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Q9QZE5 (COPG1_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 gamma-1
Alternative name(s):
Gamma-1-coat protein
Short name=Gamma-1-COP
Gene names
Name:Copg1
Synonyms:Copg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. Ref.5

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 By similarity. Interacts with EGFR upon EGF treatment; interaction is essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER By similarity. Interacts with COPB1 By similarity. Interacts with TMED10 (via C-terminus). Interacts with TMED2, TMED3, TMED7 and TMED9 By similarity.

Subcellular location

Cytoplasmcytosol. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. 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. Predominantly located in the cis-Golgi apparatus By similarity. Ref.4

Sequence similarities

Belongs to the COPG family.

Contains 4 HEAT repeats.

Sequence caution

The sequence BAC36811.1 differs from that shown. Reason: Frameshift at position 864.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Coatomer subunit gamma-1
PRO_0000304939

Regions

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

Experimental info

Sequence conflict8111H → P in AAH24896. Ref.3
Sequence conflict8411L → F in BAE31753. Ref.2
Sequence conflict8411L → F in BAE30713. Ref.2
Sequence conflict8411L → F in BAE30269. Ref.2
Sequence conflict8431R → H in BAC36811. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QZE5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CAF3201AD1118728

FASTA87497,513
        10         20         30         40         50         60 
MLKKFDKKDE ESGGGSNPLQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH 

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

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

       190        200        210        220        230        240 
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VSKMISKFTR 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 QEGPKTNNPS KYIRFIYNRV 

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

       550        560        570        580        590        600 
ALNAGYILNG LTVSIPGLEK ALQQYTLEPS EKPFDLKSVP LATTPMAEQR PESTATAAVK 

       610        620        630        640        650        660 
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC TKHTFSDHLV 

       670        680        690        700        710        720 
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL SYVPARSLPY NQPGTCYTLV ALPTEDPTAV 

       730        740        750        760        770        780 
ACTFSCVMKF TVKDCDPNTG EIDEEGYEDE YVLEDLEVTV ADHIQKVMKV NFEAAWDEVG 

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

       850        860        870 
LVRSRLLLLD TVTMQVTARS SEELPVDIIL ASVG 

« Hide

References

« Hide 'large scale' references
[1]"Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution."
Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L., Rhee M., Chung J.H.
FEBS Lett. 482:31-36(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryo, Kidney and Spleen.
[3]"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: Czech II and FVB/N.
Tissue: Mammary tumor and Salivary gland.
[4]"Differential localization of coatomer complex isoforms within the Golgi apparatus."
Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I., Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B., Wieland F.T.
Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"COPI complex is a regulator of lipid homeostasis."
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S., Oliver B.
PLoS Biol. 6:E292-E292(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF187079 mRNA. Translation: AAF01325.1.
AK049417 mRNA. Translation: BAC33743.1.
AK077461 mRNA. Translation: BAC36811.1. Frameshift.
AK147895 mRNA. Translation: BAE28212.1.
AK151284 mRNA. Translation: BAE30269.1.
AK151816 mRNA. Translation: BAE30713.1.
AK153142 mRNA. Translation: BAE31753.1.
AK164280 mRNA. Translation: BAE37716.1.
AK169256 mRNA. Translation: BAE41019.1.
AK171950 mRNA. Translation: BAE42743.1.
AK172519 mRNA. Translation: BAE43046.1.
BC008553 mRNA. Translation: AAH08553.1.
BC024686 mRNA. Translation: AAH24686.1.
BC024896 mRNA. Translation: AAH24896.1.
CCDSCCDS39549.1.
RefSeqNP_059505.1. NM_017477.2.
UniGeneMm.258785.

3D structure databases

ProteinModelPortalQ9QZE5.
SMRQ9QZE5. Positions 20-311, 604-874.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207587. 1 interaction.
IntActQ9QZE5. 1 interaction.
MINTMINT-1865908.

PTM databases

PhosphoSiteQ9QZE5.

Proteomic databases

MaxQBQ9QZE5.
PaxDbQ9QZE5.
PRIDEQ9QZE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113607; ENSMUSP00000109237; ENSMUSG00000030058.
GeneID54161.
KEGGmmu:54161.
UCSCuc009cug.1. mouse.

Organism-specific databases

CTD22820.
MGIMGI:1858696. Copg1.

Phylogenomic databases

eggNOGCOG5240.
GeneTreeENSGT00390000016313.
HOGENOMHOG000184434.
HOVERGENHBG004368.
InParanoidQ922C6.
KOK17267.
OMAEFHGLGP.
OrthoDBEOG75XGK5.
PhylomeDBQ9QZE5.
TreeFamTF300324.

Gene expression databases

ArrayExpressQ9QZE5.
BgeeQ9QZE5.
CleanExMM_COPG.
GenevestigatorQ9QZE5.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1480. 1 hit.
3.30.310.30. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
IPR017106. Coatomer_gsu.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
PANTHERPTHR10261. PTHR10261. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF08752. COP-gamma_platf. 1 hit.
[Graphical view]
PIRSFPIRSF037093. Coatomer_gamma_subunit. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCOPG1. mouse.
NextBio311004.
PROQ9QZE5.
SOURCESearch...

Entry information

Entry nameCOPG1_MOUSE
AccessionPrimary (citable) accession number: Q9QZE5
Secondary accession number(s): Q3U9F4 expand/collapse secondary AC list , Q8BP96, Q8R1A7, Q922C6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 102 of the entry and version 1 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