APC5_YEAST
ID APC5_YEAST Reviewed; 685 AA.
AC Q08683; D6W2V0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Anaphase-promoting complex subunit 5;
GN Name=APC5; Synonyms=RMC1; OrderedLocusNames=YOR249C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
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 [4]
RP PROTEIN SEQUENCE OF 519-527 AND 626-632, SUBUNIT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=9469814; DOI=10.1126/science.279.5354.1216;
RA Zachariae W., Shevchenko A., Andrews P.D., Ciosk R., Galova M., Stark M.J.,
RA Mann M., Nasmyth K.;
RT "Mass spectrometric analysis of the anaphase-promoting complex from yeast:
RT identification of a subunit related to cullins.";
RL Science 279:1216-1219(1998).
RN [5]
RP SUBUNIT, AND INTERACTION WITH MND2 AND SWM1.
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 [6]
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 [7]
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).
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 -!- 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. APC5
CC directly interacts with MND2 and SWM1. {ECO:0000269|PubMed:12609981,
CC ECO:0000269|PubMed:9469814}.
CC -!- INTERACTION:
CC Q08683; Q04601: APC4; NbExp=7; IntAct=EBI-35371, EBI-32842;
CC Q08683; P40577: MND2; NbExp=4; IntAct=EBI-35371, EBI-25433;
CC Q08683; Q12379: SWM1; NbExp=4; IntAct=EBI-35371, EBI-33330;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APC5 family. {ECO:0000305}.
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DR EMBL; Z75157; CAA99471.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11016.1; -; Genomic_DNA.
DR PIR; S67146; S67146.
DR RefSeq; NP_014892.3; NM_001183668.3.
DR AlphaFoldDB; Q08683; -.
DR BioGRID; 34639; 642.
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-1127N; -.
DR IntAct; Q08683; 20.
DR MINT; Q08683; -.
DR STRING; 4932.YOR249C; -.
DR MaxQB; Q08683; -.
DR PaxDb; Q08683; -.
DR PRIDE; Q08683; -.
DR EnsemblFungi; YOR249C_mRNA; YOR249C; YOR249C.
DR GeneID; 854423; -.
DR KEGG; sce:YOR249C; -.
DR SGD; S000005775; APC5.
DR VEuPathDB; FungiDB:YOR249C; -.
DR eggNOG; ENOG502R07C; Eukaryota.
DR GeneTree; ENSGT00390000018674; -.
DR HOGENOM; CLU_416912_0_0_1; -.
DR InParanoid; Q08683; -.
DR OMA; RETIWIN; -.
DR BioCyc; YEAST:G3O-33741-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q08683; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08683; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; IMP:SGD.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
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 InterPro; IPR037679; Apc5.
DR InterPro; IPR026000; Apc5_dom.
DR PANTHER; PTHR12830; PTHR12830; 1.
DR Pfam; PF12862; ANAPC5; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Direct protein sequencing; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..685
FT /note="Anaphase-promoting complex subunit 5"
FT /id="PRO_0000064625"
SQ SEQUENCE 685 AA; 79275 MW; 59310B47D5A1865F CRC64;
MSKYGPLGIT NFITPYDLCI LILIHAHCSQ DNGISVPTAV FLRLISPTRP SLEWNPLLKD
NSNLRSSSIV PPPVLPILDN IIRILLDDKD GNKIALTLMG YLEAINGLDS INRLMMDLEK
NCLVNNYRSM KMRTTSTRRQ MTRASFLGTF LSTCIRKYQI GDFEMRETIW INLQNFKTVF
KHTPLWLRFK DNVHIQKVKN CLLANDEISV EDQQMVEFFQ HFNNGNDADS KTMNEENYGT
LISIQHLQSI VNRQIVNWLD NTEFNLMGQE ETSSTYEEQS GLVFDLLDTL SLNDATKFPL
IFILKYLEAI KENSYQTALD SLHNYFDYKS TGNSQNYFHI SLLSLATFHS SFNECDAAIN
SFEEATRIAR ENKDMETLNL IMIWIINFIE VHPEYANRFY ITVEQIIKYL KNSSDVEDAN
IFSNAYKFET LLSMVKESKT AEVSSSLLKF MAITLQNVPS QNFDLFQSLV SYEVKFWKEL
GYESISDVYE KFLSKTSSSS LRNYDSSIIN QDIKVAFKAL EEDDFLKVKQ YLLKSESLEL
DYDQKINLKY LRVKYLVKIG DYDLSMRLIN QYVKECCEEV ADSNWRFKFE IESINVLLLS
DVGIRSLPKI IKLIDEYKEI GNPLRCVILL LKLCEVLIQV GKSMEAECLI SCNLSTILEF
PFVRKKTDEL LESLSVEEDR DVQMT
