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GMT2_YEAS8
ID   GMT2_YEAS8              Reviewed;         341 AA.
AC   C8Z742;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Probable GDP-mannose transporter 2;
DE            Short=GMT 2;
GN   Name=HVG1; Synonyms=YEM9; ORFNames=EC1118_1E8_1442g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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}.
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DR   EMBL; FN393067; CAY79208.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z742; -.
DR   SMR; C8Z742; -.
DR   EnsemblFungi; CAY79208; CAY79208; EC1118_1E8_1420g.
DR   HOGENOM; CLU_025360_1_2_1; -.
DR   Proteomes; UP000000286; Chromosome V, Scaffold EC1118_1E8.
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..341
FT                   /note="Probable GDP-mannose transporter 2"
FT                   /id="PRO_0000391665"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..176
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..251
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   341 AA;  38049 MW;  E4E46B359C640D37 CRC64;
     MSKHKHEWTE SVANSGPASI LSYCASSILM TVTNKFVVNL DNFNMNFVML FVQSLVCTVT
     LCILRIVGVA NFRSLNRTDV KNWFPISLLL VLMIYTSLKS LQYLAVPIYT IFKNLTIILI
     AYGEVLFFGG KVTSMELTSF IMMVLSSVVA TWGDQQAIAI KASSLEDLDQ ELVESTIFVL
     NPGYLWMFTN CISSALFVLI MRKRIRLTNF KDYDTMFYNN VLALPLLLVF SFIMEDWSTK
     NLSVNLSADS LAAMVISGLM SVGISYCSGW CVRVTSSTTY SMVGALNKLP IALAGLVFFD
     APKNFLSFFS IFLGFLSGLL YAVAKQKKIQ QQKVLAATLE K
 
 
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