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ZRT1_SCHPO
ID   ZRT1_SCHPO              Reviewed;         408 AA.
AC   O94639;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Zinc-regulated transporter 1;
DE   AltName: Full=High-affinity zinc transport protein zrt1;
GN   Name=zrt1; ORFNames=SPBC16D10.06;
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 [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   [2]
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).
RN   [3]
RP   FUNCTION.
RX   PubMed=18203864; DOI=10.1128/ec.00408-07;
RA   Dainty S.J., Kennedy C.A., Watt S., Baehler J., Whitehall S.K.;
RT   "Response of Schizosaccharomyces pombe to zinc deficiency.";
RL   Eukaryot. Cell 7:454-464(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234 AND THR-237, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: High-affinity zinc transport protein. Regulates intracellular
CC       zinc levels. {ECO:0000269|PubMed:18203864}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAB38510.1; -; Genomic_DNA.
DR   PIR; T39570; T39570.
DR   RefSeq; NP_596501.1; NM_001022422.2.
DR   AlphaFoldDB; O94639; -.
DR   BioGRID; 276210; 2.
DR   STRING; 4896.SPBC16D10.06.1; -.
DR   TCDB; 2.A.5.1.8; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR   iPTMnet; O94639; -.
DR   MaxQB; O94639; -.
DR   PaxDb; O94639; -.
DR   PRIDE; O94639; -.
DR   EnsemblFungi; SPBC16D10.06.1; SPBC16D10.06.1:pep; SPBC16D10.06.
DR   GeneID; 2539655; -.
DR   KEGG; spo:SPBC16D10.06; -.
DR   PomBase; SPBC16D10.06; zrt1.
DR   VEuPathDB; FungiDB:SPBC16D10.06; -.
DR   eggNOG; KOG1558; Eukaryota.
DR   HOGENOM; CLU_027089_0_2_1; -.
DR   InParanoid; O94639; -.
DR   OMA; VGMTGGW; -.
DR   PhylomeDB; O94639; -.
DR   PRO; PR:O94639; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IMP:PomBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000006; F:high-affinity zinc transmembrane transporter activity; IDA:PomBase.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0071578; P:zinc ion import across plasma membrane; IDA:PomBase.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR003689; ZIP.
DR   InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR   Pfam; PF02535; Zip; 1.
DR   TIGRFAMs; TIGR00820; zip; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..408
FT                   /note="Zinc-regulated transporter 1"
FT                   /id="PRO_0000316574"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         234
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         237
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   408 AA;  45272 MW;  0EBC0AF53CC3F0CE CRC64;
     MSLNNLSNSY NQYLAQESHQ ILRHLFLNKQ YSPLVKRDDD SSATVTCGGD ANEFNEYGHL
     GYRIGAIFVI LATSLIGMNL PLVLSKITKN RPNVYIEYLY LFARYFGSGV ILATAFIHLL
     APACNKLYDP CLDDLFGGYD WAPGICLISC WFILLLEVLL NRYVEWRFGM EIGDHHGPTL
     GAKQHSHSHE DGAHGVHEHP VYDIEECADG VEHECVKDDL EEVKLEPYTN TDSTDLTTKE
     EARSFLLKQQ LTAFIILESS IILHSVIIGL TTAVSGEEFK TLFPVIIFHQ AFEGCGLGSR
     LAGMAWGPKT AWVPWVLGVI YSLVTPIGMA AGLGVREHWD PLAHGSYAAQ GVLDAISSGI
     LVYAGLVELL AHDFLFSPER ERNWYKLIYL LACSMAGTGV MALLGKWA
 
 
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