ID   APC1_YEAST              Reviewed;        1748 AA.
AC   P53886; D6W112;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Anaphase-promoting complex subunit 1;
GN   Name=APC1; OrderedLocusNames=YNL172W; ORFNames=N1677;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 1547.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=8895471; DOI=10.1126/science.274.5290.1201;
RA   Zachariae W., Shin T.H., Galova M., Obermaier B., Nasmyth K.;
RT   "Identification of subunits of the anaphase-promoting complex of
RT   Saccharomyces cerevisiae.";
RL   Science 274:1201-1204(1996).
RN   [4]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH MND2.
RX   PubMed=12609981; DOI=10.1074/jbc.m213109200;
RA   Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.;
RT   "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-
RT   promoting complex.";
RL   J. Biol. Chem. 278:16698-16705(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1462, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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. In early mitosis, the APC/C is
CC       activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5,
CC       and other anaphase inhibitory proteins for proteolysis, thereby
CC       triggering the separation of sister chromatids at the metaphase-to-
CC       anaphase transition. In late mitosis and in G1, degradation of CLB5
CC       allows activation of the APC/C by CDH1, which is needed to destroy
CC       CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and
CC       creating the low CDK state necessary for cytokinesis and for reforming
CC       prereplicative complexes in G1 prior to another round of replication.
CC       {ECO:0000269|PubMed:12609981, ECO:0000269|PubMed:8895471}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC       tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5,
CC       APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC1
CC       interacts directly with MND2. {ECO:0000269|PubMed:12609981,
CC       ECO:0000269|PubMed:8895471}.
CC   -!- INTERACTION:
CC       P53886; P53886: APC1; NbExp=2; IntAct=EBI-29017, EBI-29017;
CC       P53886; P53068: DOC1; NbExp=9; IntAct=EBI-29017, EBI-2603;
CC       P53886; P40577: MND2; NbExp=3; IntAct=EBI-29017, EBI-25433;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC       {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 178 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the APC1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z71448; CAA96060.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10378.2; -; Genomic_DNA.
DR   PIR; S63127; S63127.
DR   RefSeq; NP_014227.4; NM_001183010.4.
DR   AlphaFoldDB; P53886; -.
DR   SMR; P53886; -.
DR   BioGRID; 35658; 507.
DR   ComplexPortal; CPX-756; Anaphase-Promoting core complex.
DR   ComplexPortal; CPX-760; Anaphase-Promoting Complex, CDC20 variant.
DR   ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR   ComplexPortal; CPX-762; Anaphase-Promoting complex AMA1 variant.
DR   DIP; DIP-970N; -.
DR   IntAct; P53886; 14.
DR   MINT; P53886; -.
DR   STRING; 4932.YNL172W; -.
DR   iPTMnet; P53886; -.
DR   MaxQB; P53886; -.
DR   PaxDb; P53886; -.
DR   PRIDE; P53886; -.
DR   EnsemblFungi; YNL172W_mRNA; YNL172W; YNL172W.
DR   GeneID; 855549; -.
DR   KEGG; sce:YNL172W; -.
DR   SGD; S000005116; APC1.
DR   VEuPathDB; FungiDB:YNL172W; -.
DR   eggNOG; KOG1858; Eukaryota.
DR   GeneTree; ENSGT00390000016757; -.
DR   HOGENOM; CLU_000746_0_0_1; -.
DR   InParanoid; P53886; -.
DR   OMA; LEEWHVY; -.
DR   BioCyc; YEAST:G3O-33185-MON; -.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P53886; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53886; protein.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:SGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:SGD.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR024990; Apc1.
DR   InterPro; IPR011989; ARM-like.
DR   PANTHER; PTHR12827; PTHR12827; 1.
DR   Pfam; PF12859; ANAPC1; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..1748
FT                   /note="Anaphase-promoting complex subunit 1"
FT                   /id="PRO_0000215875"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        1547
FT                   /note="M -> I (in Ref. 1; CAA96060)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1748 AA;  196162 MW;  33D32EC47CA40E61 CRC64;
     MTSKPSTRND YLPRETHNGE YTGDSPEWQL QINITNKIGG INGDIWLSRD GRSVKWCIED
     QCLRQFTYNQ KIIKAGYIDF EKTPDCFVVV LSDIAHVYML KNGGSTTVCF PFQIGNAFWY
     ANGVILERET SASFMDGGYD LKPIEFDLKH KYITLTDPMA PFGLISITNT FKGGINSASG
     NKTDILQDFQ LVLFPSDKDK CIAVFLDRNS KVLRFYYSRI LSSDQSRKGE LTISSTKKTG
     LDAAGNSQKS GGISKDLRKF SHLTRRSTSI NSNSHDFNAA ERVLSGNVGN ASGRTDIFAL
     PSSCSRRSLS ATLDRMGNNI APTNRAAPSG FFDSSSANTA THSNITPVSQ PMQQQQQEYL
     NQTATSSKDI VLTEISSLKL PDDIIFTSRR LSSILSKLKF LSLRFERREG LLIFHEPTHF
     CKIWLIDLLP DVLDSIPFKI YGNSPQNMIR LENLKLKEPS RIQAMYIHEL LESCLILVSE
     GQNKEEYKAC LYDPFVKITS PSKNISEELT KQNSLPSLQK LFPYPETSFT KLCFEAVKYI
     TSPAFNISFI FLWQSAYSIL LSRANDDVVG GLKMEHDAFS LVLSLLILPI PSSSAQEYQE
     YKEIYERDLF QHLKQDSEIT SSVLPRIVIG LHLIREEYSL NVLCRNEHAL LGQFLRFATA
     AMGWPDLWQS YYVPKMDSES KTFLHPREQN STFFHPLDEP PSITKSLYSI TENSSIPLCP
     FISFSRLVAT DTQVELRITP RSFKILGLYE LVHSPNFLPD YVLGILSSFK VDKDELQTYP
     LGILVPLQNI LKILEDKLSE VRDNLELLDR ADLQRCSAII NSIRSDSKEV LKRGQRDSYM
     LCKVPLAKNR SSLSKKPSDI YSILSEIVKS ASQVPLDGSA MRMSNIQDDE DIDEGRSLKL
     NAGLIFSEDK RFTHVVSLLA YYRPTKTQFF TTKTEYAQIL AQKKYFAKIM ALRTCTNGVG
     WGAVAYATEK PISTQKWVIQ PLNLISVFPD DTKITVKAPE DIAHDIVEWG QFHAGVSSGL
     RISKKATGIT GSWIAFNKPK ELDAYHGGFL LGLGLNGHLK NLEEWHIYNY LSPRNTHISI
     GLLLGMSSSM KGSMDSKLIK VISVHLVAFL PSGSSDLNID LKLQTAGIIG MGMLYLNSRH
     KRMSDSIFAQ LVSLLNVNDE MVADEEYRLA AGISLGLINL GAGQTKLRKW DSSLLGLGDD
     LPEDVYDSSD VEQNVMYEDL TTKLLEIVTS TYDVENDWIP ENSQIGAVIA IMFLFLKSNN
     FGISNMLKVD LKEILKANIN TRPELLMYRE WASNMILWEF IGDDLSFIMK DVDIGVKFSE
     LNTDLLPIYY TMAGRILAMG IRFASTGNLK IRNILLSLVD KFLPLYQYPG KQNLDFRLTI
     SVINVLTNVI VVSLSMVMCA SGDLEVLRRV KYLHEVASGP YSDLFQEIPS SKSDVSGVTQ
     VTSNTNTPGN SDRERVDETA ASLDDERSSN GSDISDPTAY LEDKKDIDDH YGKFISTNLA
     LGFLFLGSGQ YALNTSTLES IAFLSMSVLP TYTTPHPLQE LKHFWSMAVE PRCLVIKDIS
     TGDAVNNVPI ELVVEEDVEK EEVIREISTP CLLPDFSKIK SIRVKMHGYF PLEVNFTKDY
     SASDFFSGGT IIYIQRKSES VFENKASFRN VEDIHVALKR KAAESKNYSR LNLKNEQGNT
     TSSQLVESLG IQDLTMVELD TLLSAGNNTA LTDSESYNLG LLCSDKNSGD ILDCQLELWY
     KSFGPHDE