CPS3_SCHPO
ID CPS3_SCHPO Reviewed; 583 AA.
AC P41000; O14117;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein cps3;
DE AltName: Full=Meiotically up-regulated gene 188 protein;
GN Name=cps3; Synonyms=mug188, scp3; ORFNames=SPAC3A11.02;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-583.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7857672; DOI=10.1266/jjg.69.671;
RA Ishiguro J., Uhara Y., Kawahara K.;
RT "Molecular cloning and characterization of a fission yeast gene responsible
RT for supersensitivity to the spindle poison, isopropyl N-3-chlorophenyl
RT carbamate.";
RL Jpn. J. Genet. 69:671-678(1994).
RN [3]
RP SEQUENCE REVISION.
RA Ishiguro J.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
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).
CC -!- FUNCTION: Responsible for supersensitivity to the spindle poison,
CC isopropyl N-3-chlorophenyl carbamate. Has a role in meiosis.
CC {ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB16391.1; -; Genomic_DNA.
DR EMBL; AB017490; BAA33049.1; -; Genomic_DNA.
DR PIR; T11624; T11624.
DR RefSeq; NP_594201.1; NM_001019625.2.
DR AlphaFoldDB; P41000; -.
DR BioGRID; 279488; 1.
DR STRING; 4896.SPAC3A11.02.1; -.
DR iPTMnet; P41000; -.
DR MaxQB; P41000; -.
DR PaxDb; P41000; -.
DR PRIDE; P41000; -.
DR EnsemblFungi; SPAC3A11.02.1; SPAC3A11.02.1:pep; SPAC3A11.02.
DR GeneID; 2543054; -.
DR KEGG; spo:SPAC3A11.02; -.
DR PomBase; SPAC3A11.02; cps3.
DR VEuPathDB; FungiDB:SPAC3A11.02; -.
DR eggNOG; KOG1039; Eukaryota.
DR HOGENOM; CLU_468647_0_0_1; -.
DR InParanoid; P41000; -.
DR OMA; KSLQHVP; -.
DR Reactome; R-SPO-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P41000; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11224; PTHR11224; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..583
FT /note="Protein cps3"
FT /id="PRO_0000213911"
FT ZN_FING 35..62
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 64..91
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 62808 MW; 905022C7C06E4271 CRC64;
MTKKNAFKNS EDMKKYHLSE FNSEATSLTR PSPKSLQHVP CKFFRQGTCT SGKNCIFSHD
LELATEKTIC KYFQKGNCKF GSKCALEHVL PDGRKVKTRA FAPSTTAMGS SSQNISAAPM
ANIISNNDKI LPMTTMASAT ASEEKNRIKD EALVIKKEES NVAIPSEVTV AANAFSASTE
DVYSIVGDSL SKKASVKDFS DVTGIETIPA YVEATNGSST VRSPHAKRSL SSISVKSSTS
PFSGSKFLSS SSYPHTPEAH LNSNHISPAS FGSGIRTRNI FNPESMSLGL KPPILNRSYS
ASMAPGFSMN TFTATGNLGR PTKSPSVPTS VGSNKSRKFP GINGSTLTAT PSSLENLYPL
SSRRSVPNLI SSLGTSPSTF SSQFLKSTDR THSFTSKLQS FNPVGTSLLA SSLGTSQEDS
VNYDIPDEFA NEEDFIPNSL QELLTPEELE RKMSHGDEAV SSSSASRFMS KVSSNLNSGN
PTPYNSYNGT PTSSRFVAFF DRHRQESEKA TPPSLNKVSQ EPLTATTPKN LGNLTAISET
LENGQTLKSN MASSIEKSKT STEVVASYDT TLDEETQFQM DEA
