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ZHF1_SCHPO
ID   ZHF1_SCHPO              Reviewed;         387 AA.
AC   O13918; P78885;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 3.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Zinc homeostasis factor 1;
GN   Name=zhf1; Synonyms=zhf; ORFNames=SPAC23C11.14;
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 MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
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   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=FY261;
RX   PubMed=11886869; DOI=10.1074/jbc.m201031200;
RA   Clemens S., Bloss T., Vess C., Neumann D., Nies D.H., zur Nieden U.;
RT   "A transporter in the endoplasmic reticulum of Schizosaccharomyces pombe
RT   cells mediates zinc storage and differentially affects transition metal
RT   tolerance.";
RL   J. Biol. Chem. 277:18215-18221(2002).
CC   -!- FUNCTION: Involved in zinc homeostasis, where it plays a role in its
CC       accumulation in the endoplasmic reticulum/nucleus. Also has a role in
CC       the sequestration of cadmium into the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:11886869}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11886869}. Nucleus membrane
CC       {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11886869}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR   EMBL; D89236; BAA13897.1; -; mRNA.
DR   EMBL; CU329670; CAB11166.1; -; Genomic_DNA.
DR   PIR; T38252; T38252.
DR   PIR; T43140; T43140.
DR   RefSeq; NP_593645.1; NM_001019076.2.
DR   AlphaFoldDB; O13918; -.
DR   SMR; O13918; -.
DR   BioGRID; 278538; 24.
DR   STRING; 4896.SPAC23C11.14.1; -.
DR   iPTMnet; O13918; -.
DR   MaxQB; O13918; -.
DR   PaxDb; O13918; -.
DR   EnsemblFungi; SPAC23C11.14.1; SPAC23C11.14.1:pep; SPAC23C11.14.
DR   GeneID; 2542060; -.
DR   KEGG; spo:SPAC23C11.14; -.
DR   PomBase; SPAC23C11.14; zhf1.
DR   VEuPathDB; FungiDB:SPAC23C11.14; -.
DR   eggNOG; KOG1483; Eukaryota.
DR   HOGENOM; CLU_013430_4_3_1; -.
DR   InParanoid; O13918; -.
DR   OMA; IFHHAGI; -.
DR   PhylomeDB; O13918; -.
DR   Reactome; R-SPO-425410; Metal ion SLC transporters.
DR   Reactome; R-SPO-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR   PRO; PR:O13918; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:PomBase.
DR   GO; GO:0006877; P:cellular cobalt ion homeostasis; IMP:PomBase.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:PomBase.
DR   GO; GO:0140209; P:zinc ion import into endoplasmic reticulum; IMP:PomBase.
DR   GO; GO:0062111; P:zinc ion import into organelle; IDA:PomBase.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF160240; SSF160240; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Ion transport; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..387
FT                   /note="Zinc homeostasis factor 1"
FT                   /id="PRO_0000206104"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          195..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        340
FT                   /note="T -> S (in Ref. 1; BAA13897)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  42941 MW;  2526EA6559F92145 CRC64;
     MFDLARQTRI ILLLGIDVTF FFIEIITGYA IDSLALIADS FHMLNDIVSL LVALWATRLA
     HSTSHEPKYT YGWQRAEILG ALSNGVFLIA LCMFIFMEAI ERFIEPPSVS NPTLMFFVGS
     LGLLSNFVGI FLFHDHGHDH PHTHTAQNYD FPEEDDIESV LPSTIVHRCN TSQQEVSHTH
     TQVADSATES SPLLSYTGNH NGAGTSKPVN NHGSIEQDAP KQTKKRNLNM HGVFLHVLGD
     ALGNIGVISA ALFIKYTDYS WRFLFDPCIS ILLTFIILFS AIPLCKSAAL ILLQVAPQSI
     KLDDVSNLIN HLDGVESVHE LHIWQLSDVK LIATVHVCVT LPDDKGESYT KLTTDIRNVL
     QSFGIYDVTI QPEFANHPLL CDQGSSS
 
 
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