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P53622 (COPA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit alpha
Alternative name(s):
Alpha-coat protein
Short name=Alpha-COP
Retrieval from endoplasmic reticulum protein 1
Secretory protein 22
Suppressor of osmo-sensitivity 1
Gene names
Name:COP1
Synonyms:RET1, SEC33, SOO1
Ordered Locus Names:YDL145C
ORF Names:D1578
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Ref.8

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27. Interacts with KEI1 (via C-terminal region). Ref.8 Ref.10

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Ref.2 Ref.6 Ref.8

Miscellaneous

Present with 15200 molecules/cell in log phase SD medium.

Sequence similarities

Contains 6 WD repeats.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12011201Coatomer subunit alpha
PRO_0000050910

Regions

Repeat9 – 3931WD 1
Repeat51 – 8131WD 2
Repeat93 – 12331WD 3
Repeat135 – 16531WD 4
Repeat207 – 23731WD 5
Repeat251 – 28131WD 6

Experimental info

Sequence conflict7531F → L in CAA86588. Ref.1
Sequence conflict7531F → L in CAA58712. Ref.2
Sequence conflict9051I → T in CAA86588. Ref.1
Sequence conflict9051I → T in CAA58712. Ref.2
Sequence conflict10061P → L in CAA86588. Ref.1
Sequence conflict10061P → L in CAA58712. Ref.2
Sequence conflict1027 – 10282DA → NT in CAA86588. Ref.1
Sequence conflict1027 – 10282DA → NT in CAA58712. Ref.2

Secondary structure

................................................................................. 1201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53622 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D3589073106F5570

FASTA1,201135,607
        10         20         30         40         50         60 
MKMLTKFESK STRAKGIAFH PSRPWVLVAL FSSTIQLWDY RMGTLLHRFE DHEGPVRGLD 

        70         80         90        100        110        120 
FHPTQPIFVS AGDDYTIKVW SLDTNKCLYT LTGHLDYVRT VFFHRELPWI ISASDDQTIR 

       130        140        150        160        170        180 
IWNWQNRKEI ACLTGHNHFV MCAQFHPTDD LIVSASLDET IRIWDISGLR KRHSAPGTSS 

       190        200        210        220        230        240 
FEEQMSAQQN LLDGSLGDCV VKFILEGHTR GVNWASFHPT LPLIVSGSDD RQVKLWRMSA 

       250        260        270        280        290        300 
TKAWEVDTCR GHTNNVDSVI FHPHQNLIIS VGEDKTLRVW DLDKRTPVKQ FKRENDRFWL 

       310        320        330        340        350        360 
IAAHPHINLF GAAHDSGIMV FKLDRERPCS FIHQNQLFFV NAEKQIQSFN FQKRVASLPY 

       370        380        390        400        410        420 
ASLKGIGQPW DAFRSISYNP SQHSVLVNEA NGKFALVILP KQPVGAVEPT SVTQDTGNFA 

       430        440        450        460        470        480 
TFVGRNRFVV YNKNTESVEV RSLENKVTRN IKVEETVRTI VAAGPGSVLV IHPREVILYD 

       490        500        510        520        530        540 
VQQGKKVSQL AVKNVKYVSW SLDGQYVALM SKHTITLATK KLELINSMHE TIRIKSAAWD 

       550        560        570        580        590        600 
ETGVLIYSTL NHIRYSLLNG DRGIIKTLEK TLYITKVQGK LVYCLNREGE IEILTIDPTE 

       610        620        630        640        650        660 
YRFKKALVNK NFPEVLRLIK DSNLVGQNII SYLQKSGYPE IALQFVQDPH IRFDLALEYG 

       670        680        690        700        710        720 
NLDVALDEAK KLNDSSTWER LIQEALAQGN ASLAEMIYQT QHSFDKLSFL YLVTGDVNKL 

       730        740        750        760        770        780 
SKMQNIAQTR EDFGSMLLNT FYNNSTKERS SIFAEGGSLP LAYAVAKANG DEAAASAFLE 

       790        800        810        820        830        840 
QAEVDEQDVT LPDQMDASNF VQRPVISKPL EKWPLKEAEL SYFEKAVLGQ IDDLTIDDET 

       850        860        870        880        890        900 
PAVNTTQEQE EPLGEENFND EDIGEDEGAW DLGDEDLDVG EELPEEVEQG EITSPAQEVE 

       910        920        930        940        950        960 
TAIWIKNSKL PAVLVAAGAF DAAVQALSKQ VGVVKLEPLK KYFTNIYEGC RTYIPSTPCE 

       970        980        990       1000       1010       1020 
LPAQLGYVRA YDDTVSEDQI LPYVPGLDVV NEKMNEGYKN FKLNKPDIAI ECFREAIYRI 

      1030       1040       1050       1060       1070       1080 
TLLMVDDAED EKLAHKILET AREYILGLSI ELERRSLKEG NTVRMLELAA YFTKAKLSPI 

      1090       1100       1110       1120       1130       1140 
HRTNALQVAM SQHFKHKNFL QASYFAGEFL KIISSGPRAE QARKIKNKAD SMASDAIPID 

      1150       1160       1170       1180       1190       1200 
FDPYAKFDIC AATYKPIYED TPSVSDPLTG SKYVITEKDK IDRIAMISKI GAPASGLRIR 


V 

« Hide

References

« Hide 'large scale' references
[1]"Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum."
Letourneur F., Gaynor E.C., Hennecke S., Demolliere C., Durden R., Emr S.D., Riezman H., Cosson P.
Cell 79:1199-1207(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
Strain: PC70.
[2]"Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth."
Gerich B., Orci L., Tschochner H., Lottspeich F., Ravazolla M., Amherdt M., Wieland F., Harter C.
Proc. Natl. Acad. Sci. U.S.A. 92:3229-3233(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, SUBCELLULAR LOCATION.
Strain: RS453.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Analysis of a 23 kb region on the left arm of yeast chromosome IV."
Delaveau T.T.D., Blugeon C., Jacq C., Perea J.
Yeast 12:1587-1592(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-1201.
Strain: ATCC 96604 / S288c / FY1679.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast."
Gabriely G., Kama R., Gerst J.E.
Mol. Cell. Biol. 27:526-540(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS27.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization."
Sato K., Noda Y., Yoda K.
Mol. Biol. Cell 20:4444-4457(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KEI1.
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46617 Genomic DNA. Translation: CAA86588.1.
X83754 Genomic DNA. Translation: CAA58712.1.
Z74193 Genomic DNA. Translation: CAA98719.1.
Z74192 Genomic DNA. Translation: CAA98718.1.
X97751 Genomic DNA. Translation: CAA66346.1.
BK006938 Genomic DNA. Translation: DAA11713.1.
PIRERBYA. S67692.
RefSeqNP_010136.1. NM_001180205.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MKQX-ray2.50B/D/F642-818[»]
3MV2X-ray2.90A/C/E900-1201[»]
3MV3X-ray3.25A/C/E900-1201[»]
ProteinModelPortalP53622.
SMRP53622. Positions 1-818, 899-1201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31916. 164 interactions.
DIPDIP-2582N.
IntActP53622. 37 interactions.
MINTMINT-422687.
STRING4932.YDL145C.

Proteomic databases

MaxQBP53622.
PaxDbP53622.
PeptideAtlasP53622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL145C; YDL145C; YDL145C.
GeneID851410.
KEGGsce:YDL145C.

Organism-specific databases

CYGDYDL145c.
SGDS000002304. COP1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00520000055597.
HOGENOMHOG000195913.
KOK05236.
OMAFWVLGAH.
OrthoDBEOG7TN016.

Enzyme and pathway databases

BioCycYEAST:G3O-29542-MONOMER.

Gene expression databases

GenevestigatorP53622.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR016391. Coatomer_asu.
IPR010714. Coatomer_asu_C.
IPR006692. Coatomer_WD-assoc_reg.
IPR020472. G-protein_beta_WD-40_rep.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF04053. Coatomer_WDAD. 1 hit.
PF06957. COPI_C. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PIRSFPIRSF003354. Coatomer_alpha_subunit. 1 hit.
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50969. SSF50969. 1 hit.
SSF50978. SSF50978. 2 hits.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53622.
NextBio968591.
PROP53622.

Entry information

Entry nameCOPA_YEAST
AccessionPrimary (citable) accession number: P53622
Secondary accession number(s): D6VRK3, Q07595
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references