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PRZ1_SCHPO
ID   PRZ1_SCHPO              Reviewed;         681 AA.
AC   Q09838;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Transcriptional regulator prz1;
DE   AltName: Full=Pbp1-responsive zinc finger protein 1;
GN   Name=prz1; ORFNames=SPAC4G8.13c;
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   FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=12637524; DOI=10.1074/jbc.m212900200;
RA   Hirayama S., Sugiura R., Lu Y., Maeda T., Kawagishi K., Yokoyama M.,
RA   Tohda H., Giga-Hama Y., Shuntoh H., Kuno T.;
RT   "Zinc finger protein Prz1 regulates Ca2+ but not Cl- homeostasis in fission
RT   yeast. Identification of distinct branches of calcineurin signaling pathway
RT   in fission yeast.";
RL   J. Biol. Chem. 278:18078-18084(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-546, 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: Involved in the regulation of calcium ion homeostasis. Binds
CC       to the calcineurin-dependent response element. Transcriptionally
CC       regulates pmc1. {ECO:0000269|PubMed:12637524}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12637524}. Cytoplasm
CC       {ECO:0000269|PubMed:12637524}.
CC   -!- PTM: Phosphorylated. Dephosphorylated by calcineurin which leads to
CC       rapid translocation from the cytoplasm to the nucleus.
CC       {ECO:0000269|PubMed:12637524, ECO:0000269|PubMed:18257517}.
CC   -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAA91214.1; -; Genomic_DNA.
DR   PIR; T38858; S62490.
DR   RefSeq; NP_593073.1; NM_001018471.2.
DR   AlphaFoldDB; Q09838; -.
DR   SMR; Q09838; -.
DR   BioGRID; 278297; 369.
DR   STRING; 4896.SPAC4G8.13c.1; -.
DR   iPTMnet; Q09838; -.
DR   MaxQB; Q09838; -.
DR   PaxDb; Q09838; -.
DR   PRIDE; Q09838; -.
DR   EnsemblFungi; SPAC4G8.13c.1; SPAC4G8.13c.1:pep; SPAC4G8.13c.
DR   GeneID; 2541806; -.
DR   KEGG; spo:SPAC4G8.13c; -.
DR   PomBase; SPAC4G8.13c; prz1.
DR   VEuPathDB; FungiDB:SPAC4G8.13c; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_403405_0_0_1; -.
DR   InParanoid; Q09838; -.
DR   OMA; MNTHTNY; -.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q09838; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0071889; F:14-3-3 protein binding; IPI:PomBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IMP:PomBase.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:PomBase.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:PomBase.
DR   GO; GO:0071277; P:cellular response to calcium ion; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..681
FT                   /note="Transcriptional regulator prz1"
FT                   /id="PRO_0000046814"
FT   ZN_FING         570..594
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         600..622
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         628..650
FT                   /note="C2H2-type 3; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   681 AA;  74190 MW;  BB912939969503C8 CRC64;
     MERQRSEEAN RRFKDLNPSS LYDNLSKPDL GGSSELHTYM NDTSLADIPL FEDTLASEVS
     SSLISNPSKN NIQHLHPNTS EPFKTSSKSD EYDSYPRTGN VPTFSFTELN DTSVSGFGSQ
     AVFENSVSPL SNPSNSPQAF DLTQGSSSTH NANDFTVNNV GSRRQSIYEF NIGIPSSNID
     SSQFLPVSRA IAASEISPSS SPQLLTSFLP SGSVSNPSSP YLQGSVGALY EADAFNFVDV
     MSQASGTEVD SERFPSVDFE DPSLLMENQQ NITGTGSFAD YLQPPSSGSL GAFTNASPGE
     SNTGIDFDTD NTNLNPSVDL LSNHSTPSFI FENSPSAEFS HQSSPYLVPN SGRTLNSENA
     RESTIRSVNS PFSEDHADAS LTTHVFDPIS PTALSNSVLN YDSNNFSGTP QINVVPSSPS
     KSQSGPSLPA NPLLQTDISI TYSQSASPVS GQPAMNENSY DLQNANLCAP EMSPTYTARH
     RSNSAGSRFD AYEPIPQLYT HFSHSSECLS VNQDTELLGK IENDNSKSND YLSVRNTRPR
     SRSLNSLVGN KSENSSSSKA KSESKSQGNY VCTFAGCNKR FTRAYNLKSH MNTHTNYRPF
     QCSICKKSFA RQHDKRRHEQ LHTGIKAFAC VTCNQRFARM DALNRHYKSE VGQNCLRTAT
     ERGIQVPPSR KTAVASTSKQ K
 
 
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