Reviewed, UniProtKB/Swiss-Prot P53068 (APC10_YEAST)

Names and origin

Protein names

Recommended name:
    Anaphase-promoting complex subunit DOC1
Alternative name(s):
    Destruction of cyclin B protein 1

Gene names

Name:	DOC1
Synonyms:	APC10
Ordered Locus Names:	YGL240W
ORF Names:	HRC283

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. DOC1 is required, together with the coactivators CDH1 and CDC20, for recognition and binding of the substrates.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1.
Subcellular location	Cytoplasm. Nucleus.
Miscellaneous	Present with 1364 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the APC10 family. Contains 1 DOC domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Ref.5 Inferred from direct assay. Source: SGD cyclin catabolic process Traceable author statement. Source: SGD mitotic metaphase/anaphase transition Traceable author statement. Source: SGD mitotic sister chromatid segregation Traceable author statement. Source: SGD mitotic spindle elongation Traceable author statement. Source: SGD
Cellular component	anaphase-promoting complex Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	enzyme regulator activity Ref.5 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 250

250

Anaphase-promoting complex subunit DOC1

Regions

Domain

60 – 246

187

DOC

Experimental info

Mutagenesis

94

1

S → F in DOC1-1; G2/M cell cycle arrest at 37 degrees Celsius

Secondary structure

1

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250

Helix Strand Turn

Details...

Beta strand

31 – 35

5

Helix

41 – 43

3

Turn

44 – 46

3

Helix

62 – 77

16

Beta strand

79 – 83

5

Helix

85 – 87

3

Beta strand

88 – 93

6

Helix

101 – 104

4

Beta strand

105 – 107

3

Beta strand

117 – 133

17

Beta strand

135 – 141

7

Helix

142 – 145

4

Helix

146 – 148

3

Beta strand

149 – 160

12

Turn

161 – 163

3

Beta strand

165 – 174

10

Beta strand

176 – 181

6

Beta strand

193 – 206

14

Beta strand

213 – 215

3

Beta strand

217 – 222

6

Sequences

	Sequence		Length	Mass (Da)
	P53068-1 [UniParc]. Last modified November 9, 2004. Version 2. Checksum: F3C58B1BB986442D	FASTA	250	28,777
	10 20 30 40 50 60 MDPIGINKVL DHLAPSELIK PVKSCHNKPS VLVLDDRIVD AATKDLYVNG FQEEIQYQNP 70 80 90 100 110 120 TPENLQHMFH QGIEILDSAR MINVTHLALW KPSSFKLGNP VDFALDDNYD TFWQSDGGQP 130 140 150 160 170 180 HQLDIMFSKR MDICVMAIFF SMIADESYAP SLVKVYAGHS PSDARFYKML EVRNVNGWVA 190 200 210 220 230 240 LRFLDNREDD QLLKCQFIRL LFPVNHENGK DTHLRGIRLY VPSNEPHQDT HEWAQTLPET 250 NNVFQDAILR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII, reveals the presence of eight open reading frames." Vandenbol M., Durand P., Portetelle D., Hilger F. Yeast 11:1519-1523(1995) [PubMed: 8750240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[4]	"A novel yeast screen for mitotic arrest mutants identifies DOC1, a new gene involved in cyclin proteolysis." Hwang L.H., Murray A.W. Mol. Biol. Cell 8:1877-1887(1997) [PubMed: 9348530] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF SER-94.
[5]	"The Doc1 subunit is a processivity factor for the anaphase-promoting complex." Carroll C.W., Morgan D.O. Nat. Cell Biol. 4:880-887(2002) [PubMed: 12402045] [Abstract] Cited for: FUNCTION, SUBSTRATE RECOGNITION.
[6]	"Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition." Passmore L.A., McCormack E.A., Au S.W., Paul A., Willison K.R., Harper J.W., Barford D. EMBO J. 22:786-796(2003) [PubMed: 12574115] [Abstract] Cited for: SUBUNIT, ROLE IN APC/C SUBSTRATE RECOGNITION.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit." Au S.W., Leng X., Harper J.W., Barford D. J. Mol. Biol. 316:955-968(2002) [PubMed: 11884135] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-250.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z49149 Genomic DNA. Translation: CAA89016.1. Different initiation.
Z72762 Genomic DNA. Translation: CAA96959.1. Different initiation.
Z72761 Genomic DNA. Translation: CAA96958.1.

PIR

S53941.

RefSeq

NP_011274.2.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQP	X-ray	2.20	A/B	30-250	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1128N.

IntAct

P53068.

Proteomic databases

PeptideAtlas

P53068.

Genome annotation databases

Ensembl

YGL240W. Saccharomyces cerevisiae. [Contig view]

GeneID

852611.

GenomeReviews

Gene locus YGL240W in contig Y13135_GR.

KEGG

sce:YGL240W.

NMPDR

fig|4932.3.peg.2377.

Organism-specific databases

CYGD

YGL240w.

SGD

S000003209. DOC1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P53068.

Gene expression databases

GermOnline

YGL240W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004939. APC10.
[Graphical view]

PANTHER

PTHR12936. APC10. 1 hit.

Pfam

PF03256. APC10. 1 hit.
[Graphical view]

PROSITE

PS51284. DOC. 1 hit.
[Graphical view]

ProDom

P53068.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

P53068.

ProtoNet

Search...

Entry information

Entry name

APC10_YEAST

Accession

Primary (citable) accession number: P53068

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 9, 2004
Last modified:	July 22, 2008
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)