SDS23_SCHPO
ID SDS23_SCHPO Reviewed; 408 AA.
AC Q09826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein sds23/moc1;
DE AltName: Full=Multicopy suppressor of overexpressed cyr1 protein 1;
DE AltName: Full=Phosphoprotein at stationary phase 1 protein;
GN Name=sds23; Synonyms=moc1, psp1; ORFNames=SPBC646.13;
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].
RX PubMed=8978689; DOI=10.1002/j.1460-2075.1996.tb01053.x;
RA Ishii K., Kumada K., Toda T., Yanagida M.;
RT "Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of
RT anaphase is lessened by the dosage increase of a novel gene sds23+.";
RL EMBO J. 15:6629-6640(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawamukai M., Adachi Y., Fukuda T., Nakagawa T., Matsuda H.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-333, AND MUTAGENESIS OF SER-333.
RX PubMed=9242669; DOI=10.1074/jbc.272.32.19993;
RA Jang Y.-J., Won M., Chung K.-S., Kim D.-U., Hoe K.-L., Park C., Yoo H.-S.;
RT "A novel protein, Psp1, essential for cell cycle progression of
RT Schizosaccharomyces pombe is phosphorylated by Cdc2-Cdc13 upon entry into
RT G0-like stationary phase of cell growth.";
RL J. Biol. Chem. 272:19993-20002(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16273369; DOI=10.1007/s00294-005-0028-z;
RA Goldar M.M., Jeong H.T., Tanaka K., Matsuda H., Kawamukai M.;
RT "Moc3, a novel Zn finger type protein involved in sexual development, ascus
RT formation, and stress response of Schizosaccharomyces pombe.";
RL Curr. Genet. 48:345-355(2005).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-329; SER-333 AND
RP SER-341, 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: Required for normal DNA replication and for proper mitosis.
CC Induces sexual development and ascus formation.
CC {ECO:0000269|PubMed:16273369, ECO:0000269|PubMed:9242669}.
CC -!- INTERACTION:
CC Q09826; Q10281: rkp1; NbExp=3; IntAct=EBI-7169035, EBI-696304;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:9242669}. Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:9242669}.
CC -!- PTM: Phosphorylated during the stationary phase of the cell cycle.
CC {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9242669}.
CC -!- SIMILARITY: Belongs to the SDS23 family. {ECO:0000305}.
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DR EMBL; D86840; BAA13172.1; -; Genomic_DNA.
DR EMBL; D87870; BAA13486.1; -; mRNA.
DR EMBL; L36906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329671; CAA22817.1; -; Genomic_DNA.
DR PIR; T43240; T43240.
DR RefSeq; NP_595371.1; NM_001021279.2.
DR AlphaFoldDB; Q09826; -.
DR SMR; Q09826; -.
DR BioGRID; 277632; 158.
DR IntAct; Q09826; 33.
DR MINT; Q09826; -.
DR STRING; 4896.SPBC646.13.1; -.
DR iPTMnet; Q09826; -.
DR MaxQB; Q09826; -.
DR PaxDb; Q09826; -.
DR PRIDE; Q09826; -.
DR EnsemblFungi; SPBC646.13.1; SPBC646.13.1:pep; SPBC646.13.
DR PomBase; SPBC646.13; sds23.
DR VEuPathDB; FungiDB:SPBC646.13; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_024459_1_1_1; -.
DR InParanoid; Q09826; -.
DR OMA; HRMWVTD; -.
DR PhylomeDB; Q09826; -.
DR PRO; PR:Q09826; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:PomBase.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:PomBase.
DR GO; GO:2001211; P:negative regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IMP:PomBase.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:1902471; P:regulation of mitotic actomyosin contractile ring localization; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR016711; Ssd23.
DR Pfam; PF00571; CBS; 2.
DR PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 1.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 3.
PE 1: Evidence at protein level;
KW CBS domain; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..408
FT /note="Protein sds23/moc1"
FT /id="PRO_0000097651"
FT DOMAIN 51..112
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 140..197
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 214..271
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 297..362
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 376..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 333
FT /note="Phosphoserine; by CDC2"
FT /evidence="ECO:0000269|PubMed:18257517,
FT ECO:0000269|PubMed:9242669"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 333
FT /note="S->A: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:9242669"
SQ SEQUENCE 408 AA; 44288 MW; 1C865AC3B1D04AC8 CRC64;
MPLSTQSSDS LSSAGRQSFG VNSVSDFLAQ FPIPTNLPSN KWQDIPVTFL HDNEIALIDP
ETSMEEASSI LIDRDLSALP IVAAKGSNEI ATTFDYADLN SFLLMVVGFD DFNDGRFKKV
AEDIRAGKVI TAYEVAKLGK NKDDFITIPH TTSLGRLAEI LSSGIRRVAV TNEQGELSFM
ASQRSIIRFL WNNIRAFPDL EPLMSRTIHS LDIGSTDITC ISGDQKVAAA LRQMNQTGIG
SLAVVDAQFR LLGNISLVDV KYVTRSSSVY LLNKSCAHFL SVIKSEQGIR AGKDSAPAFN
IYESSTFAFT LAKLVATQCH RLWLVQSPSC PPSPKNNAHL SPGSMGGVKV NQLLGVVSLT
DIISVLYAHM KGTLPPAPHS APSLRHGRRG STSSHRSHSK ASVDTQRR
