COPG1_BOVIN
ID COPG1_BOVIN Reviewed; 874 AA.
AC P53620; Q2T9Q0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Coatomer subunit gamma-1;
DE AltName: Full=Gamma-1-coat protein;
DE Short=Gamma-1-COP;
GN Name=COPG1; Synonyms=COPG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8700856; DOI=10.1073/pnas.93.5.1902;
RA Harter C., Pavel J., Coccia F., Draken E., Wegehingel S., Tschochner H.,
RA Wieland F.T.;
RT "Nonclathrin coat protein gamma, a subunit of coatomer, binds to the
RT cytoplasmic dilysine motif of membrane proteins of the early secretory
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1902-1906(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 312-874, PROTEIN SEQUENCE OF 578-591;
RP 605-618; 796-806 AND 862-874, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=1360908; DOI=10.1016/0014-5793(92)80973-k;
RA Stenbeck G., Schreiner R., Herrmann D., Auerbach S., Lottspeich F.,
RA Rothman J.E., Wieland F.T.;
RT "Gamma-COP, a coat subunit of non-clathrin-coated vesicles with homology to
RT Sec21p.";
RL FEBS Lett. 314:195-198(1992).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1898986; DOI=10.1038/349248a0;
RA Waters M.G., Serafini T., Rothman J.E.;
RT "'Coatomer': a cytosolic protein complex containing subunits of non-
RT clathrin-coated Golgi transport vesicles.";
RL Nature 349:248-251(1991).
RN [5]
RP INTERACTION WITH TMED2; TMED3; TMED7; TMED9 AND TMED10.
RX PubMed=16940185; DOI=10.1128/mcb.01055-06;
RA Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.;
RT "Coatomer, the coat protein of COPI transport vesicles, discriminates
RT endoplasmic reticulum residents from p24 proteins.";
RL Mol. Cell. Biol. 26:8011-8021(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 554-874.
RX PubMed=14527408; DOI=10.1016/j.molcel.2003.08.002;
RA Hoffman G.R., Rahl P.B., Collins R.N., Cerione R.A.;
RT "Conserved structural motifs in intracellular trafficking pathways:
RT structure of the gammaCOP appendage domain.";
RL Mol. Cell 12:615-625(2003).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors. Required for limiting lipid storage in lipid droplets.
CC Involved in lipid homeostasis by regulating the presence of perilipin
CC family members PLIN2 and PLIN3 at the lipid droplet surface and
CC promoting the association of adipocyte triglyceride lipase (PNPLA2)
CC with the lipid droplet surface to mediate lipolysis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with
CC ZNF289/ARFGAP2 through its C-terminal appendage domain (By similarity).
CC Interacts with EGFR upon EGF treatment; interaction is essential for
CC regulation of EGF-dependent nuclear transport of EGFR by retrograde
CC trafficking from the Golgi to the ER (By similarity). Interacts with
CC COPB1 (By similarity). Interacts with TMED10 (via C-terminus).
CC Interacts with TMED2, TMED3, TMED7 and TMED9. {ECO:0000250,
CC ECO:0000269|PubMed:16940185, ECO:0000269|PubMed:1898986}.
CC -!- INTERACTION:
CC P53620; Q92538: GBF1; Xeno; NbExp=2; IntAct=EBI-8511600, EBI-359050;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. Predominantly located
CC in the cis-Golgi apparatus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; X92987; CAA63574.1; -; mRNA.
DR EMBL; BC111322; AAI11323.1; -; mRNA.
DR EMBL; X70019; CAA49616.1; -; mRNA.
DR PIR; S33957; S33957.
DR RefSeq; NP_001032904.1; NM_001037815.2.
DR PDB; 1PZD; X-ray; 2.31 A; A=555-874.
DR PDB; 3TJZ; X-ray; 2.90 A; B/E=1-355.
DR PDBsum; 1PZD; -.
DR PDBsum; 3TJZ; -.
DR AlphaFoldDB; P53620; -.
DR SMR; P53620; -.
DR BioGRID; 160192; 2.
DR DIP; DIP-739N; -.
DR IntAct; P53620; 1.
DR MINT; P53620; -.
DR STRING; 9913.ENSBTAP00000017588; -.
DR PaxDb; P53620; -.
DR PeptideAtlas; P53620; -.
DR PRIDE; P53620; -.
DR GeneID; 338055; -.
DR KEGG; bta:338055; -.
DR CTD; 22820; -.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; P53620; -.
DR OrthoDB; 255234at2759; -.
DR TreeFam; TF300324; -.
DR EvolutionaryTrace; P53620; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..874
FT /note="Coatomer subunit gamma-1"
FT /id="PRO_0000193857"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 322..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..874
FT /note="Interaction with ZNF289/ARFGAP2"
FT /evidence="ECO:0000250"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
FT CONFLICT 684
FT /note="S -> T (in Ref. 2; AAI11323)"
FT /evidence="ECO:0000305"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 304..309
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:1PZD"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 644..654
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 656..667
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 672..686
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 688..693
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 704..711
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 722..735
FT /evidence="ECO:0007829|PDB:1PZD"
FT TURN 737..739
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 747..752
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:1PZD"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:1PZD"
FT HELIX 772..779
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 785..793
FT /evidence="ECO:0007829|PDB:1PZD"
FT HELIX 797..808
FT /evidence="ECO:0007829|PDB:1PZD"
FT TURN 814..817
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 824..834
FT /evidence="ECO:0007829|PDB:1PZD"
FT STRAND 839..862
FT /evidence="ECO:0007829|PDB:1PZD"
FT HELIX 863..872
FT /evidence="ECO:0007829|PDB:1PZD"
SQ SEQUENCE 874 AA; 97386 MW; A9072FA70C1A0005 CRC64;
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDSY
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VSKMISKFTR HGLKSPFAYC MMIRVASRQL
EDEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDANRSI ATLAITTLLK TGSEGSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFSMLREEGG FEYKRAIVDC
IISIIEENAE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPRTSNPS KYIRFIYNRV
VLEHAEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LAVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPLAEQR TESTPVTAAK
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTDHMV
FQFDCTNTLN DQTLENVTVQ MEPSEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV
ACTFSCVMKF TVKDCDPTTG EADDEGYEDE YVLEDLEVTI ADHIQKVMKL NFEAAWDEVG
DEFQKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS SEELPVDIVL ASVG
