ID   CIP2_SCHPO              Reviewed;         576 AA.
AC   Q09868; Q9USF7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=RNA-binding post-transcriptional regulator cip2;
DE   AltName: Full=Csx1-interacting protein 2;
GN   Name=cip2; ORFNames=SPAC12G12.03;
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 [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 [LARGE SCALE GENOMIC DNA] OF 383-570, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH CSX1, SUBCELLULAR
RP   LOCATION, AND PHOSPHORYLATION.
RX   PubMed=16407405; DOI=10.1091/mbc.e05-09-0847;
RA   Martin V., Rodriguez-Gabriel M.A., McDonald W.H., Watt S., Yates J.R. III,
RA   Baehler J., Russell P.;
RT   "Cip1 and Cip2 are novel RNA-recognition-motif proteins that counteract
RT   Csx1 function during oxidative stress.";
RL   Mol. Biol. Cell 17:1176-1183(2006).
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: Regulates global gene expression after oxidative stress.
CC       Interacts and stabilizes mRNAs and may regulate their transition
CC       between different cytoplasmic components after oxidative stress.
CC       {ECO:0000269|PubMed:16407405}.
CC   -!- SUBUNIT: Interacts with csx1. {ECO:0000269|PubMed:16407405}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:16407405, ECO:0000269|PubMed:16823372}.
CC   -!- PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:16407405}.
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DR   EMBL; CU329670; CAA91498.1; -; Genomic_DNA.
DR   EMBL; AB027784; BAA87088.1; -; Genomic_DNA.
DR   PIR; S62534; S62534.
DR   RefSeq; NP_592895.1; NM_001018295.2.
DR   AlphaFoldDB; Q09868; -.
DR   BioGRID; 279571; 38.
DR   IntAct; Q09868; 3.
DR   STRING; 4896.SPAC12G12.03.1; -.
DR   iPTMnet; Q09868; -.
DR   MaxQB; Q09868; -.
DR   PaxDb; Q09868; -.
DR   PRIDE; Q09868; -.
DR   EnsemblFungi; SPAC12G12.03.1; SPAC12G12.03.1:pep; SPAC12G12.03.
DR   GeneID; 2543139; -.
DR   KEGG; spo:SPAC12G12.03; -.
DR   PomBase; SPAC12G12.03; cip2.
DR   VEuPathDB; FungiDB:SPAC12G12.03; -.
DR   eggNOG; KOG0108; Eukaryota.
DR   HOGENOM; CLU_473406_0_0_1; -.
DR   InParanoid; Q09868; -.
DR   OMA; LFYHRTD; -.
DR   PhylomeDB; Q09868; -.
DR   PRO; PR:Q09868; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IGI:PomBase.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IMP:PomBase.
DR   CDD; cd02639; R3H_RRM; 1.
DR   CDD; cd12253; RRM_PIN4_like; 1.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR034186; PIN4-like_RRM.
DR   InterPro; IPR034069; R3H_Cip2.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..576
FT                   /note="RNA-binding post-transcriptional regulator cip2"
FT                   /id="PRO_0000082018"
FT   DOMAIN          232..310
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          355..420
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
SQ   SEQUENCE   576 AA;  62069 MW;  41FBD27201EE7D07 CRC64;
     MAEGTSQRPL TPLSQAFLST NTLSPASSPL TFHSEAASLR RKRSNFFPKL DELNGAQDEE
     MRGLNIPGGS GYLENRYGRD KFTFSDAAVN SAGMGGSGIF SHNNADDGLG DGSSTVLPSS
     LKQMLDPEIS TANNPSAKPR RTRLQTAWKE ATNSAGLSLR SASALDVLKN SGPATTSLLS
     STTYPFDSLN AFNEPSHSHV PNSASSTALS RGMSNSVTLT APPEPDEETI PTAIVIKNIP
     FSLKKEVLFK VFTALDIPRP YAFNYHFDNG VFRGLAFANF HSPEEAKTVV QVLNGYEITG
     RRLRVEWKRQ LPPAERERVE RGKQEKRAVE ERKNQLKSPF SVANIGAGID FDLNDPAILN
     VYSHILLFYY RSDNTNDLVF DSSTTQEERR VAALLASRLN LNHSVTGDGE AKQVVITMPS
     THFTPANNSS ANHSPLMAPN ASTLNPSSLG ASNLSQPSLA NHLSSSGLFD NGLFSSGGLS
     SNFSSLRRPA PSMHLADSIR SLRGLNDSKA FSDIRSMPAT PLELATPFAN LNVSSPLDRN
     ATNSSNTLNG SAMNDYFASL TPSNTGAIGS RTFTKN