SLP1_SCHPO
ID SLP1_SCHPO Reviewed; 488 AA.
AC P78972;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=WD repeat-containing protein slp1;
GN Name=slp1; ORFNames=SPAC821.08c;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9001228; DOI=10.1128/mcb.17.2.742;
RA Matsumoto T.;
RT "A fission yeast homolog of CDC20/p55CDC/Fizzy is required for recovery
RT from DNA damage and genetically interacts with p34cdc2.";
RL Mol. Cell. Biol. 17:742-750(1997).
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 FUNCTION, AND MUTAGENESIS OF 131-ALA-PHE-132.
RX PubMed=9461438; DOI=10.1126/science.279.5353.1045;
RA Kim S.H., Lin D.P., Matsumoto S., Kitazono A., Matsumoto T.;
RT "Fission yeast Slp1: an effector of the Mad2-dependent spindle
RT checkpoint.";
RL Science 279:1045-1047(1998).
RN [4]
RP INTERACTION WITH MAD3.
RX PubMed=11909965; DOI=10.1128/mcb.22.8.2728-2742.2002;
RA Millband D.N., Hardwick K.G.;
RT "Fission yeast Mad3p is required for Mad2p to inhibit the anaphase-
RT promoting complex and localizes to kinetochores in a Bub1p-, Bub3p-, and
RT Mph1p-dependent manner.";
RL Mol. Cell. Biol. 22:2728-2742(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH MES1 AND CDC13.
RX PubMed=15791259; DOI=10.1038/nature03406;
RA Izawa D., Goto M., Yamashita A., Yamano H., Yamamoto M.;
RT "Fission yeast Mes1p ensures the onset of meiosis II by blocking
RT degradation of cyclin Cdc13p.";
RL Nature 434:529-533(2005).
CC -!- FUNCTION: Required for mad2-dependent spindle checkpoint activation.
CC Promotes ubiquitin-dependent degradation of cdc13 by the anaphase
CC promoting complex/cyclosome (APC/C). {ECO:0000269|PubMed:15791259,
CC ECO:0000269|PubMed:9001228, ECO:0000269|PubMed:9461438}.
CC -!- SUBUNIT: Interacts with cdc13, mad3 and mes1.
CC {ECO:0000269|PubMed:11909965, ECO:0000269|PubMed:15791259}.
CC -!- INTERACTION:
CC P78972; O14417: mad2; NbExp=8; IntAct=EBI-1252744, EBI-1269310;
CC P78972; P41005: mes1; NbExp=2; IntAct=EBI-1252744, EBI-1553555;
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; U77983; AAC49621.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB57442.1; -; Genomic_DNA.
DR PIR; T41719; T41719.
DR RefSeq; NP_593161.1; NM_001018559.2.
DR PDB; 4AEZ; X-ray; 2.30 A; A/D/G=88-488.
DR PDBsum; 4AEZ; -.
DR AlphaFoldDB; P78972; -.
DR SMR; P78972; -.
DR BioGRID; 279650; 30.
DR ComplexPortal; CPX-3924; Mitotic Checkpoint Complex.
DR ComplexPortal; CPX-764; Anaphase-Promoting Complex variant 2.
DR DIP; DIP-38036N; -.
DR ELM; P78972; -.
DR IntAct; P78972; 4.
DR STRING; 4896.SPAC821.08c.1; -.
DR iPTMnet; P78972; -.
DR PaxDb; P78972; -.
DR PRIDE; P78972; -.
DR EnsemblFungi; SPAC821.08c.1; SPAC821.08c.1:pep; SPAC821.08c.
DR GeneID; 2543222; -.
DR KEGG; spo:SPAC821.08c; -.
DR PomBase; SPAC821.08c; slp1.
DR VEuPathDB; FungiDB:SPAC821.08c; -.
DR eggNOG; KOG0305; Eukaryota.
DR HOGENOM; CLU_014831_6_0_1; -.
DR OMA; NGHEDRV; -.
DR PhylomeDB; P78972; -.
DR Reactome; R-SPO-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-SPO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P78972; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0033597; C:mitotic checkpoint complex; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:PomBase.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IC:ComplexPortal.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:1905188; P:positive regulation of metaphase/anaphase transition of meiosis I; EXP:PomBase.
DR GO; GO:1905191; P:positive regulation of metaphase/anaphase transition of meiosis II; EXP:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; NAS: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; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..488
FT /note="WD repeat-containing protein slp1"
FT /id="PRO_0000051220"
FT REPEAT 178..215
FT /note="WD 1"
FT REPEAT 219..258
FT /note="WD 2"
FT REPEAT 261..298
FT /note="WD 3"
FT REPEAT 302..341
FT /note="WD 4"
FT REPEAT 344..386
FT /note="WD 5"
FT REPEAT 388..429
FT /note="WD 6"
FT REPEAT 434..473
FT /note="WD 7"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 131..132
FT /note="AF->PY: Abrogates binding to mad2 and overrides
FT activation of the spindle checkpoint by mad2."
FT /evidence="ECO:0000269|PubMed:9461438"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:4AEZ"
SQ SEQUENCE 488 AA; 53418 MW; 52E021FD4EECE5DE CRC64;
MEIAGNSSTI SPTFSTPTKK RNLVFPNSPI TPLHQQALLG RNGRSSKRCS PKSSFIRNSP
KIDVVNTDWS IPLCGSPRNK SRPASRSDRF IPSRPNTANA FVNSISSDVP FDYSESVAEA
CGFDLNTRVL AFKLDAPEAK KPVDLRTQHN RPQRPVVTPA KRRFNTTPER VLDAPGIIDD
YYLNLLDWSN LNVVAVALER NVYVWNADSG SVSALAETDE STYVASVKWS HDGSFLSVGL
GNGLVDIYDV ESQTKLRTMA GHQARVGCLS WNRHVLSSGS RSGAIHHHDV RIANHQIGTL
QGHSSEVCGL AWRSDGLQLA SGGNDNVVQI WDARSSIPKF TKTNHNAAVK AVAWCPWQSN
LLATGGGTMD KQIHFWNAAT GARVNTVDAG SQVTSLIWSP HSKEIMSTHG FPDNNLSIWS
YSSSGLTKQV DIPAHDTRVL YSALSPDGRI LSTAASDENL KFWRVYDGDH VKRPIPITKT
PSSSITIR
