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Q8CIE6 (COPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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

Cleaved into the following 2 chains:

  1. Xenin
    Alternative name(s):
    Xenopsin-related peptide
  2. Proxenin
Gene names
Name:Copa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors By similarity.

Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor By similarity.

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1 By similarity.

Subcellular location

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

Xenin: Secreted By similarity.

Sequence similarities

Contains 6 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12241224Coatomer subunit alpha
PRO_0000327496
Peptide1 – 3535Proxenin
PRO_0000327497
Peptide1 – 2525Xenin
PRO_0000327498

Regions

Repeat7 – 3731WD 1
Repeat49 – 7931WD 2
Repeat91 – 12131WD 3
Repeat133 – 16331WD 4
Repeat203 – 23331WD 5
Repeat247 – 27731WD 6

Amino acid modifications

Modified residue1731Phosphoserine By similarity
Modified residue1851Phosphothreonine By similarity
Modified residue4021Phosphoserine By similarity

Experimental info

Sequence conflict7611S → T in AAH24070. Ref.2
Sequence conflict7611S → T in AAH47429. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CIE6 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 48AB72AD9CBDDD6B

FASTA1,224138,432
        10         20         30         40         50         60 
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH 

        70         80         90        100        110        120 
KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW 

       130        140        150        160        170        180 
NWQSRTCVCV LTGHNHYVMC AQFHPSEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD 

       190        200        210        220        230        240 
VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW 

       250        260        270        280        290        300 
EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH 

       310        320        330        340        350        360 
PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG 

       370        380        390        400        410        420 
SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW 

       430        440        450        460        470        480 
VARNRFAVLD RMHSLLIKNL KNEITKKIQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK 

       490        500        510        520        530        540 
RTLASVKISK VKYVIWSADM SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV 

       550        560        570        580        590        600 
FIYTTSNHIK YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK 

       610        620        630        640        650        660 
LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS LALECGNIEI 

       670        680        690        700        710        720 
ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF DKLSFLYLIT GNLEKLRKMM 

       730        740        750        760        770        780 
KIAEIRKDMS GHYQNALYLG DVSERVRILK NCGQKSLAYL SAATHGLDEE AESLKETFDP 

       790        800        810        820        830        840 
EKETIPDIDP NAKLLQPPAP IMPLDTNWPL LTVSKGFFEG SIASKGKGGA LAADIDIDTV 

       850        860        870        880        890        900 
GTEGWGEDAE LQLDEDGFVE APEGLGEDVL GKGQEEGGGW DVEEDLELPP ELDVPSGVSG 

       910        920        930        940        950        960 
SAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI QFGPYKQLFL 

       970        980        990       1000       1010       1020 
QTYARGRTTY QALPCLPSMY SYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG 

      1030       1040       1050       1060       1070       1080 
KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLCMEIER KKLPKETLDQ 

      1090       1100       1110       1120       1130       1140 
QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ 

      1150       1160       1170       1180       1190       1200 
TRKILSACEK NPTDACQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI 

      1210       1220 
CRVTTVTEIG KDVIGLRISP LQFR 

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver and Mammary tumor.
[3]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC158930 Genomic DNA. No translation available.
BC024070 mRNA. Translation: AAH24070.1.
BC047429 mRNA. Translation: AAH47429.1.
CCDSCCDS35780.1.
RefSeqNP_034068.3. NM_009938.4.
UniGeneMm.30041.
Mm.412417.

3D structure databases

ProteinModelPortalQ8CIE6.
SMRQ8CIE6. Positions 1-810, 905-1224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198835. 20 interactions.
IntActQ8CIE6. 19 interactions.
MINTMINT-4116336.

PTM databases

PhosphoSiteQ8CIE6.

Proteomic databases

MaxQBQ8CIE6.
PaxDbQ8CIE6.
PRIDEQ8CIE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000135192; ENSMUSP00000118179; ENSMUSG00000026553.
GeneID12847.
KEGGmmu:12847.
UCSCuc007dpn.2. mouse.

Organism-specific databases

CTD1314.
MGIMGI:1334462. Copa.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00520000055597.
HOGENOMHOG000195913.
HOVERGENHBG005379.
InParanoidQ8CIE6.
KOK05236.
OrthoDBEOG78WKQX.
TreeFamTF105693.

Gene expression databases

ArrayExpressQ8CIE6.
BgeeQ8CIE6.
GenevestigatorQ8CIE6.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR016391. Coatomer_asu.
IPR010714. Coatomer_asu_C.
IPR006692. Coatomer_WD-assoc_reg.
IPR020472. G-protein_beta_WD-40_rep.
IPR011048. Haem_d1.
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. 6 hits.
[Graphical view]
PIRSFPIRSF003354. Coatomer_alpha_subunit. 1 hit.
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
SSF51004. SSF51004. 3 hits.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOPA. mouse.
NextBio282392.
PROQ8CIE6.
SOURCESearch...

Entry information

Entry nameCOPA_MOUSE
AccessionPrimary (citable) accession number: Q8CIE6
Secondary accession number(s): E9Q075
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot