ID   APC2_SCHPO              Reviewed;         681 AA.
AC   Q874R3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Anaphase-promoting complex subunit 2;
DE   AltName: Full=20S cyclosome/APC complex protein apc2;
GN   Name=apc2; ORFNames=SPBP23A10.04;
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 [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   [2]
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.
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. {ECO:0000269|PubMed:12477395}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; CU329671; CAD62574.1; -; Genomic_DNA.
DR   RefSeq; NP_001018806.1; NM_001021720.2.
DR   AlphaFoldDB; Q874R3; -.
DR   SMR; Q874R3; -.
DR   BioGRID; 280280; 7.
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; Q874R3; 2.
DR   STRING; 4896.SPBP23A10.04.1; -.
DR   MaxQB; Q874R3; -.
DR   PaxDb; Q874R3; -.
DR   EnsemblFungi; SPBP23A10.04.1; SPBP23A10.04.1:pep; SPBP23A10.04.
DR   GeneID; 3361204; -.
DR   KEGG; spo:SPBP23A10.04; -.
DR   PomBase; SPBP23A10.04; apc2.
DR   VEuPathDB; FungiDB:SPBP23A10.04; -.
DR   eggNOG; KOG2165; Eukaryota.
DR   HOGENOM; CLU_007149_4_2_1; -.
DR   InParanoid; Q874R3; -.
DR   OMA; IHNMLTM; -.
DR   PhylomeDB; Q874R3; -.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q874R3; -.
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:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR044554; APC2-like.
DR   InterPro; IPR014786; APC2_C.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45957; PTHR45957; 1.
DR   Pfam; PF08672; ANAPC2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM01013; APC2; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF75632; SSF75632; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..681
FT                   /note="Anaphase-promoting complex subunit 2"
FT                   /id="PRO_0000237683"
SQ   SEQUENCE   681 AA;  78743 MW;  891764869C542EEB CRC64;
     MNDTDLSTFT GRSLLIDQLS SVTQGTPVLD FIDKLRIHFY TTIRQNLLKI DLKNICSLHD
     LTDQLSDFWL VYEQSVLESP ILSPELDRIL TCFRCLCRRY LPISVIESVL TEYLDQVLKV
     WLESKTNPCL DMEKFFQLCE KFKQLGLSSV LKERFVYVLQ LHVGSLLTTR YAMSWEQSVY
     HEALEWIRTE FGVLVEHVFS LSNPAVLVQL DHLVSQILAH LRSDNILDIV LHYPNSLGAI
     EDLRLVARQK QQRQYLTETF VKDCTSSILT ASSDSSYILL FYVSTIRCFV ALDPPGVLLD
     KAAKPIRSFL NEREDAYKCL VSLLFVDGEK GLRSELSQIP TENIDSTTDR FDNYHWMPDP
     IDAAPDFKKP TDRDVVGSLI SIFKSKEPLV KELQLLLADR LLQLTDYHYE VEAKNIEFLK
     YRFGETVLQM CSVMLNDIEN SRFIDQSIHM ENYVSKGLHV TILSRLFWPT LSVRYFHLPG
     PLKKELDAYA EEYRERKRKR ELVFLPNLGS VELEIELEDR TLTLTVTPEQ AAFISLFEET
     STLHIEKAAE LLDQPKEIVE RHLKFWLHHR VLTDIGDDRY RVRETEAETA TETVLDEIQG
     VSAVQSEAES SAAEMRVYWS FVVGMLTNLG ALELERIHNM LTMFIPPPNG YTRTQSELRE
     FLALMIKEEK LEFTGGAYKL K