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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
 
 
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