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ITR1_SCHPO
ID   ITR1_SCHPO              Reviewed;         575 AA.
AC   Q10286; Q9UU75;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Myo-inositol transporter 1;
GN   Name=itr1; ORFNames=SPAC4F8.15, SPAC7D4.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=9560432; DOI=10.1007/s002940050334;
RA   Niederberger C., Graub R., Schweingruber A.-M., Fankhauser H., Rusu M.,
RA   Poitelea M., Edenharter L., Schweingruber M.E.;
RT   "Exogenous inositol and genes responsible for inositol transport are
RT   required for mating and sporulation in Shizosaccharomyces pombe.";
RL   Curr. Genet. 33:255-261(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 136-280, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Transporter for myo-inositol. {ECO:0000269|PubMed:9560432}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC         Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC         Evidence={ECO:0000305|PubMed:9560432};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; X98622; CAA67211.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16718.1; -; Genomic_DNA.
DR   EMBL; AB027770; BAA87074.1; -; Genomic_DNA.
DR   PIR; T43400; T43400.
DR   RefSeq; NP_593858.2; NM_001019287.2.
DR   AlphaFoldDB; Q10286; -.
DR   SMR; Q10286; -.
DR   BioGRID; 279577; 4.
DR   STRING; 4896.SPAC4F8.15.1; -.
DR   iPTMnet; Q10286; -.
DR   MaxQB; Q10286; -.
DR   PaxDb; Q10286; -.
DR   PRIDE; Q10286; -.
DR   EnsemblFungi; SPAC4F8.15.1; SPAC4F8.15.1:pep; SPAC4F8.15.
DR   GeneID; 2543145; -.
DR   KEGG; spo:SPAC4F8.15; -.
DR   PomBase; SPAC4F8.15; itr1.
DR   VEuPathDB; FungiDB:SPAC4F8.15; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_5_1; -.
DR   InParanoid; Q10286; -.
DR   OMA; VWILYMS; -.
DR   PhylomeDB; Q10286; -.
DR   Reactome; R-SPO-429593; Inositol transporters.
DR   PRO; PR:Q10286; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
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:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005366; F:myo-inositol:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1904679; P:myo-inositol import across plasma membrane; IGI:PomBase.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..575
FT                   /note="Myo-inositol transporter 1"
FT                   /id="PRO_0000050453"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..129
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..156
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..186
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..246
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..376
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        398..400
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..441
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..486
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..510
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        511..531
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        532..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   575 AA;  62758 MW;  3B7C5EFF86C596AE CRC64;
     MSISSKDFQN VTSAGFADDT FAADTFAADK KSPFESSVFE NKTQVLPVDS VSRLSNGARS
     RSNSNISLSE PHALNDTVED QPVSKWVWVL AFAAGIGGLL FGYDTGVISG ALVVIGTSLG
     GHELTNGGKE FITSATSLGA LLGGIIAGAL ADFFGRKPVI AIASIIIIVG SIVQVTAHHL
     WHMIVGRFVI GWGVGIASLI IPLYLSEIAP SKIRGRLVII YVLLITAGQV IAYGIDTAFE
     HVHNGWRWMV GLAMVPAAFQ LFILIWLPES PRLLVKKERS QEAYNTLARI YPTAHPYEIK
     TKLYLIQEGV RDPFSGSRWQ KIVKTFKELY FNPSNFRALI LACGLQAMQQ LSGFNSLMYF
     SSTIFEVVGF NNPTATGLII AATNFVFTIV AFGVIDFFGR RILLLLTVWG MIAALIVCAV
     AFHFLPKDEN GNYTSGQSNA WAIVVLISMI VYVASYASGL GNLPWQQSEL FPMSVRGLGT
     GMSTAVNWAG NLGIGASFLT LMSEITPTGT FALYGGLCFL GWLGALFCYP DLTDYTIEEI
     GELLKHGFGV RESMRHLKRV RQERAWSRED KEQNN
 
 
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