COPE_BOVIN
ID COPE_BOVIN Reviewed; 308 AA.
AC Q28104; A1L5B2; Q2TBL7; Q9N286;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Coatomer subunit epsilon;
DE AltName: Full=Epsilon-coat protein;
DE Short=Epsilon-COP;
GN Name=COPE; Synonyms=COPE1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8132710; DOI=10.1083/jcb.124.6.883;
RA Hara-Kuge S., Kuge O., Orci L., Amherdt M., Ravazzola M., Wieland F.,
RA Rothman J.;
RT "En bloc incorporation of coatomer subunits during the assembly of COP-
RT coated vesicles.";
RL J. Cell Biol. 124:883-892(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hahn Y., Chung J.H.;
RT "Identification of epsilon-COP genes from various organisms.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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. The 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 with 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC -!- INTERACTION:
CC Q28104; Q27954: COPA; NbExp=5; IntAct=EBI-620457, EBI-620400;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by RCHY1 in the presence of androgen, leading to
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
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DR EMBL; X76980; CAA54287.1; -; mRNA.
DR EMBL; AB042117; BAA94967.1; -; mRNA.
DR EMBL; BT029899; ABM06145.1; -; mRNA.
DR EMBL; BC109963; AAI09964.1; -; mRNA.
DR PIR; I46019; I46019.
DR RefSeq; NP_788846.1; NM_176673.1.
DR PDB; 3MKR; X-ray; 2.60 A; A=17-307.
DR PDBsum; 3MKR; -.
DR AlphaFoldDB; Q28104; -.
DR SMR; Q28104; -.
DR IntAct; Q28104; 1.
DR STRING; 9913.ENSBTAP00000001071; -.
DR PaxDb; Q28104; -.
DR PeptideAtlas; Q28104; -.
DR PRIDE; Q28104; -.
DR Ensembl; ENSBTAT00000001071; ENSBTAP00000001071; ENSBTAG00000000810.
DR GeneID; 338085; -.
DR KEGG; bta:338085; -.
DR CTD; 11316; -.
DR VEuPathDB; HostDB:ENSBTAG00000000810; -.
DR VGNC; VGNC:27595; COPE.
DR eggNOG; KOG3081; Eukaryota.
DR GeneTree; ENSGT00390000003478; -.
DR HOGENOM; CLU_049363_0_0_1; -.
DR InParanoid; Q28104; -.
DR OMA; MIVLSQH; -.
DR OrthoDB; 1161199at2759; -.
DR TreeFam; TF313390; -.
DR EvolutionaryTrace; Q28104; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000000810; Expressed in ascending colon and 108 other tissues.
DR ExpressionAtlas; Q28104; baseline and differential.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0099612; P:protein localization to axon; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006822; Coatomer_esu.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10805; PTHR10805; 1.
DR PIRSF; PIRSF016478; Coatomer_esu; 1.
DR SUPFAM; SSF48452; SSF48452; 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; Transport; Ubl conjugation.
FT CHAIN 1..308
FT /note="Coatomer subunit epsilon"
FT /id="PRO_0000193849"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14579"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14579"
FT CONFLICT 94
FT /note="D -> H (in Ref. 1; CAA54287)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="T -> N (in Ref. 4; AAI09964)"
FT /evidence="ECO:0000305"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 285..304
FT /evidence="ECO:0007829|PDB:3MKR"
SQ SEQUENCE 308 AA; 34481 MW; 219385CA17A3B7DA CRC64;
MAPPAPGPAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKPSSPERDV ERDVFLYRAY
LAQRKYGVVL DEIKPSSAPE LQAVRMFAEY LASDSRRDAI VAELDREMSR SVDVTNTTFL
LMAASIYFYD QNPDAALRTL HQGDSLECMA MTVQILLKLD RLDLARKELK KMQDQDEDAT
LTQLATAWVS LAAGGEKLQD AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGVLQ
EALDKDSGHP ETLINLVVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY RAKENDFDRL
VLQYAPSA
