APC3_SCHPO
ID APC3_SCHPO Reviewed; 665 AA.
AC P10505; Q9US21;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Anaphase-promoting complex subunit 3;
DE AltName: Full=20S cyclosome/APC complex protein apc3;
DE AltName: Full=Nuclear alteration protein 2;
DE AltName: Full=Nuclear scaffold-like protein p76;
GN Name=nuc2; Synonyms=apc3; ORFNames=SPAC17C9.01c, SPAC1851.01;
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-504.
RX PubMed=3283148; DOI=10.1083/jcb.106.4.1171;
RA Hirano M., Hiraoka Y., Yanagida M.;
RT "A temperature-sensitive mutation of the Schizosaccharomyces pombe gene
RT nuc2+ that encodes a nuclear scaffold-like protein blocks spindle
RT elongation in mitotic anaphase.";
RL J. Cell Biol. 106:1171-1183(1988).
RN [2]
RP SEQUENCE REVISION TO 649.
RA Yanagida M.;
RL Submitted (MAR-1989) to the EMBL/GenBank/DDBJ databases.
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 DOMAINS.
RX PubMed=2297790; DOI=10.1016/0092-8674(90)90746-2;
RA Hirano T., Kinoshita N., Morikawa K., Yanagida M.;
RT "Snap helix with knob and hole: essential repeats in S. pombe nuclear
RT protein nuc2+.";
RL Cell 60:319-328(1990).
RN [5]
RP FUNCTION, AND INTERACTION WITH CUT9.
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 [6]
RP INTERACTION WITH APC10.
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 [7]
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).
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. Interacts with spindle apparatus,
CC chromosomes, or nuclear envelope, and interconnect nuclear and
CC cytoskeletal functions in mitosis, so the elongation of the spindle in
CC anaphase is blocked. {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. Interacts with apc10 and cut9. {ECO:0000269|PubMed:12477395,
CC ECO:0000269|PubMed:9264466, ECO:0000269|PubMed:9736616}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
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DR EMBL; X07693; CAA30532.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA97347.1; -; Genomic_DNA.
DR PIR; A30185; A30185.
DR PIR; T50124; T50124.
DR RefSeq; NP_594604.2; NM_001020032.2.
DR AlphaFoldDB; P10505; -.
DR SMR; P10505; -.
DR BioGRID; 278900; 19.
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; P10505; 2.
DR STRING; 4896.SPAC17C9.01c.1; -.
DR MaxQB; P10505; -.
DR PaxDb; P10505; -.
DR PRIDE; P10505; -.
DR EnsemblFungi; SPAC17C9.01c.1; SPAC17C9.01c.1:pep; SPAC17C9.01c.
DR GeneID; 2542438; -.
DR KEGG; spo:SPAC17C9.01c; -.
DR PomBase; SPAC17C9.01c; nuc2.
DR VEuPathDB; FungiDB:SPAC17C9.01c; -.
DR eggNOG; KOG1126; Eukaryota.
DR HOGENOM; CLU_008850_0_1_1; -.
DR InParanoid; P10505; -.
DR OMA; MCKYDCY; -.
DR PhylomeDB; P10505; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P10505; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051728; P:cell cycle switching, mitotic to meiotic cell cycle; 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:0000070; P:mitotic sister chromatid segregation; 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; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..665
FT /note="Anaphase-promoting complex subunit 3"
FT /id="PRO_0000106304"
FT REPEAT 115..148
FT /note="TPR 1"
FT REPEAT 329..362
FT /note="TPR 2"
FT REPEAT 363..396
FT /note="TPR 3"
FT REPEAT 431..464
FT /note="TPR 4"
FT REPEAT 466..498
FT /note="TPR 5"
FT REPEAT 499..532
FT /note="TPR 6"
FT REPEAT 534..566
FT /note="TPR 7"
FT REPEAT 568..600
FT /note="TPR 8"
FT REPEAT 601..634
FT /note="TPR 9"
FT DNA_BIND 191..257
FT MUTAGEN 504
FT /note="G->D: In nuc2-663; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:3283148"
FT CONFLICT 440
FT /note="C -> W (in Ref. 1; CAA30532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 76171 MW; 97775DC061ECAFBA CRC64;
MTDRLKCLIW YCIDNQNYDN SIFYSERLHA IEDSNESLYL LAYSHFLNLD YNIVYDLLDR
VISHVPCTYL FARTSLILGR YKQGISAVEA CRSNWRSIQP NINDSISSRG HPDASCMLDV
LGTMYKKAGF LKKATDCFVE AVSINPYNFS AFQNLTAIGV PLDANNVFVI PPYLTAMKGF
EKSQTNATAS VPEPSFLKKS KESSSSSNKF SVSESIANSY SNSSISAFTK WFDRVDASEL
PGSEKERHQS LKLQSQSQTS KNLLAFNDAQ KADSNNRDTS LKSHFVEPRT QALRPGARLT
YKLREARSSK RGESTPQSFR EEDNNLMELL KLFGKGVYLL AQYKLREALN CFQSLPIEQQ
NTPFVLAKLG ITYFELVDYE KSEEVFQKLR DLSPSRVKDM EVFSTALWHL QKSVPLSYLA
HETLETNPYS PESWCILANC FSLQREHSQA LKCINRAIQL DPTFEYAYTL QGHEHSANEE
YEKSKTSFRK AIRVNVRHYN AWYGLGMVYL KTGRNDQADF HFQRAAEINP NNSVLITCIG
MIYERCKDYK KALDFYDRAC KLDEKSSLAR FKKAKVLILL HDHDKALVEL EQLKAIAPDE
ANVHFLLGKI FKQMRKKNLA LKHFTIAWNL DGKATHIIKE SIENLDIPEE NLLTETGEIY
RNLET
