COPD_DICDI
ID COPD_DICDI Reviewed; 540 AA.
AC Q55EZ6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Coatomer subunit delta;
DE AltName: Full=Delta-coat protein;
DE Short=Delta-COP;
GN Name=copd; ORFNames=DDB_G0268702;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000004; EAL72940.1; -; Genomic_DNA.
DR RefSeq; XP_646874.1; XM_641782.1.
DR AlphaFoldDB; Q55EZ6; -.
DR STRING; 44689.DDB0305305; -.
DR PaxDb; Q55EZ6; -.
DR PRIDE; Q55EZ6; -.
DR EnsemblProtists; EAL72940; EAL72940; DDB_G0268702.
DR GeneID; 8616557; -.
DR KEGG; ddi:DDB_G0268702; -.
DR dictyBase; DDB_G0268702; copD.
DR eggNOG; KOG2635; Eukaryota.
DR HOGENOM; CLU_019988_3_0_1; -.
DR InParanoid; Q55EZ6; -.
DR OMA; YDARKHV; -.
DR PhylomeDB; Q55EZ6; -.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q55EZ6; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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..540
FT /note="Coatomer subunit delta"
FT /id="PRO_0000330861"
FT DOMAIN 304..540
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 169..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60335 MW; C83068FF0AECF0B8 CRC64;
MVVLAAAICT KNGKALLSRQ FSEMTKSRVE GLLAAFPKLI GLGRQHTFIE TENIRYVYQP
LESLYIVLIT NKNSNILEDL ETLHLLAKLV PEYSNFDEYD ISKNAFELIF TFDEVIAMGY
KERVTLQQIK HFISMESHEE ERFRMEEKIK QKEAQILASS KAKEIERMRH EEMLRGKRSG
GYTGISGGGG MGSGGMGSNQ YRDNDRDNYH SNNNNNNNNN NNNNNNNNNN RDRDRGDSPN
TSRPSAASSG SQGGMILGGK SGTNKNSAIA QVLKEEKIVE KVEDVEQLLD SQISQIPETP
TVPQEGVHIT VEESFTSFVE SDGTVESIDI KGGLSVQIND QSLGKVKVNL KQGKLSKQFQ
FITHPNIDKA LFGEQSVLRL RDGGKGFPSG GILKWRCKTN QESMMPIRVN CWPSPGRDST
TVNLEYDSLV GYELKSVFIV IPNPTSNAPI INQFDGLYEY DNKQKCVIWK IPLIDDSNRQ
GSMEFSVKGN TQSFFPVKIQ FTASQTICDT TVGSVFVEDS NQSTNFSTET TLSVDTYEIK
