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Reviewed, UniProtKB/Swiss-Prot Q9Y678 (COPG_HUMAN)

Last modified July 7, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Coatomer subunit gamma
Alternative name(s):
    Gamma-coat protein
      Short name=Gamma-COP
Gene names
Name: COPG
Synonyms: COPG1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with ZNF289/ARFGAP2 through its C-terminal appendage domain. Ref.4

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.

Sequence similarities

Belongs to the COPG family.

Contains 4 HEAT repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Coatomer subunit gamma
PRO_0000193858

Regions

Repeat64 – 10138HEAT 1
Repeat283 – 32038HEAT 2
Repeat322 – 35534HEAT 3
Repeat356 – 39237HEAT 4
Region609 – 874266Interaction with ZNF289/ARFGAP2

Natural variations

Natural variant6811M → T: dbSNP rs15648.
VAR_054039

Experimental info

Mutagenesis7761W → S: Loss of interaction with ZNF289/ARFGAP2. Ref.4

Secondary structure

........................................... 874
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y678-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A2FAB492C598EC98

FASTA87497,718
        10         20         30         40         50         60 
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH 

        70         80         90        100        110        120 
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY 

       130        140        150        160        170        180 
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE 

       190        200        210        220        230        240 
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL 

       250        260        270        280        290        300 
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK 

       310        320        330        340        350        360 
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL 

       370        380        390        400        410        420 
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC 

       430        440        450        460        470        480 
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV 

       490        500        510        520        530        540 
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK 

       550        560        570        580        590        600 
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK 

       610        620        630        640        650        660 
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV 

       670        680        690        700        710        720 
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV 

       730        740        750        760        770        780 
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG 

       790        800        810        820        830        840 
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI 

       850        860        870 
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG 

« Hide

References

« Hide 'large scale' references
[1]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[3]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]"Gamma-COP appendage domain -- structure and function."
Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.
Traffic 5:79-88(2004) [PubMed: 14690497] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH ZNF289, MUTAGENESIS OF TRP-776.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF100756 mRNA. Translation: AAD43020.1.
BC066650 mRNA. Translation: AAH66650.1.
IPIIPI00783982.
RefSeqNP_057212.1.
UniGeneHs.518250

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1R4XX-ray1.90A608-874[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y678. 10 interactions.

Proteomic databases

PeptideAtlasQ9Y678.
PRIDEQ9Y678.

Genome annotation databases

EnsemblENSG00000181789. Homo sapiens. [Contig view]
GeneID22820.
KEGGhsa:22820.
UCSCuc003els.1. human.

Organism-specific databases

GeneCardsGC03P130451.
H-InvDBHIX0023057.
HGNCHGNC:2236. COPG.
PharmGKBPA26752.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9Y678.
OMAQ9Y678. LNFEAAW.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9Y678.
BgeeQ9Y678.
CleanExHS_COPG.
GermOnlineENSG00000181789. Homo sapiens.

Family and domain databases

InterProIPR011989. ARM-like.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR017106. Coatomer_gamma_subunit.
IPR014863. Coatomer_gsu_app.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
Gene3DG3DSA:3.30.310.30. AP2_A_adaptin_C. 1 hit.
G3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:2.60.40.1480. Coatomer_gsu_app_Ig-like-sub. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF08752. Gamma-COP. 1 hit.
[Graphical view]
PIRSFPIRSF037093. Coatomer_gamma_subunit. 1 hit.
PROSITEPS50077. HEAT_REPEAT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43212.

Entry information

Entry nameCOPG_HUMAN
AccessionPrimary (citable) accession number: Q9Y678
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: July 7, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents