APC11_SCHPO
ID APC11_SCHPO Reviewed; 94 AA.
AC Q9UT86; P79054;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Anaphase-promoting complex subunit 11;
DE AltName: Full=20S cyclosome/APC complex protein apc11;
GN Name=apc11; ORFNames=SPAC343.03;
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 MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(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 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 -!- SEQUENCE CAUTION:
CC Sequence=BAA19216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB001022; BAA19216.1; ALT_SEQ; mRNA.
DR EMBL; CU329670; CAB52266.1; -; Genomic_DNA.
DR PIR; T38652; T38652.
DR RefSeq; NP_593423.1; NM_001018856.2.
DR AlphaFoldDB; Q9UT86; -.
DR SMR; Q9UT86; -.
DR BioGRID; 279616; 9.
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; Q9UT86; 2.
DR STRING; 4896.SPAC343.03.1; -.
DR SwissPalm; Q9UT86; -.
DR MaxQB; Q9UT86; -.
DR PaxDb; Q9UT86; -.
DR EnsemblFungi; SPAC343.03.1; SPAC343.03.1:pep; SPAC343.03.
DR GeneID; 2543187; -.
DR KEGG; spo:SPAC343.03; -.
DR PomBase; SPAC343.03; apc11.
DR VEuPathDB; FungiDB:SPAC343.03; -.
DR eggNOG; KOG1493; Eukaryota.
DR HOGENOM; CLU_115512_0_1_1; -.
DR InParanoid; Q9UT86; -.
DR OMA; QWRWDTG; -.
DR PhylomeDB; Q9UT86; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q9UT86; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16456; RING-H2_APC11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Metal-binding; Mitosis; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..94
FT /note="Anaphase-promoting complex subunit 11"
FT /id="PRO_0000055750"
FT ZN_FING 35..78
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 94 AA; 10557 MW; C7770021339C3626 CRC64;
MKVKILRYHA IANWTWDTPK DDVCGICRVP FDGCCPQCTS PGDNCPIVWG KCKHIFHAHC
IQNWLATSGS QGQCPMDRQT FVVADSTNEK SETQ
