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
