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Q9QZE5

- COPG1_MOUSE

UniProt

Q9QZE5 - COPG1_MOUSE

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Protein

Coatomer subunit gamma-1

Gene

Copg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. establishment of Golgi localization Source: Ensembl
  2. intracellular protein transport Source: InterPro
  3. organelle transport along microtubule Source: Ensembl
  4. vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_227904. COPI Mediated Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit gamma-1
Alternative name(s):
Gamma-1-coat protein
Short name:
Gamma-1-COP
Gene namesi
Name:Copg1
Synonyms:Copg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1858696. Copg1.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; 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. Predominantly located in the cis-Golgi apparatus.By similarity

GO - Cellular componenti

  1. COPI vesicle coat Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Coatomer subunit gamma-1PRO_0000304939Add
BLAST

Proteomic databases

MaxQBiQ9QZE5.
PaxDbiQ9QZE5.
PRIDEiQ9QZE5.

PTM databases

PhosphoSiteiQ9QZE5.

Expressioni

Gene expression databases

BgeeiQ9QZE5.
CleanExiMM_COPG.
ExpressionAtlasiQ9QZE5. baseline and differential.
GenevestigatoriQ9QZE5.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi207587. 1 interaction.
IntActiQ9QZE5. 1 interaction.
MINTiMINT-1865908.

Structurei

3D structure databases

ProteinModelPortaliQ9QZE5.
SMRiQ9QZE5. Positions 20-349, 472-533, 604-874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati64 – 10138HEAT 1Add
BLAST
Repeati283 – 32038HEAT 2Add
BLAST
Repeati322 – 35534HEAT 3Add
BLAST
Repeati356 – 39237HEAT 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni609 – 874266Interaction with ZNF289/ARFGAP2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the COPG family.Curated
Contains 4 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5240.
GeneTreeiENSGT00390000016313.
HOGENOMiHOG000184434.
HOVERGENiHBG004368.
InParanoidiQ9QZE5.
KOiK17267.
OMAiEFHGLGP.
OrthoDBiEOG75XGK5.
PhylomeDBiQ9QZE5.
TreeFamiTF300324.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1480. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR011989. 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]
PANTHERiPTHR10261. PTHR10261. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF08752. COP-gamma_platf. 1 hit.
[Graphical view]
PIRSFiPIRSF037093. Coatomer_gamma_subunit. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9QZE5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKKFDKKDE ESGGGSNPLQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK
60 70 80 90 100
ILYLINQGEH LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE
110 120 130 140 150
DVIIVTSSLT KDMTGKEDNY RGPAVRALCQ ITDSTMLQAV ERYMKQAIVD
160 170 180 190 200
KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE AQEAASSDNI MVQYHALGLL
210 220 230 240 250
YHVRKNDRLA VSKMISKFTR HGLKSPFAYC MMIRVASKQL EEEDGSRDSP
260 270 280 290 300
LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
310 320 330 340 350
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK
360 370 380 390 400
TGSESSIDRL MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF
410 420 430 440 450
LFTMLREEGG FEYKRAIVDC IISIIEENSE SKETGLSHLC EFIEDCEFTV
460 470 480 490 500
LATRILHLLG QEGPKTNNPS KYIRFIYNRV VLEHEEVRAG AVSALAKFGA
510 520 530 540 550
QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK ALNAGYILNG
560 570 580 590 600
LTVSIPGLEK ALQQYTLEPS EKPFDLKSVP LATTPMAEQR PESTATAAVK
610 620 630 640 650
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC
660 670 680 690 700
TKHTFSDHLV FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL SYVPARSLPY
710 720 730 740 750
NQPGTCYTLV ALPTEDPTAV ACTFSCVMKF TVKDCDPNTG EIDEEGYEDE
760 770 780 790 800
YVLEDLEVTV ADHIQKVMKV NFEAAWDEVG DEFEKEETFT LSTIKTLEEA
810 820 830 840 850
VGNIVKFLGM HPCERSDKVP ENKNTHTLLL AGVFRGGHDI LVRSRLLLLD
860 870
TVTMQVTARS SEELPVDIIL ASVG
Length:874
Mass (Da):97,513
Last modified:May 1, 2000 - v1
Checksum:iCAF3201AD1118728
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti811 – 8111H → P in AAH24896. (PubMed:15489334)Curated
Sequence conflicti841 – 8411L → F in BAE31753. (PubMed:16141072)Curated
Sequence conflicti841 – 8411L → F in BAE30713. (PubMed:16141072)Curated
Sequence conflicti841 – 8411L → F in BAE30269. (PubMed:16141072)Curated
Sequence conflicti843 – 8431R → H in BAC36811. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39549.1.
RefSeqiNP_059505.1. NM_017477.2.
UniGeneiMm.258785.

Genome annotation databases

EnsembliENSMUST00000113607; ENSMUSP00000109237; ENSMUSG00000030058.
GeneIDi54161.
KEGGimmu:54161.
UCSCiuc009cug.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS39549.1.
RefSeqi NP_059505.1. NM_017477.2.
UniGenei Mm.258785.

3D structure databases

ProteinModelPortali Q9QZE5.
SMRi Q9QZE5. Positions 20-349, 472-533, 604-874.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207587. 1 interaction.
IntActi Q9QZE5. 1 interaction.
MINTi MINT-1865908.

PTM databases

PhosphoSitei Q9QZE5.

Proteomic databases

MaxQBi Q9QZE5.
PaxDbi Q9QZE5.
PRIDEi Q9QZE5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000113607 ; ENSMUSP00000109237 ; ENSMUSG00000030058 .
GeneIDi 54161.
KEGGi mmu:54161.
UCSCi uc009cug.1. mouse.

Organism-specific databases

CTDi 22820.
MGIi MGI:1858696. Copg1.

Phylogenomic databases

eggNOGi COG5240.
GeneTreei ENSGT00390000016313.
HOGENOMi HOG000184434.
HOVERGENi HBG004368.
InParanoidi Q9QZE5.
KOi K17267.
OMAi EFHGLGP.
OrthoDBi EOG75XGK5.
PhylomeDBi Q9QZE5.
TreeFami TF300324.

Enzyme and pathway databases

Reactomei REACT_227904. COPI Mediated Transport.

Miscellaneous databases

ChiTaRSi Copg1. mouse.
NextBioi 311004.
PROi Q9QZE5.
SOURCEi Search...

Gene expression databases

Bgeei Q9QZE5.
CleanExi MM_COPG.
ExpressionAtlasi Q9QZE5. baseline and differential.
Genevestigatori Q9QZE5.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
2.60.40.1480. 1 hit.
3.30.310.30. 1 hit.
InterProi IPR011989. 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 ]
PANTHERi PTHR10261. PTHR10261. 1 hit.
Pfami PF01602. Adaptin_N. 1 hit.
PF08752. COP-gamma_platf. 1 hit.
[Graphical view ]
PIRSFi PIRSF037093. Coatomer_gamma_subunit. 1 hit.
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: SUBCELLULAR LOCATION.
  5. Cited for: FUNCTION.

Entry informationi

Entry nameiCOPG1_MOUSE
AccessioniPrimary (citable) accession number: Q9QZE5
Secondary accession number(s): Q3U9F4
, Q8BP96, Q8R1A7, Q922C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3