CIP1_SCHPO
ID CIP1_SCHPO Reviewed; 490 AA.
AC O42923;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=RNA-binding post-transcriptional regulator cip1;
DE AltName: Full=Csx1-interacting protein 1;
GN Name=cip1; ORFNames=SPBC16A3.18;
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 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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-41; SER-49; SER-86;
RP SER-141; SER-397; SER-401; SER-427; THR-431; SER-435; SER-456 AND SER-466,
RP AND 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: 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:16407405,
CC ECO:0000269|PubMed:16823372}.
CC -!- PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:16407405,
CC ECO:0000269|PubMed:18257517}.
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DR EMBL; CU329671; CAA16869.1; -; Genomic_DNA.
DR PIR; T39534; T39534.
DR RefSeq; NP_596771.1; NM_001023792.2.
DR AlphaFoldDB; O42923; -.
DR SMR; O42923; -.
DR BioGRID; 276373; 40.
DR IntAct; O42923; 3.
DR STRING; 4896.SPBC16A3.18.1; -.
DR iPTMnet; O42923; -.
DR MaxQB; O42923; -.
DR PaxDb; O42923; -.
DR PRIDE; O42923; -.
DR EnsemblFungi; SPBC16A3.18.1; SPBC16A3.18.1:pep; SPBC16A3.18.
DR GeneID; 2539823; -.
DR KEGG; spo:SPBC16A3.18; -.
DR PomBase; SPBC16A3.18; cip1.
DR VEuPathDB; FungiDB:SPBC16A3.18; -.
DR eggNOG; KOG0108; Eukaryota.
DR HOGENOM; CLU_600138_0_0_1; -.
DR InParanoid; O42923; -.
DR OMA; FNYHYDN; -.
DR PRO; PR:O42923; -.
DR Proteomes; UP000002485; Chromosome II.
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; cd12253; RRM_PIN4_like; 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; 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; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..490
FT /note="RNA-binding post-transcriptional regulator cip1"
FT /id="PRO_0000255601"
FT DOMAIN 202..280
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 16..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 490 AA; 53478 MW; CCE63830E9B83981 CRC64;
MPNEIFPWKI RVDESRGLAG NSGTKKSNHE ALSRLQSPLN SPKLQPIGSP QASRKTSGSG
SSAPLYPKWS GALSLASSRA ASPAPSDSFP TFGYSQLGGL ENSSKGSALF NSANSIGTPY
LSSRNSNSAN EASAMAFHNV SPPSGAESSS ESKSFSASGK GNKADTSAEP SLDAFNSTQI
KAGSTANSNS TPVEPGEDTI PTAIVVKNIP FSLEKDTLLD HFKQLGIPRP YAFNYHYDNG
IFRGLAFANF YRPEEAQVVV QTLNGYEING RRLRVEWKRQ LPAAEREKVE KAKKRQAEER
RRKQQYKMFE VSFTDQGLNL NDTGTLETYS RLLLFAHQCI PSREITFETT SKDGNLLNAI
RIFCLYFDLD YYARPNGEVL KLVVTHPNKK NTSVSQSQPA SPNLRFNMPA PLATRFLQEH
SLNGTKSAPI TPPPSFAVPL TNQLRSIDDK IYGNESPLQK ASTLSSPFNS KNDNDASTSA
SKQSFGVSHF
