CSX1_SCHPO
ID CSX1_SCHPO Reviewed; 632 AA.
AC O13759; Q09331; Q09335;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=RNA-binding post-transcriptional regulator csx1;
GN Name=csx1; ORFNames=SPAC17A2.09c;
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 161-393.
RX PubMed=8769419; DOI=10.1083/jcb.134.4.949;
RA Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y.,
RA Hirata A., Yanagida M.;
RT "Aberrant mitosis in fission yeast mutants defective in fatty acid
RT synthetase and acetyl CoA carboxylase.";
RL J. Cell Biol. 134:949-961(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH CIP1 AND CIP2.
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 FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-42; SER-54;
RP SER-291 AND SER-455.
RX PubMed=14633985; DOI=10.1093/emboj/cdg597;
RA Rodriguez-Gabriel M.A., Burns G., McDonald W.H., Martin V., Yates J.R. III,
RA Baehler J., Russell P.;
RT "RNA-binding protein Csx1 mediates global control of gene expression in
RT response to oxidative stress.";
RL EMBO J. 22:6256-6266(2003).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-54; SER-67 AND
RP SER-69, 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 atf1 and pcr1 mRNAs after oxidative stress,
CC thus controlling their turnover. {ECO:0000269|PubMed:14633985}.
CC -!- SUBUNIT: Interacts with cip1 and cip2. {ECO:0000269|PubMed:16407405}.
CC -!- INTERACTION:
CC O13759; Q10156: lkh1; NbExp=3; IntAct=EBI-1562021, EBI-7486409;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14633985,
CC ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB16569.1; -; Genomic_DNA.
DR EMBL; D83417; BAA11918.1; -; Genomic_DNA.
DR EMBL; D83418; BAA11919.1; -; Genomic_DNA.
DR PIR; T37810; T37810.
DR RefSeq; NP_594243.1; NM_001019666.2.
DR AlphaFoldDB; O13759; -.
DR SMR; O13759; -.
DR BioGRID; 278627; 10.
DR IntAct; O13759; 3.
DR MINT; O13759; -.
DR STRING; 4896.SPAC17A2.09c.1; -.
DR iPTMnet; O13759; -.
DR MaxQB; O13759; -.
DR PaxDb; O13759; -.
DR PRIDE; O13759; -.
DR EnsemblFungi; SPAC17A2.09c.1; SPAC17A2.09c.1:pep; SPAC17A2.09c.
DR GeneID; 2542151; -.
DR KEGG; spo:SPAC17A2.09c; -.
DR PomBase; SPAC17A2.09c; csx1.
DR VEuPathDB; FungiDB:SPAC17A2.09c; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_446298_0_0_1; -.
DR InParanoid; O13759; -.
DR OMA; HMQGYLC; -.
DR PRO; PR:O13759; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IMP:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0010628; P:positive regulation of gene expression; EXP:PomBase.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..632
FT /note="RNA-binding post-transcriptional regulator csx1"
FT /id="PRO_0000081536"
FT DOMAIN 85..167
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 182..261
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 297..369
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine; by MAPK sty1"
FT /evidence="ECO:0000269|PubMed:14633985,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 54
FT /note="Phosphoserine; by MAPK sty1"
FT /evidence="ECO:0000269|PubMed:14633985,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 291
FT /note="Phosphoserine; by MAPK sty1"
FT /evidence="ECO:0000269|PubMed:14633985"
FT MOD_RES 455
FT /note="Phosphoserine; by MAPK sty1"
FT /evidence="ECO:0000269|PubMed:14633985"
FT CONFLICT 265
FT /note="A -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> E (in Ref. 2; BAA11919)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> R (in Ref. 2; BAA11919)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..393
FT /note="VSDEGFDRTLS -> FQMRVRKNSFR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 67870 MW; 3852A0BDBCBD0C85 CRC64;
MSIDCLYRRS SLFDTSFVPL HSSIPATSKM SASNSDVNAP ISPVVDEGKS ELVSPTLERL
VAPFNCSPSS TPLQDVAGVG SKMSDTLWMG DLEPWMDATF IQQLWASLNE PVNVKVMRSK
ASSSETLISY CFVQFSSSAA AERALMKYNN TMIPGAHCTF KLNWATGGGI QHNNFVSRDP
EFSIFVGDLL PTTEDSDLFM TFRSIYPSCT SAKIIVDPVT GLSRKYGFVR FSSEKEQQHA
LMHMQGYLCQ GRPLRISVAS PKSRASIAAD SALGIVPTST SNRQPNQDLC SMDPLNTTVF
VGGLASNLSE KDLQVCFQPF GRILNIKIPF GKGCGFVQYS EKSAAEKAIN TMQGALVGTS
HIRLAWGHNT LPVSALSQSQ SQVSDEGFDR TLSANQIFGM NQSVIGANSG SSNSSGSSLK
SAPVSPRTAA AQSLLPNSVV SSINGMNSVN FSTISPPPLS RSASISPTLS GSGSGLTPLS
SHFPSAATGL VGGQVYPQSS VLQSSKINGS AKVQPSVKLP EWLQPFSGNN HNSFATQDLL
TRVSSLKLVD DEQPASLNGS AFQARASRPW NLGRERQSSL IDLRHELEQN ENGLEKSGFG
LNLRGRLPPR SYSTFNCTGQ YLQPSLRLSR DS
