ID ZIP1_SCHPO Reviewed; 330 AA.
AC Q10424;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Transcription factor zip1;
GN Name=zip1; ORFNames=SPAC25G10.03;
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].
RX PubMed=10102365; DOI=10.1007/s004380050970;
RA Ohmiya R., Kato C., Yamada H., Aiba H., Mizuno T.;
RT "Isolation of multicopy suppressors of the calcium sensitivity of a mutant
RT lacking the bZIP transcription factor Atf1 in fission yeast.";
RL Mol. Gen. Genet. 261:297-306(1999).
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 INTERACTION WITH POF1.
RX PubMed=15660136; DOI=10.1038/sj.emboj.7600536;
RA Harrison C., Katayama S., Dhut S., Chen D., Jones N., Bahler J., Toda T.;
RT "SCF(Pof1)-ubiquitin and its target Zip1 transcription factor mediate
RT cadmium response in fission yeast.";
RL EMBO J. 24:599-610(2005).
RN [4]
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).
CC -!- FUNCTION: Mediates cell growth arrest in response to cadmium exposure,
CC which is essential to maintain cell viability. Regulates cadmium stress
CC specific genes. {ECO:0000269|PubMed:15660136}.
CC -!- SUBUNIT: Interacts with pof1. {ECO:0000269|PubMed:15660136}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Ubiquitinated by pof1.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA94632.1; -; Genomic_DNA.
DR PIR; T38374; T38374.
DR RefSeq; NP_594523.1; NM_001019952.2.
DR AlphaFoldDB; Q10424; -.
DR SMR; Q10424; -.
DR BioGRID; 279160; 34.
DR IntAct; Q10424; 1.
DR STRING; 284812.Q10424; -.
DR iPTMnet; Q10424; -.
DR MaxQB; Q10424; -.
DR PaxDb; 4896-SPAC25G10-03-1; -.
DR EnsemblFungi; SPAC25G10.03.1; SPAC25G10.03.1:pep; SPAC25G10.03.
DR PomBase; SPAC25G10.03; zip1.
DR VEuPathDB; FungiDB:SPAC25G10.03; -.
DR eggNOG; ENOG502S7ZI; Eukaryota.
DR HOGENOM; CLU_874818_0_0_1; -.
DR InParanoid; Q10424; -.
DR OMA; LEMENNW; -.
DR PRO; PR:Q10424; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISM:PomBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14705; bZIP_Zip1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR13044; ACTIVATING TRANSCRIPTION FACTOR ATF 4/5; 1.
DR PANTHER; PTHR13044:SF14; CRYPTOCEPHAL, ISOFORM A; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Cadmium; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..330
FT /note="Transcription factor zip1"
FT /id="PRO_0000076540"
FT DOMAIN 264..327
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 133..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..288
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 292..320
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 146..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 36189 MW; A681434C779DF960 CRC64;
MDFTPNSAIN HLNLKFDDVP VSDDFSKDDL AEQLNVFTNP YFLDLEPSSM LSEGYYGFVS
QPSGSSNSNK QEKNVQQQNP EKISTLQQVK EEEVSNTFSA PLNATGNFSS ANPASIDLAY
LDLQKLLTLP DHSKETQEKT SSQRELFEQK SSVASASKDN VSSSSILQGS ASSKLLPDQS
ARQHQVLVGQ TAIPTSEASS SINNTPLQAP VSSFADQNAF TNPLSTFASP DLASVSSPSL
SSYKGAQSPN ANSKRTKATS AIRTAAEEDK RRRNTAASAR FRIKKKLKEQ QLERTAKELT
EKVAILETRV RELEMENNWL KGLIRPTSNF
//
