ID   SCW1_SCHPO              Reviewed;         561 AA.
AC   O74452;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Cell wall integrity protein scw1;
DE   AltName: Full=Strong cell wall protein 1;
GN   Name=scw1; ORFNames=SPCC16C4.07;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12242222; DOI=10.1093/genetics/162.1.45;
RA   Karagiannis J., Oulton R., Young P.G.;
RT   "The Scw1 RNA-binding domain protein regulates septation and cell-wall
RT   structure in fission yeast.";
RL   Genetics 162:45-58(2002).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; THR-193; SER-196;
RP   SER-216; THR-218; SER-231; SER-298; SER-302; SER-325 AND SER-370, AND
RP   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: Acts as a negative regulator of cell wall and septum
CC       deposition. {ECO:0000269|PubMed:12242222}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242222}.
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DR   EMBL; CU329672; CAA20746.1; -; Genomic_DNA.
DR   PIR; T41097; T41097.
DR   RefSeq; NP_587917.1; NM_001022908.2.
DR   AlphaFoldDB; O74452; -.
DR   BioGRID; 275924; 24.
DR   STRING; 4896.SPCC16C4.07.1; -.
DR   iPTMnet; O74452; -.
DR   MaxQB; O74452; -.
DR   PaxDb; O74452; -.
DR   PRIDE; O74452; -.
DR   EnsemblFungi; SPCC16C4.07.1; SPCC16C4.07.1:pep; SPCC16C4.07.
DR   GeneID; 2539358; -.
DR   KEGG; spo:SPCC16C4.07; -.
DR   PomBase; SPCC16C4.07; scw1.
DR   VEuPathDB; FungiDB:SPCC16C4.07; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_482467_0_0_1; -.
DR   InParanoid; O74452; -.
DR   OMA; STQPGYK; -.
DR   PRO; PR:O74452; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IMP:PomBase.
DR   Gene3D; 3.30.70.330; -; 1.
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; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..561
FT                   /note="Cell wall integrity protein scw1"
FT                   /id="PRO_0000081901"
FT   DOMAIN          426..503
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          192..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         193
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         218
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   561 AA;  60394 MW;  A6BE9F60E3214F80 CRC64;
     MFVGSPSAIE KPLSLSSKTK VGDETEFTED ALRGSSLVPT GILNGDDECH ALHMSPQAIH
     SQAGKAESDG LPTYASVEKS TTPIGRLLSN LNGGLASAPP KVGFGFPRYY ALRIEDLPRD
     LTPREFLCTF LFATNVVSVE LNPVSVDNEV AHGLAVFSSR DAAASARDTL LSSDVYSACS
     MIILDNYRKG SQTNLSDETE GSESSVSFNR LSRNHSPTRP LLGNRDLFRR SSNHVSASMP
     TANHSESAYR HSKTPLGDST FQAPNNGGSL HSDRLWSSFP VSYPLTLANV LAKDEVGSPT
     WSPTPSKSST NLRQDGVPPI LRFNSLSINT NVARNYLSSE KGYSAHTQNS SAQSPHPRVF
     SANSAFSTTS PPPLTPSTSR DYPFSASTIS PSTPFSAYSS SHGIHQRIPA STPTNTNPAD
     QNPPCNTIYV GNLPPSTSEE ELKVLFSTQV GYKRLCFRTK GNGPMCFVEF ENIPYAMEAL
     KNLQGVCLSS SIKGGIRLSF SKNPLGVRSS SSSHNNHNGN VRNLHSGSMN NYNTDSLLNH
     TGGHNEVHAS PSWGNNLMYG K