_1050p28;
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; DS480381; EDO19171.1; -; Genomic_DNA.
DR RefSeq; XP_001647029.1; XM_001646979.1.
DR AlphaFoldDB; A7TES5; -.
DR SMR; A7TES5; -.
DR STRING; 436907.A7TES5; -.
DR EnsemblFungi; EDO19171; EDO19171; Kpol_1050p28.
DR GeneID; 5547502; -.
DR KEGG; vpo:Kpol_1050p28; -.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; A7TES5; -.
DR OMA; WCIRKTS; -.
DR OrthoDB; 1093260at2759; -.
DR PhylomeDB; A7TES5; -.
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 2"
FT /id="PRO_0000333539"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..47
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..108
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..174
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..248
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..300
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 36748 MW; D2B4AD85B93B227C CRC64;
MSSLKVSQQD KKWVNSGSVA ILAYCASSIL MTITNKVVMS DRTFNMNFLL LFIQSLVCVI
TLLVLKVLGS VNFRSFNKTD ARNWFPISIC LVLMIFTSSK SLQYLSVPVY TIFKNLTIIV
IAYGEVLFFG SSVGNMELGS FALMIVSSLI AAHGDYLHSV ERLKKMLGPN VSFSFIVNIG
YFWIAANCFA SALFVLLMRK RIQVTNFKDF DTMFYNNVLS LPLLLLGSYL FEDWSQENLL
PHVDIDNLST MIISGLASVA ISYCSGWCVR VTSSTTYSMV GALNKLPIAL TGFLFNDAAR
NLSSAASILL GFASGIIYAV AKQKKLQNSE KI
