CUT9_SCHPO
ID CUT9_SCHPO Reviewed; 671 AA.
AC P41889; O14231;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Anaphase-promoting complex subunit cut9;
DE AltName: Full=20S cyclosome/APC complex protein cut9;
DE AltName: Full=Cell untimely torn protein 9;
GN Name=cut9; Synonyms=dre1; ORFNames=SPAC6F12.15c;
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 MUTAGENESIS OF GLY-412 AND ALA-535.
RX PubMed=7798319; DOI=10.1083/jcb.127.6.1655;
RA Samejima I., Yanagida M.;
RT "Bypassing anaphase by fission yeast cut9 mutation: requirement of cut9+ to
RT initiate anaphase.";
RL J. Cell Biol. 127:1655-1670(1994).
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, INTERACTION WITH NUC2, AND PHOSPHORYLATION.
RX PubMed=9264466; DOI=10.1242/jcs.110.15.1793;
RA Yamada H., Kumada K., Yanagida M.;
RT "Distinct subunit functions and cell cycle regulated phosphorylation of 20S
RT APC/cyclosome required for anaphase in fission yeast.";
RL J. Cell Sci. 110:1793-1804(1997).
RN [4]
RP SUBUNIT.
RX PubMed=12477395; DOI=10.1016/s0960-9822(02)01331-3;
RA Yoon H.-J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J.,
RA Gould K.L.;
RT "Proteomics analysis identifies new components of the fission and budding
RT yeast anaphase-promoting complexes.";
RL Curr. Biol. 12:2048-2054(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-597 IN COMPLEX WITH HCN1, TPR
RP REPEATS, AND SUBUNIT.
RX PubMed=20924356; DOI=10.1038/emboj.2010.247;
RA Zhang Z., Kulkarni K., Hanrahan S.J., Thompson A.J., Barford D.;
RT "The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat
RT superhelix with a homo-dimer interface similar to Cdc27.";
RL EMBO J. 29:3733-3744(2010).
CC -!- FUNCTION: Component of the anaphase-promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. The APC/C is thought to confer substrate specificity and, in the
CC presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC formation of protein-ubiquitin conjugates that are subsequently
CC degraded by the 26S proteasome. May play a pivotal role in the control
CC of anaphase. {ECO:0000269|PubMed:9264466}.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits: apc1, apc2,
CC nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and
CC apc15. Homodimer. Interacts directly with nuc2 and hcn1.
CC {ECO:0000269|PubMed:12477395, ECO:0000269|PubMed:20924356,
CC ECO:0000269|PubMed:9264466}.
CC -!- INTERACTION:
CC P41889; O42659: apc14; NbExp=2; IntAct=EBI-1160859, EBI-1251592;
CC P41889; O94688: apc15; NbExp=2; IntAct=EBI-1160859, EBI-1251604;
CC P41889; O13916: hcn1; NbExp=2; IntAct=EBI-1160859, EBI-1251563;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: TPR repeats 1-7 mediate homodimerization while TPR repeats 8
CC and 10-13 bind to hcn1, burying its N-terminal acetyl-methionine.
CC {ECO:0000269|PubMed:20924356}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9264466}.
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DR EMBL; D31844; BAA06630.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11098.1; -; Genomic_DNA.
DR PIR; A55164; A55164.
DR RefSeq; NP_593301.1; NM_001018731.2.
DR PDB; 2XPI; X-ray; 2.60 A; A/D=1-597.
DR PDBsum; 2XPI; -.
DR AlphaFoldDB; P41889; -.
DR SMR; P41889; -.
DR BioGRID; 278089; 55.
DR ComplexPortal; CPX-763; Anaphase-Promoting Complex variant 1.
DR ComplexPortal; CPX-764; Anaphase-Promoting Complex variant 2.
DR ComplexPortal; CPX-765; Anaphase-Promoting Complex variant 3.
DR ComplexPortal; CPX-766; Anaphase-Promoting Complex variant 4.
DR IntAct; P41889; 6.
DR MINT; P41889; -.
DR STRING; 4896.SPAC6F12.15c.1; -.
DR iPTMnet; P41889; -.
DR MaxQB; P41889; -.
DR PaxDb; P41889; -.
DR PRIDE; P41889; -.
DR EnsemblFungi; SPAC6F12.15c.1; SPAC6F12.15c.1:pep; SPAC6F12.15c.
DR GeneID; 2541592; -.
DR KEGG; spo:SPAC6F12.15c; -.
DR PomBase; SPAC6F12.15c; cut9.
DR VEuPathDB; FungiDB:SPAC6F12.15c; -.
DR eggNOG; KOG1173; Eukaryota.
DR HOGENOM; CLU_011751_4_0_1; -.
DR InParanoid; P41889; -.
DR OMA; DPFHNNA; -.
DR PhylomeDB; P41889; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P41889; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..671
FT /note="Anaphase-promoting complex subunit cut9"
FT /id="PRO_0000106281"
FT REPEAT 83..114
FT /note="TPR 1"
FT REPEAT 117..142
FT /note="TPR 2"
FT REPEAT 150..173
FT /note="TPR 3"
FT REPEAT 198..229
FT /note="TPR 4"
FT REPEAT 234..257
FT /note="TPR 5"
FT REPEAT 268..296
FT /note="TPR 6"
FT REPEAT 306..334
FT /note="TPR 7"
FT REPEAT 341..368
FT /note="TPR 8"
FT REPEAT 373..402
FT /note="TPR 9"
FT REPEAT 407..435
FT /note="TPR 10"
FT REPEAT 442..470
FT /note="TPR 11"
FT REPEAT 475..507
FT /note="TPR 12"
FT REPEAT 513..545
FT /note="TPR 13"
FT REPEAT 550..579
FT /note="TPR 14"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 412
FT /note="G->D: In cut9-T98; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7798319"
FT MUTAGEN 535
FT /note="A->T: In cut9-665; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7798319"
FT CONFLICT 103
FT /note="A -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:2XPI"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:2XPI"
FT TURN 436..439
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 457..470
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 491..507
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 516..528
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 566..579
FT /evidence="ECO:0007829|PDB:2XPI"
FT HELIX 584..592
FT /evidence="ECO:0007829|PDB:2XPI"
SQ SEQUENCE 671 AA; 75889 MW; 5300382396270BE2 CRC64;
MVVKRTQTDS RMQSTPGNHN HPDAHANAAY MTPPSMGALN ANNSNSQLST LTISPMTYLA
NNTSTDGSFL KERNAQNTDS LSREDYLRLW RHDALMQQQY KCAAFVGEKV LDITGNPNDA
FWLAQVYCCT GDYARAKCLL TKEDLYNRSS ACRYLAAFCL VKLYDWQGAL NLLGETNPFR
KDEKNANKLL MQDGGIKLEA SMCYLRGQVY TNLSNFDRAK ECYKEALMVD AKCYEAFDQL
VSNHLLTADE EWDLVLKLNY STYSKEDAAF LRSLYMLKLN KTSHEDELRR AEDYLSSING
LEKSSDLLLC KADTLFVRSR FIDVLAITTK ILEIDPYNLD VYPLHLASLH ESGEKNKLYL
ISNDLVDRHP EKAVTWLAVG IYYLCVNKIS EARRYFSKSS TMDPQFGPAW IGFAHSFAIE
GEHDQAISAY TTAARLFQGT HLPYLFLGMQ HMQLGNILLA NEYLQSSYAL FQYDPLLLNE
LGVVAFNKSD MQTAINHFQN ALLLVKKTQS NEKPWAATWA NLGHAYRKLK MYDAAIDALN
QGLLLSTNDA NVHTAIALVY LHKKIPGLAI THLHESLAIS PNEIMASDLL KRALEENSLT
SGFLNSKYVF EDEVSEYMQQ SNLNTSDKSM SMEDQSGKVT ESVNDRTQVL YADSRSEMMM
DDIEGNVSEQ R
