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FEP1_SCHPO
ID   FEP1_SCHPO              Reviewed;         564 AA.
AC   Q10134;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 155.
DE   RecName: Full=Iron-sensing transcriptional repressor {ECO:0000305};
DE   AltName: Full=Transcription factor gaf2;
DE            Short=Gaf-2;
GN   Name=fep1 {ECO:0000303|PubMed:11956219};
GN   Synonyms=gaf2 {ECO:0000303|PubMed:8799335};
GN   ORFNames=SPAC23E2.01 {ECO:0000312|PomBase:SPAC23E2.01};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11956219; DOI=10.1074/jbc.m202682200;
RA   Pelletier B., Beaudoin J., Mukai Y., Labbe S.;
RT   "Fep1, an iron sensor regulating iron transporter gene expression in
RT   Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 277:22950-22958(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8799335; DOI=10.1080/15216549600201131;
RA   Hoe K.-L., Won M.-S., Yoo O.-J.J., Yoo H.-S.;
RT   "Molecular cloning of GAF2, a Schizosaccharomyces pombe GATA factor, which
RT   has two zinc-finger sequences.";
RL   Biochem. Mol. Biol. Int. 39:127-135(1996).
RN   [3]
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   [4]
RP   INTERACTION WITH TUP11.
RX   PubMed=14668334; DOI=10.1074/jbc.m312787200;
RA   Znaidi S., Pelletier B., Mukai Y., Labbe S.;
RT   "The Schizosaccharomyces pombe corepressor Tup11 interacts with the iron-
RT   responsive transcription factor Fep1.";
RL   J. Biol. Chem. 279:9462-9474(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=12888492; DOI=10.1093/nar/gkg647;
RA   Pelletier B., Beaudoin J., Philpott C.C., Labbe S.;
RT   "Fep1 represses expression of the fission yeast Schizosaccharomyces pombe
RT   siderophore-iron transport system.";
RL   Nucleic Acids Res. 31:4332-4344(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP   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).
RN   [7]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=25733668; DOI=10.1074/jbc.m115.642058;
RA   Mourer T., Jacques J.F., Brault A., Bisaillon M., Labbe S.;
RT   "Shu1 is a cell-surface protein involved in iron acquisition from heme in
RT   Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 290:10176-10190(2015).
RN   [8]
RP   FUNCTION.
RX   PubMed=29549126; DOI=10.1074/jbc.ra118.002132;
RA   Normant V., Mourer T., Labbe S.;
RT   "The major facilitator transporter Str3 is required for low-affinity heme
RT   acquisition in Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 293:6349-6362(2018).
CC   -!- FUNCTION: Transcriptional repressor that binds the consensus promoter
CC       sequence 5'-[AT]GATAA-3' during iron-replete conditions to down-
CC       regulate transcription of target genes (PubMed:11956219,
CC       PubMed:25733668). Represses the expression of the iron transporter fio1
CC       in response to high iron concentrations (PubMed:11956219,
CC       PubMed:25733668). Also represses the expression of str1, str2 and str3
CC       (PubMed:12888492, PubMed:29549126). Represses the expression of shu1 in
CC       presence of iron (PubMed:25733668). {ECO:0000269|PubMed:11956219,
CC       ECO:0000269|PubMed:12888492, ECO:0000269|PubMed:25733668,
CC       ECO:0000269|PubMed:29549126}.
CC   -!- ACTIVITY REGULATION: Activated by iron. {ECO:0000269|PubMed:25733668}.
CC   -!- SUBUNIT: Interacts with tup11. {ECO:0000269|PubMed:14668334}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11956219}.
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DR   EMBL; AY099027; AAM29187.1; -; Genomic_DNA.
DR   EMBL; AJ457978; CAD30004.1; -; Genomic_DNA.
DR   EMBL; L29051; AAB38022.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA93113.1; -; Genomic_DNA.
DR   PIR; T38291; T38291.
DR   PIR; T43298; T43298.
DR   RefSeq; NP_592936.1; NM_001018337.2.
DR   AlphaFoldDB; Q10134; -.
DR   BioGRID; 278023; 68.
DR   IntAct; Q10134; 1.
DR   STRING; 4896.SPAC23E2.01.1; -.
DR   iPTMnet; Q10134; -.
DR   MaxQB; Q10134; -.
DR   PaxDb; Q10134; -.
DR   PRIDE; Q10134; -.
DR   EnsemblFungi; SPAC23E2.01.1; SPAC23E2.01.1:pep; SPAC23E2.01.
DR   GeneID; 2541522; -.
DR   KEGG; spo:SPAC23E2.01; -.
DR   PomBase; SPAC23E2.01; fep1.
DR   VEuPathDB; FungiDB:SPAC23E2.01; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   HOGENOM; CLU_524924_0_0_1; -.
DR   InParanoid; Q10134; -.
DR   OMA; NSLLCNA; -.
DR   PhylomeDB; Q10134; -.
DR   Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:Q10134; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:PomBase.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0005506; F:iron ion binding; IDA:PomBase.
DR   GO; GO:0140482; F:iron sensor activity; IDA:PomBase.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:PomBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:PomBase.
DR   GO; GO:1905569; P:negative regulation of ferrichrome biosynthetic process; IMP:PomBase.
DR   GO; GO:0097739; P:negative regulation of ferrichrome biosynthetic process in response to iron; IC:GOC-OWL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0034396; P:negative regulation of transcription from RNA polymerase II promoter in response to iron; IMP:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00202; ZnF_GATA; 2.
DR   Gene3D; 3.30.50.10; -; 2.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071; PTHR10071; 2.
DR   Pfam; PF00320; GATA; 2.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 2.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..564
FT                   /note="Iron-sensing transcriptional repressor"
FT                   /id="PRO_0000083476"
FT   ZN_FING         12..36
FT                   /note="GATA-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   ZN_FING         172..196
FT                   /note="GATA-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          100..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        182
FT                   /note="L -> K (in Ref. 2; AAB38022)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  60611 MW;  0ED74CE0B6E210B7 CRC64;
     MAAKPAPFGQ SCSNCHKTTT SLWRRGPDNS LLCNACGLYQ KHRKHARPVK SEDLKDISPL
     IQQVCKNGTC AGDGFCNGTG GSASCTGCPA LNNRIRSLNA SKSQSGRKSL SPNPSSVPSS
     TETKASPTPL ESKPQIVSDT TTETSNGTSR RRSSHNQHED SSPPHEPSVT FCQNCATTNT
     PLWRRDESGN PICNACGLYY KIHGVHRPVT MKKAIIKRRK RLVFNGNANE SQHNLKRMSS
     GDSGSSVKQQ STRDGPFSKS FPNGNGHASG NSGEGLAEHG MNTGVLPPAS TFPSYNSNFT
     GFLPSSFNPS PLMTLSRLAA GEPDNNGKVY YSYGPTQEQS ILPLPENKHE GLPPYQNEYV
     PNGIRANQVV YPGQLVAVGN DSSKQLSEST TSNTDNNGVA TANQSNPLGM KFHLPPILPV
     GESVCLPPRT SAKPRIAEGI ASLLNPEEPP SNSDKQPSMS NGPKSEVSPS QSQQAPLIQS
     STSPVSLQFP PEVQGSNVDK RNYALNVLSQ LRSQHDLMIQ ELHNLNQHIQ QIDEWLRSSD
     NENMASEHIK SSTPAVVASG ALQT
 
 
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