ID   APC1_SCHPO              Reviewed;        1458 AA.
AC   Q9URV2; O13457;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Anaphase-promoting complex subunit 1;
DE   AltName: Full=20S cyclosome/APC complex protein apc1;
DE   AltName: Full=Cell untimely torn protein 4;
GN   Name=cut4; Synonyms=apc1; ORFNames=SPBC106.09;
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 FUNCTION.
RX   PubMed=8918880; DOI=10.1038/384276a0;
RA   Yamashita Y.M., Nakaseko Y., Samejima I., Kumada K., Yamada H.,
RA   Michaelson D., Yanagida M.;
RT   "20S cyclosome complex formation and proteolytic activity inhibited by the
RT   cAMP/PKA pathway.";
RL   Nature 384:276-279(1996).
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. Mutations to this protein prevent the
CC       exit from mitosis. {ECO:0000269|PubMed:8918880}.
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 APC1 family. {ECO:0000305}.
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DR   EMBL; D85196; BAA22618.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB53725.1; -; Genomic_DNA.
DR   PIR; T39266; T39266.
DR   PIR; T51995; T51995.
DR   RefSeq; NP_595158.1; NM_001021067.2.
DR   AlphaFoldDB; Q9URV2; -.
DR   SMR; Q9URV2; -.
DR   BioGRID; 276194; 26.
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; Q9URV2; 6.
DR   STRING; 4896.SPBC106.09.1; -.
DR   iPTMnet; Q9URV2; -.
DR   MaxQB; Q9URV2; -.
DR   PaxDb; Q9URV2; -.
DR   PRIDE; Q9URV2; -.
DR   EnsemblFungi; SPBC106.09.1; SPBC106.09.1:pep; SPBC106.09.
DR   GeneID; 2539639; -.
DR   KEGG; spo:SPBC106.09; -.
DR   PomBase; SPBC106.09; cut4.
DR   VEuPathDB; FungiDB:SPBC106.09; -.
DR   eggNOG; KOG1858; Eukaryota.
DR   HOGENOM; CLU_000746_0_0_1; -.
DR   InParanoid; Q9URV2; -.
DR   OMA; CHRRMSE; -.
DR   PhylomeDB; Q9URV2; -.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q9URV2; -.
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:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; IPI: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: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:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR024990; Apc1.
DR   InterPro; IPR011989; ARM-like.
DR   PANTHER; PTHR12827; PTHR12827; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1458
FT                   /note="Anaphase-promoting complex subunit 1"
FT                   /id="PRO_0000215874"
FT   REPEAT          873..895
FT                   /note="PC 1"
FT   REPEAT          959..982
FT                   /note="PC 2"
FT   REPEAT          1006..1024
FT                   /note="PC 3"
FT   REPEAT          1099..1124
FT                   /note="PC 4"
FT   REGION          186..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        995
FT                   /note="A -> V (in Ref. 1; BAA22618)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1458 AA;  165411 MW;  182E65BDA3A82183 CRC64;
     MLELKTNVIQ DPELKDSLDL QENDRVEIIG DAVHYIVNDH LNRVFNYTVD QQKIHAALIT
     TFASGKKAIV VILDDIGYVY YVGDNNNDSY IINVPFSTES AWSSPSGLYL QRHRSSDENL
     NTDLPHIFCL NDPLDELTLI KFDGKKILSL FDSIVYVVGE IVVTHNKKEK KLSFWRSRFI
     DPESDQSIKS SRNRRRESSF SREKNPDLTR SDSIHYTANT RLSEKFEEQG LAYSTIFSHI
     ESFPITGSTS FDSILGNGVL VITTLVKELE KGYMMLFRLV RDRSPYFLDS LQLHAINLSA
     IKSKHLQKIV VLSSKGKVSL ESPMSPSLPI EGTFRSFRVH GATLYLEDTD GVQRYISLDN
     RASNSLVKWC LSVIRYVLPL REYEIFYTGH LYALFAFKLS HDEAFISSIL ACFTFFSRDK
     VHVEPIEDCN EAYSLSSKFH FKKEILIASQ LSSHLDYSTF KNYLMPLAIT LHFISEELRL
     DSVVKPRKDQ LVALLLQITT WLKWPRYCEY YNFDIAETFL SIPLSIQVDV EEPVGPTSIL
     QWIIECLRSQ STVPFYGLES YGLPHSCSTM FPQTLSLMQL LDCLLNPNMT LQNLVEEMVR
     LGISRKRCER YPFGILCIIF TVLEIAAEEY SPNWESEELR LVNRLDVDSF LHPKTPKWVF
     NKQDQEVKEI KALTSTVTDS TLVDTQSFHP YKVVTDMIFR EDRRLAEVNK LLNYSSQITI
     MTEHFDVDLS SVPMQQKVAQ CICVRTLSVP IGAGMLTYGS KNPLPTEKVT PRLFNFTLHL
     HPGTLIIQPN KEFVTQELTE WPEFNVGVAL GLSISKFSKE INTSWIMFNR PETLTAYHAG
     FLFGLGLNGH LKALATWHSF IYLTSKHDTT SIGLLLGLAS SYLGSMDAKV TKLLSVHISA
     LLPVGSNELN ISPLTQTAGI LGIGLLFHDS CHRRMSEVTM EEILASNESE LKNEGYKLAA
     GFSLGLINLG RGSNLPGMSD LKLVSRLQVG ISSQATFQSL EAGSPGAIMA LTMIYMKTND
     LEVAKKIDIP KSRYLLDFYR PDLILLRVAG KNLIMWDEVK ADYEWVKYQI PDIMLSQFDL
     QEKKVLSSDD LLLYNVLAGI CFSLGLRFAG TGNPKAKEIL INFLDSFIRL CHLPAKTHDE
     RVTAVTVIRC TQIVALSSSC VMAGYCDLDV LRRLRVLHGR MEPVNYGAQM ATHMALGILS
     LGGGRYSLSR SNLAIAALLI SFYPQFPRTT QDNRAHLQAA RNLWALAVEE RCIIPRNQDT
     KQPCIVPLNV VQKSGAVQKL EAPILLPPYD SISSVSTLGD KYWNLKIDLD NNSDYRELLR
     ESQTLTLMPY DRTSSKEEPL NLFPKLKDTS SPLWNLVKTS RLFQSSNSPL NVASLQESNN
     KTSLGVKLLL SMDFDNLTRD RLLSLQILLQ FFESCWTGVL LNKFHSRQYL FLSRDLVEDL
     SLRVWEYVYS HNHNEESV