SRW1_SCHPO
ID SRW1_SCHPO Reviewed; 556 AA.
AC O13286; A7VJ97;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=WD repeat-containing protein srw1;
DE AltName: Full=Suppressor of rad/wee1;
GN Name=srw1; Synonyms=ste9; ORFNames=SPAC144.13c;
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 [MRNA], AND FUNCTION.
RX PubMed=9398669; DOI=10.1091/mbc.8.12.2475;
RA Yamaguchi S., Murakami H., Okayama H.;
RT "A WD repeat protein controls the cell cycle and differentiation by
RT negatively regulating Cdc2/B-type cyclin complexes.";
RL Mol. Biol. Cell 8:2475-2486(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9571240; DOI=10.1091/mbc.9.5.1065;
RA Kitamura K., Maekawa H., Shimoda C.;
RT "Fission yeast ste9, a homolog of hct1/cdh1 and Fizzy-related, is a novel
RT negative regulator of cell cycle progression during G1-phase.";
RL Mol. Biol. Cell 9:1065-1080(1998).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9736616; DOI=10.1093/emboj/17.18.5388;
RA Kominami K., Seth-Smith H., Toda T.;
RT "Apc10 and Ste9/Srw1, two regulators of the APC-cyclosome, as well as the
RT CDK inhibitor Rum1 are required for G1 cell-cycle arrest in fission
RT yeast.";
RL EMBO J. 17:5388-5399(1998).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT SER-62; THR-98; THR-177 AND SER-214, AND
RP MUTAGENESIS OF SER-62; THR-98; THR-177 AND SER-214.
RX PubMed=10921878; DOI=10.1093/emboj/19.15.3968;
RA Yamaguchi S., Okayama H., Nurse P.;
RT "Fission yeast Fizzy-related protein srw1p is a G(1)-specific promoter of
RT mitotic cyclin B degradation.";
RL EMBO J. 19:3968-3977(2000).
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-187, AND IDENTIFICATION BY
RP 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: Has a role in cell differentiation and cell cycling by
CC negatively regulating cig2 and cdc12-associated cdc2. Down-regulates
CC the level of cdc13, particularly in a nitrogen deprived environment.
CC Regulator of cell cycle G1 phase progression. Prevents onset of mitosis
CC during the pre-Start G1 period. Required for degradation of cdc13
CC mitotic cyclin B during G1 arrest but not during mitotic exit.
CC {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:9398669,
CC ECO:0000269|PubMed:9571240, ECO:0000269|PubMed:9736616}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Phosphorylated by cdc2-cdc13-CDK complex. This targets srw1 for
CC proteolysis which in turn promotes cdc13 turnover. Dephosphorylated
CC during G1 arrest. {ECO:0000269|PubMed:10921878,
CC ECO:0000269|PubMed:18257517}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; AB005589; BAA22152.1; -; mRNA.
DR EMBL; AB001285; BAF76646.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB59693.1; -; Genomic_DNA.
DR PIR; T37680; T37680.
DR RefSeq; NP_594674.1; NM_001020103.2.
DR AlphaFoldDB; O13286; -.
DR SMR; O13286; -.
DR BioGRID; 279271; 24.
DR ComplexPortal; CPX-765; Anaphase-Promoting Complex variant 3.
DR ELM; O13286; -.
DR STRING; 4896.SPAC144.13c.1; -.
DR iPTMnet; O13286; -.
DR PaxDb; O13286; -.
DR PRIDE; O13286; -.
DR EnsemblFungi; SPAC144.13c.1; SPAC144.13c.1:pep; SPAC144.13c.
DR GeneID; 2542824; -.
DR KEGG; spo:SPAC144.13c; -.
DR PomBase; SPAC144.13c; srw1.
DR VEuPathDB; FungiDB:SPAC144.13c; -.
DR eggNOG; KOG0305; Eukaryota.
DR HOGENOM; CLU_014831_4_1_1; -.
DR InParanoid; O13286; -.
DR OMA; WVQRGTH; -.
DR PhylomeDB; O13286; -.
DR Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SPO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-SPO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:O13286; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0031568; P:mitotic G1 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:PomBase.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IDA:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..556
FT /note="WD repeat-containing protein srw1"
FT /id="PRO_0000051228"
FT REPEAT 246..285
FT /note="WD 1"
FT REPEAT 289..328
FT /note="WD 2"
FT REPEAT 331..368
FT /note="WD 3"
FT REPEAT 372..411
FT /note="WD 4"
FT REPEAT 414..456
FT /note="WD 5"
FT REPEAT 458..499
FT /note="WD 6"
FT REPEAT 502..541
FT /note="WD 7"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10921878"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10921878"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10921878"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10921878"
FT MUTAGEN 62
FT /note="S->A: Increased mobility on Western blot."
FT /evidence="ECO:0000269|PubMed:10921878"
FT MUTAGEN 98
FT /note="T->A: Increased mobility on Western blot."
FT /evidence="ECO:0000269|PubMed:10921878"
FT MUTAGEN 177
FT /note="T->A: Increased mobility on Western blot."
FT /evidence="ECO:0000269|PubMed:10921878"
FT MUTAGEN 214
FT /note="S->A: Increased mobility on Western blot."
FT /evidence="ECO:0000269|PubMed:10921878"
SQ SEQUENCE 556 AA; 62060 MW; 9F9D13EC90F6964E CRC64;
MDEFDGFTRP TSSNSSANRN SNNSMNRVEN NNSNSDSANT VDSRGDAHTR MRQGFEKSFP
SSPNKKRPRT NEGDRFIPSR DASTELWTGF TKVEGPLTPV KKKQSVADRN FTTLLRSELF
GSNDETFNNS PIATPNTTIG VSTPRTDSGI DDIELTQRTP PSSSHTSSSI LQNTPVTPSR
KIFHYLSPRD RNKSSYGKKA QYQDNPNRTI YSLSPVRSIT KDLISASRLE GRELPSIPYR
VLDAPGLAGD FYLNLLDWGQ CNMLAVALAS RVYLWSGISS EVTVMHNFYP TDTVTSLRWV
QRGTHLAVGT HNGSVEIWDA ATCKKTRTMS GHTERVGALS WNDHVLSSGG RDNHILHRDV
RAPEHYFRVL TAHRQEVCGL EWNSNENLLA SGGNDNALMV WDKFEEKPLY SFHNHIAAVK
AITWSPHQRG ILASGGGTAD RTIKLWNTQR GSMLHNIDTG SQVCNLLWSK QTNEFISTHG
FMENEVALWN YPSVSRVGTL KGHTDRVLYL AMSPNGENIV TGAADETLRF WKLFDSKSKH
SASTMSSPFD PTMKIR
