APC10_YEAST
ID APC10_YEAST Reviewed; 250 AA.
AC P53068; D6VV95;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Anaphase-promoting complex subunit DOC1;
DE AltName: Full=Destruction of cyclin B protein 1;
GN Name=DOC1; Synonyms=APC10; OrderedLocusNames=YGL240W; ORFNames=HRC283;
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 204508 / S288c;
RX PubMed=8750240; DOI=10.1002/yea.320111507;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left
RT arm of chromosome VII, reveals the presence of eight open reading frames.";
RL Yeast 11:1519-1523(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBUNIT, AND MUTAGENESIS OF SER-94.
RX PubMed=9348530; DOI=10.1091/mbc.8.10.1877;
RA Hwang L.H., Murray A.W.;
RT "A novel yeast screen for mitotic arrest mutants identifies DOC1, a new
RT gene involved in cyclin proteolysis.";
RL Mol. Biol. Cell 8:1877-1887(1997).
RN [6]
RP FUNCTION, AND SUBSTRATE RECOGNITION.
RX PubMed=12402045; DOI=10.1038/ncb871;
RA Carroll C.W., Morgan D.O.;
RT "The Doc1 subunit is a processivity factor for the anaphase-promoting
RT complex.";
RL Nat. Cell Biol. 4:880-887(2002).
RN [7]
RP SUBUNIT, AND ROLE IN APC/C SUBSTRATE RECOGNITION.
RX PubMed=12574115; DOI=10.1093/emboj/cdg084;
RA Passmore L.A., McCormack E.A., Au S.W., Paul A., Willison K.R.,
RA Harper J.W., Barford D.;
RT "Doc1 mediates the activity of the anaphase-promoting complex by
RT contributing to substrate recognition.";
RL EMBO J. 22:786-796(2003).
RN [8]
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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-250.
RX PubMed=11884135; DOI=10.1006/jmbi.2002.5399;
RA Au S.W., Leng X., Harper J.W., Barford D.;
RT "Implications for the ubiquitination reaction of the anaphase-promoting
RT complex from the crystal structure of the Doc1/Apc10 subunit.";
RL J. Mol. Biol. 316:955-968(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. 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 DOC1 is required, together with the coactivators CDH1 and CDC20, for
CC recognition and binding of the substrates.
CC {ECO:0000269|PubMed:12402045, ECO:0000269|PubMed:12574115}.
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.
CC {ECO:0000269|PubMed:12574115, ECO:0000269|PubMed:9348530}.
CC -!- INTERACTION:
CC P53068; P53886: APC1; NbExp=9; IntAct=EBI-2603, EBI-29017;
CC P53068; P09798: CDC16; NbExp=13; IntAct=EBI-2603, EBI-4208;
CC P53068; P38042: CDC27; NbExp=4; IntAct=EBI-2603, EBI-4249;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1364 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APC10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89016.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA96959.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z49149; CAA89016.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z72762; CAA96959.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z72761; CAA96958.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07879.1; -; Genomic_DNA.
DR PIR; S53941; S53941.
DR RefSeq; NP_011274.2; NM_001181106.1.
DR PDB; 1GQP; X-ray; 2.20 A; A/B=30-250.
DR PDBsum; 1GQP; -.
DR AlphaFoldDB; P53068; -.
DR SMR; P53068; -.
DR BioGRID; 33000; 231.
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-1128N; -.
DR IntAct; P53068; 18.
DR MINT; P53068; -.
DR STRING; 4932.YGL240W; -.
DR MaxQB; P53068; -.
DR PaxDb; P53068; -.
DR PRIDE; P53068; -.
DR EnsemblFungi; YGL240W_mRNA; YGL240W; YGL240W.
DR GeneID; 852611; -.
DR KEGG; sce:YGL240W; -.
DR SGD; S000003209; DOC1.
DR VEuPathDB; FungiDB:YGL240W; -.
DR eggNOG; KOG3437; Eukaryota.
DR GeneTree; ENSGT00390000013722; -.
DR HOGENOM; CLU_039415_2_0_1; -.
DR InParanoid; P53068; -.
DR OMA; WVALTFE; -.
DR BioCyc; YEAST:G3O-30712-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P53068; -.
DR PRO; PR:P53068; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53068; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:SGD.
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; IGI:SGD.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA: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 CDD; cd08366; APC10; 1.
DR InterPro; IPR016901; APC10/Doc1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR12936; PTHR12936; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR SMART; SM01337; APC10; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..250
FT /note="Anaphase-promoting complex subunit DOC1"
FT /id="PRO_0000174016"
FT DOMAIN 60..246
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT MUTAGEN 94
FT /note="S->F: In DOC1-1; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9348530"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1GQP"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 117..133
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1GQP"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:1GQP"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 193..206
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1GQP"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1GQP"
SQ SEQUENCE 250 AA; 28777 MW; F3C58B1BB986442D CRC64;
MDPIGINKVL DHLAPSELIK PVKSCHNKPS VLVLDDRIVD AATKDLYVNG FQEEIQYQNP
TPENLQHMFH QGIEILDSAR MINVTHLALW KPSSFKLGNP VDFALDDNYD TFWQSDGGQP
HQLDIMFSKR MDICVMAIFF SMIADESYAP SLVKVYAGHS PSDARFYKML EVRNVNGWVA
LRFLDNREDD QLLKCQFIRL LFPVNHENGK DTHLRGIRLY VPSNEPHQDT HEWAQTLPET
NNVFQDAILR
