ID   ZFS1_SCHPO              Reviewed;         404 AA.
AC   P47979;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Zinc finger protein zfs1;
DE   AltName: Full=Multicopy suppressor of overexpressed cyr1 protein 4;
GN   Name=zfs1; Synonyms=moc4; ORFNames=SPBC1718.07c;
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], AND SUBCELLULAR LOCATION.
RX   PubMed=8534915; DOI=10.1091/mbc.6.9.1185;
RA   Kanoh J., Sugimoto A., Yamamoto M.;
RT   "Schizosaccharomyces pombe zfs1+ encoding a zinc-finger protein functions
RT   in the mating pheromone recognition pathway.";
RL   Mol. Biol. Cell 6:1185-1195(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH MOC3.
RX   PubMed=16273369; DOI=10.1007/s00294-005-0028-z;
RA   Goldar M.M., Jeong H.T., Tanaka K., Matsuda H., Kawamukai M.;
RT   "Moc3, a novel Zn finger type protein involved in sexual development, ascus
RT   formation, and stress response of Schizosaccharomyces pombe.";
RL   Curr. Genet. 48:345-355(2005).
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   FUNCTION.
RX   PubMed=10462526; DOI=10.1242/jcs.112.18.3103;
RA   Beltraminelli N., Murone M., Simanis V.;
RT   "The S. pombe zfs1 gene is required to prevent septation if mitotic
RT   progression is inhibited.";
RL   J. Cell Sci. 112:3103-3114(1999).
RN   [5]
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).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF HIS-351 AND CYS-370.
RX   PubMed=18042546; DOI=10.1074/jbc.m707154200;
RA   Cuthbertson B.J., Liao Y., Birnbaumer L., Blackshear P.J.;
RT   "Characterization of zfs1 as an mRNA-binding and -destabilizing protein in
RT   Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 283:2586-2594(2008).
CC   -!- FUNCTION: Binds to specific AU-rich elements (ARE) in the 3'-
CC       untranslated region of target mRNAs and promotes their degradation.
CC       Binds to ARE present in the arz1 mRNA and stimulates the rate of arz1
CC       mRNA decay. Required for coordination of septum formation with exit
CC       from mitosis. Involved in the mating response pathway. Induces sexual
CC       development and ascus formation. {ECO:0000269|PubMed:10462526,
CC       ECO:0000269|PubMed:16273369, ECO:0000269|PubMed:18042546}.
CC   -!- SUBUNIT: Interacts with moc3. {ECO:0000269|PubMed:16273369}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:8534915}.
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DR   EMBL; D49913; BAA08654.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB75997.1; -; Genomic_DNA.
DR   PIR; T50335; T50335.
DR   RefSeq; NP_596453.1; NM_001022372.2.
DR   AlphaFoldDB; P47979; -.
DR   SMR; P47979; -.
DR   BioGRID; 276502; 310.
DR   IntAct; P47979; 19.
DR   MINT; P47979; -.
DR   STRING; 4896.SPBC1718.07c.1; -.
DR   iPTMnet; P47979; -.
DR   MaxQB; P47979; -.
DR   PaxDb; P47979; -.
DR   PRIDE; P47979; -.
DR   EnsemblFungi; SPBC1718.07c.1; SPBC1718.07c.1:pep; SPBC1718.07c.
DR   GeneID; 2539958; -.
DR   KEGG; spo:SPBC1718.07c; -.
DR   PomBase; SPBC1718.07c; zfs1.
DR   VEuPathDB; FungiDB:SPBC1718.07c; -.
DR   eggNOG; KOG1677; Eukaryota.
DR   HOGENOM; CLU_681784_0_0_1; -.
DR   InParanoid; P47979; -.
DR   OMA; CCFLHDE; -.
DR   Reactome; R-SPO-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR   Reactome; R-SPO-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR   PRO; PR:P47979; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:1905762; F:CCR4-NOT complex binding; IDA:PomBase.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0044692; F:exoribonuclease activator activity; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:PomBase.
DR   GO; GO:0062104; F:pumilio-response element binding; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; EXP:PomBase.
DR   GO; GO:0140610; F:RNA sequestering activity; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IGI:PomBase.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:PomBase.
DR   GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
DR   GO; GO:0110044; P:regulation of cell cycle switching, mitotic to meiotic cell cycle; IGI:PomBase.
DR   InterPro; IPR045877; ZFP36-like.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR12547; PTHR12547; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; SSF90229; 2.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..404
FT                   /note="Zinc finger protein zfs1"
FT                   /id="PRO_0000089175"
FT   ZN_FING         326..354
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         364..392
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          134..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         351
FT                   /note="H->I: Abolishes mRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18042546"
FT   MUTAGEN         370
FT                   /note="C->G: Abolishes mRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18042546"
SQ   SEQUENCE   404 AA;  43435 MW;  DFBCDDC23BAFDFF8 CRC64;
     MVYSPMSRPQ VPLAFRQWPP YNYKSDPLVN SKLSQSTTSV NAGPSLISPS FLDSYANSSS
     LLHKPSTNLG SLKTSSLLAS DEVFPSSVMP QLRPLDSSLS VSPEMDGWPW HHNSSSNPQG
     YAWTPSLLSS NATSYLHSGS SPHGNTSNHP SPISSLESLP SRSSTGSGSL DFSGLANLHD
     DSKSLAMSLN MAGVPVSVDE NSQTSFPFVH GQPESTMSRK PKLCVQSKSM TNIRNSVAKP
     SLVRQSHSAG VIPIKPTASN ASIRNAPSNL SKQFSPSGNS PLTEASKPFV PQPSAAGDFR
     QAKGSASHPH GSGSSNGVAP NGKRALYKTE PCKNWQISGT CRYGSKCQFA HGNQELKEPP
     RHPKYKSERC RSFMMYGYCP YGLRCCFLHD ESNAQKSATI KQSP