ID   COPD_CAEEL              Reviewed;         515 AA.
AC   Q09236;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Probable coatomer subunit delta;
DE   AltName: Full=Delta-coat protein;
DE            Short=Delta-COP;
GN   Name=copd-1 {ECO:0000312|WormBase:C13B9.3};
GN   ORFNames=C13B9.3 {ECO:0000312|WormBase:C13B9.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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       (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   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       Delta-COP subfamily. {ECO:0000305}.
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DR   EMBL; FO080523; CCD64377.1; -; Genomic_DNA.
DR   PIR; C88487; C88487.
DR   RefSeq; NP_498463.1; NM_066062.4.
DR   AlphaFoldDB; Q09236; -.
DR   SMR; Q09236; -.
DR   BioGRID; 41156; 12.
DR   DIP; DIP-26714N; -.
DR   STRING; 6239.C13B9.3; -.
DR   iPTMnet; Q09236; -.
DR   EPD; Q09236; -.
DR   PaxDb; Q09236; -.
DR   PeptideAtlas; Q09236; -.
DR   PRIDE; Q09236; -.
DR   EnsemblMetazoa; C13B9.3.1; C13B9.3.1; WBGene00015734.
DR   GeneID; 175940; -.
DR   KEGG; cel:CELE_C13B9.3; -.
DR   UCSC; C13B9.3; c. elegans.
DR   CTD; 175940; -.
DR   WormBase; C13B9.3; CE01778; WBGene00015734; copd-1.
DR   eggNOG; KOG2635; Eukaryota.
DR   GeneTree; ENSGT00390000017207; -.
DR   HOGENOM; CLU_019988_3_0_1; -.
DR   InParanoid; Q09236; -.
DR   OMA; YDARKHV; -.
DR   OrthoDB; 1027200at2759; -.
DR   PhylomeDB; Q09236; -.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q09236; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015734; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR027059; Coatomer_dsu.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR028565; MHD.
DR   PANTHER; PTHR10121; PTHR10121; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   SUPFAM; SSF49447; SSF49447; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..515
FT                   /note="Probable coatomer subunit delta"
FT                   /id="PRO_0000193846"
FT   DOMAIN          276..515
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   REGION          161..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  56646 MW;  E4CA3BC9D580AC78 CRC64;
     MVLIAACILS KTGKLLVARQ FVNDMMRSRL EGLVDAFPKL IGNEKEAATR QHTFVETDSV
     RYVYHPLDNI YLVLVTTKNS NILEDLETLR LFVRVIPEYC RSNEEKEILA HDFDLIFAFD
     EVVTLGYRES VNLAQIRTFT EMDSHEERVF MQIKEAQEKA AKQAMAEKAK ELKRAQKEAL
     SRGLKPSYQS STGISSSSTP NAAAVSEPAA PRPSAPKGPI GGGKALKLGG KTNNEDDFLD
     TLRQQGQSIA PVQKASLSGG VSSLAAPIST APRVKREVVH VRTEEKINTR VSRDGGLESG
     EVQATVTLSI GSPEFIPISI KMNNGSAAGT QLQVHPNLDK KEWQSSSTLK IKPNGKPYPV
     NSDVGILKWK MALSEEEQLP ISFNCWPQES SDGVQVNIEY TLQREDITLN NVRIIVPLPT
     ATAPSVGECD GEYEYHKTKN VIVWSLAVID SSNSSGTLEF SVPNGHCDHF FPVSVGFTSE
     NLFVPITVQK VVKNDGSPVT YSVETTFNSE NFEIV