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GMT_USTMA
ID   GMT_USTMA               Reviewed;         471 AA.
AC   Q4PFQ1; A0A0D1CDI8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=GDP-mannose transporter;
DE            Short=GMT;
GN   Name=VRG4; ORFNames=UMAG_01062;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) 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   -!- 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; CM003141; KIS71152.1; -; Genomic_DNA.
DR   RefSeq; XP_011387028.1; XM_011388726.1.
DR   AlphaFoldDB; Q4PFQ1; -.
DR   SMR; Q4PFQ1; -.
DR   STRING; 5270.UM01062P0; -.
DR   EnsemblFungi; KIS71152; KIS71152; UMAG_01062.
DR   GeneID; 23562184; -.
DR   KEGG; uma:UMAG_01062; -.
DR   VEuPathDB; FungiDB:UMAG_01062; -.
DR   eggNOG; KOG1444; Eukaryota.
DR   HOGENOM; CLU_025360_1_2_1; -.
DR   InParanoid; Q4PFQ1; -.
DR   OMA; IRVWIPV; -.
DR   OrthoDB; 1093260at2759; -.
DR   Proteomes; UP000000561; Chromosome 2.
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:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IBA:GO_Central.
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..471
FT                   /note="GDP-mannose transporter"
FT                   /id="PRO_0000333537"
FT   TOPO_DOM        1..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..101
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..279
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..354
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..408
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  51117 MW;  DD52FF54195B05BB CRC64;
     MSSGSRSFFT PQETRLELPQ GAAHQTPDIT RPASPSENDR APFLNGGPSD AREDVRMGAK
     ALRNDSEKPA VGIMALAPIL CYCAASITMT VVNKFTVSGR GFNMNLLVLL IQSTVGVTCV
     WIAERAGLIQ LRGLNAKDAW NWMPLSIMLV FVIWTGSKAL QYLNISVYTI FKNLTIILIA
     YGEVMWFGGR VTRIVLCSFL FMVLSSVIAA WSDISNVFAI GNLSMPHTPD SIMGGMAKDP
     ITGALFPAFD PLKTEKDAIN AQLQSASAND VIEGFQGYGL LSSGYVWMAL NCICSATYVL
     LMRKRIKVTG FKDWDTMFYN NFLSIPVLLL MSFLVEDWSY ANLHKNFPDD KQTKLISAIV
     FSGACAILIS YTTAWCIRAT SSTTYSMVGA LNKLPVALSG MVFFHDPPVT FSSVSAIAVG
     FFAGLVYAFG KNKQAEAAKL GGHASANGSS SMSGSKDGSS LPMHTFNDRK D
 
 
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