APC10_SCHPO
ID APC10_SCHPO Reviewed; 189 AA.
AC O42971;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Anaphase-promoting complex subunit 10;
DE AltName: Full=20S cyclosome/APC complex protein apc10;
GN Name=apc10; ORFNames=SPBC1A4.01, SPBC1E8.06;
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], FUNCTION, AND INTERACTION WITH NUC2.
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 [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 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. Acts as a positive regulator of the
CC anaphase promoting complex (APC)-cyclosome. Involved in G1 cell cycle
CC arrest in response to nitrogen starvation. Required for ubiquitination
CC and degradation of the mitotic B-type cyclin, cdc13.
CC {ECO:0000269|PubMed:9736616}.
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 nuc2. {ECO:0000269|PubMed:12477395,
CC ECO:0000269|PubMed:9736616}.
CC -!- SIMILARITY: Belongs to the APC10 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA16839.1; -; Genomic_DNA.
DR EMBL; AB012919; BAA32157.1; -; Genomic_DNA.
DR PIR; T39849; T39849.
DR RefSeq; NP_595803.1; NM_001021705.2.
DR AlphaFoldDB; O42971; -.
DR SMR; O42971; -.
DR BioGRID; 276837; 113.
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; O42971; 2.
DR STRING; 4896.SPBC1A4.01.1; -.
DR MaxQB; O42971; -.
DR PaxDb; O42971; -.
DR EnsemblFungi; SPBC1A4.01.1; SPBC1A4.01.1:pep; SPBC1A4.01.
DR GeneID; 2540307; -.
DR KEGG; spo:SPBC1A4.01; -.
DR PomBase; SPBC1A4.01; apc10.
DR VEuPathDB; FungiDB:SPBC1A4.01; -.
DR eggNOG; KOG3437; Eukaryota.
DR HOGENOM; CLU_039415_3_0_1; -.
DR InParanoid; O42971; -.
DR OMA; FITIEFP; -.
DR PhylomeDB; O42971; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:O42971; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR CDD; cd08366; APC10; 1.
DR InterPro; IPR016901; APC10/Doc1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR12936; PTHR12936; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR PIRSF; PIRSF028841; APC10_sub; 1.
DR SMART; SM01337; APC10; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..189
FT /note="Anaphase-promoting complex subunit 10"
FT /id="PRO_0000174015"
FT DOMAIN 2..187
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
SQ SEQUENCE 189 AA; 21474 MW; 91AB73EA9D2FDE05 CRC64;
MAQIRQEALK KQKSETQKST EGFVDIGNLA QWTCSSEKSG FPIRLVRDDN IDTYWQSDGS
QPHTIHIKFV KRVSIKYVSM YLQYTLDESY TPSTLRISAG TGFQDLEIVT TVQVEEPTGW
VHVPVGDFGR NGLLDVHLIQ IKILANHQSG KDSHVRLIKI YAPEIEQPAI AVDEIPYTSL
QFISRNQLR