ID   COPE_PONAB              Reviewed;         308 AA.
AC   Q5RFR8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Coatomer subunit epsilon;
DE   AltName: Full=Epsilon-coat protein;
DE            Short=Epsilon-COP;
GN   Name=COPE;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. {ECO:0000250}.
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: Phosphorylated by PKA. {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; CR857084; CAH89389.1; -; mRNA.
DR   RefSeq; NP_001124585.1; NM_001131113.2.
DR   AlphaFoldDB; Q5RFR8; -.
DR   SMR; Q5RFR8; -.
DR   STRING; 9601.ENSPPYP00000010924; -.
DR   PRIDE; Q5RFR8; -.
DR   Ensembl; ENSPPYT00000011349; ENSPPYP00000010924; ENSPPYG00000009753.
DR   GeneID; 100171420; -.
DR   KEGG; pon:100171420; -.
DR   CTD; 11316; -.
DR   eggNOG; KOG3081; Eukaryota.
DR   GeneTree; ENSGT00390000003478; -.
DR   HOGENOM; CLU_049363_0_0_1; -.
DR   InParanoid; Q5RFR8; -.
DR   OMA; MIVLSQH; -.
DR   OrthoDB; 1161199at2759; -.
DR   TreeFam; TF313390; -.
DR   Proteomes; UP000001595; Chromosome 19.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..308
FT                   /note="Coatomer subunit epsilon"
FT                   /id="PRO_0000328665"
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   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14579"
SQ   SEQUENCE   308 AA;  34457 MW;  5154695227544FB7 CRC64;
     MAPPAPGPTS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPETDV ERDVFLYRAY
     LAQRKFGVVL DEIKPSSAPE LQAVRMFADY LAHESRRDSI VAELDREMSR SVDVTNTTFL
     LMAASIYLHD QNPDAALRAL HQGDSLECTA MTVQILLKLD RLDLARKELK RMQDLDEDAT
     LTQLATAWVS LATGGEKLQD AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGLLQ
     EALDKDSGYP ETLVNLIVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY QAKENDFDRL
     VLQYAPSA