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Protein

Coatomer subunit gamma-1

Gene

COPG1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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. 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 similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • intracellular protein transport Source: InterPro
  • intra-Golgi vesicle-mediated transport Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • COPI vesicle coat Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
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_0000193857Add
BLAST

Proteomic databases

PaxDbiP53620.
PRIDEiP53620.

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 similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GBF1Q925382EBI-8511600,EBI-359050From a different organism.

Protein-protein interaction databases

BioGridi160192. 1 interaction.
DIPiDIP-739N.
IntActiP53620. 1 interaction.
STRINGi9913.ENSBTAP00000017588.

Structurei

Secondary structure

1
874
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 307Combined sources
Helixi31 – 333Combined sources
Beta strandi36 – 383Combined sources
Helixi41 – 5717Combined sources
Helixi63 – 7412Combined sources
Helixi75 – 784Combined sources
Helixi82 – 9514Combined sources
Turni96 – 983Combined sources
Helixi102 – 1054Combined sources
Helixi106 – 1149Combined sources
Helixi118 – 13114Combined sources
Turni134 – 1363Combined sources
Helixi137 – 14812Combined sources
Helixi153 – 16614Combined sources
Turni167 – 1693Combined sources
Helixi171 – 1755Combined sources
Helixi178 – 1847Combined sources
Helixi190 – 20415Combined sources
Helixi208 – 21912Combined sources
Helixi226 – 23611Combined sources
Helixi264 – 27411Combined sources
Helixi292 – 2976Combined sources
Beta strandi298 – 3036Combined sources
Helixi304 – 3096Combined sources
Helixi609 – 61810Combined sources
Helixi621 – 6233Combined sources
Beta strandi644 – 65411Combined sources
Beta strandi656 – 66712Combined sources
Beta strandi672 – 68615Combined sources
Beta strandi688 – 6936Combined sources
Beta strandi695 – 6984Combined sources
Beta strandi704 – 7118Combined sources
Beta strandi722 – 73514Combined sources
Turni737 – 7393Combined sources
Beta strandi747 – 7526Combined sources
Beta strandi756 – 7583Combined sources
Helixi760 – 7634Combined sources
Beta strandi764 – 7663Combined sources
Helixi772 – 7798Combined sources
Beta strandi785 – 7939Combined sources
Helixi797 – 80812Combined sources
Turni814 – 8174Combined sources
Beta strandi824 – 83411Combined sources
Beta strandi839 – 86224Combined sources
Helixi863 – 87210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZDX-ray2.31A555-874[»]
3TJZX-ray2.90B/E1-355[»]
ProteinModelPortaliP53620.
SMRiP53620. Positions 604-874.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53620.

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

eggNOGiKOG1078. Eukaryota.
COG5240. LUCA.
HOGENOMiHOG000184434.
HOVERGENiHBG004368.
InParanoidiP53620.
KOiK17267.
OrthoDBiEOG75XGK5.
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.
IPR032154. Coatomer_g_Cpla.
IPR017106. Coatomer_gsu.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
PANTHERiPTHR10261. PTHR10261. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF16381. Coatomer_g_Cpla. 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.

P53620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK
60 70 80 90 100
ILYLINQGEH LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE
110 120 130 140 150
DVIIVTSSLT KDMTGKEDSY RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD
160 170 180 190 200
KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE AQEAASSDNI MVQYHALGLL
210 220 230 240 250
YHVRKNDRLA VSKMISKFTR HGLKSPFAYC MMIRVASRQL EDEDGSRDSP
260 270 280 290 300
LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
310 320 330 340 350
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDANRSI ATLAITTLLK
360 370 380 390 400
TGSEGSIDRL MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF
410 420 430 440 450
LFSMLREEGG FEYKRAIVDC IISIIEENAE SKETGLSHLC EFIEDCEFTV
460 470 480 490 500
LATRILHLLG QEGPRTSNPS KYIRFIYNRV VLEHAEVRAG AVSALAKFGA
510 520 530 540 550
QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK ALNAGYILNG
560 570 580 590 600
LAVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPLAEQR TESTPVTAAK
610 620 630 640 650
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC
660 670 680 690 700
TKHTFTDHMV FQFDCTNTLN DQTLENVTVQ MEPSEAYEVL CYVPARSLPY
710 720 730 740 750
NQPGTCYTLV ALPKEDPTAV ACTFSCVMKF TVKDCDPTTG EADDEGYEDE
760 770 780 790 800
YVLEDLEVTI ADHIQKVMKL NFEAAWDEVG DEFQKEETFT LSTIKTLEEA
810 820 830 840 850
VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI LVRSRLLLLD
860 870
TVTMQVTARS SEELPVDIVL ASVG
Length:874
Mass (Da):97,386
Last modified:October 1, 1996 - v1
Checksum:iA9072FA70C1A0005
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti684 – 6841S → T in AAI11323 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92987 mRNA. Translation: CAA63574.1.
BC111322 mRNA. Translation: AAI11323.1.
X70019 mRNA. Translation: CAA49616.1.
PIRiS33957.
RefSeqiNP_001032904.1. NM_001037815.2.
UniGeneiBt.65158.

Genome annotation databases

GeneIDi338055.
KEGGibta:338055.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92987 mRNA. Translation: CAA63574.1.
BC111322 mRNA. Translation: AAI11323.1.
X70019 mRNA. Translation: CAA49616.1.
PIRiS33957.
RefSeqiNP_001032904.1. NM_001037815.2.
UniGeneiBt.65158.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZDX-ray2.31A555-874[»]
3TJZX-ray2.90B/E1-355[»]
ProteinModelPortaliP53620.
SMRiP53620. Positions 604-874.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi160192. 1 interaction.
DIPiDIP-739N.
IntActiP53620. 1 interaction.
STRINGi9913.ENSBTAP00000017588.

Proteomic databases

PaxDbiP53620.
PRIDEiP53620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi338055.
KEGGibta:338055.

Organism-specific databases

CTDi22820.

Phylogenomic databases

eggNOGiKOG1078. Eukaryota.
COG5240. LUCA.
HOGENOMiHOG000184434.
HOVERGENiHBG004368.
InParanoidiP53620.
KOiK17267.
OrthoDBiEOG75XGK5.
TreeFamiTF300324.

Miscellaneous databases

EvolutionaryTraceiP53620.
NextBioi20812506.

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.
IPR032154. Coatomer_g_Cpla.
IPR017106. Coatomer_gsu.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
PANTHERiPTHR10261. PTHR10261. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF16381. Coatomer_g_Cpla. 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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway."
    Harter C., Pavel J., Coccia F., Draken E., Wegehingel S., Tschochner H., Wieland F.T.
    Proc. Natl. Acad. Sci. U.S.A. 93:1902-1906(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "Gamma-COP, a coat subunit of non-clathrin-coated vesicles with homology to Sec21p."
    Stenbeck G., Schreiner R., Herrmann D., Auerbach S., Lottspeich F., Rothman J.E., Wieland F.T.
    FEBS Lett. 314:195-198(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 312-874, PROTEIN SEQUENCE OF 578-591; 605-618; 796-806 AND 862-874, SUBCELLULAR LOCATION.
    Tissue: Brain.
  4. "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles."
    Waters M.G., Serafini T., Rothman J.E.
    Nature 349:248-251(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  5. "Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins."
    Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.
    Mol. Cell. Biol. 26:8011-8021(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMED2; TMED3; TMED7; TMED9 AND TMED10.
  6. "Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain."
    Hoffman G.R., Rahl P.B., Collins R.N., Cerione R.A.
    Mol. Cell 12:615-625(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 554-874.

Entry informationi

Entry nameiCOPG1_BOVIN
AccessioniPrimary (citable) accession number: P53620
Secondary accession number(s): Q2T9Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 116 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.