ID A0A1I8PCH3_STOCA Unreviewed; 525 AA.
AC A0A1I8PCH3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN Name=106085118 {ECO:0000313|EnsemblMetazoa:SCAU006836-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU006836-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU006836-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU006836-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 {ECO:0000256|RuleBase:RU364018}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|RuleBase:RU364018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364018,
CC ECO:0000256|RuleBase:RU366052}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000256|RuleBase:RU364018,
CC ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052};
CC Cytoplasmic side {ECO:0000256|RuleBase:RU364018,
CC ECO:0000256|RuleBase:RU366052}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU364018,
CC ECO:0000256|RuleBase:RU366052}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}.
CC Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC Delta-COP subfamily. {ECO:0000256|ARBA:ARBA00010516,
CC ECO:0000256|RuleBase:RU364018}.
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 RefSeq; XP_013104619.1; XM_013249165.1.
DR AlphaFoldDB; A0A1I8PCH3; -.
DR STRING; 35570.A0A1I8PCH3; -.
DR EnsemblMetazoa; SCAU006836-RA; SCAU006836-PA; SCAU006836.
DR GeneID; 106085118; -.
DR KEGG; scac:106085118; -.
DR VEuPathDB; VectorBase:SCAU006836; -.
DR OrthoDB; 205756at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:UniProtKB-UniRule.
DR CDD; cd09254; AP_delta-COPI_MHD; 1.
DR CDD; cd14830; Delta_COP_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
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; COATOMER SUBUNIT DELTA; 1.
DR PANTHER; PTHR10121:SF0; COATOMER SUBUNIT DELTA; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364018};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU364018};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364018};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU364018}; Membrane {ECO:0000256|RuleBase:RU364018};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU364018};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364018}.
FT DOMAIN 284..525
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 171..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 58122 MW; 80EE48F5FFB8A9D3 CRC64;
MVLIAAAVCT KNGKVIISRQ FVEMTKARIE GLLAAFPKLM TAGKQHTYVE TDSVRYVYQP
MEKLYMLLIT TKASNILEDL ETLRLFSKVI PEYCHTLEEK EILENAFNLI FAFDEIVALG
YRESVNLAQI KTFVEMDSHE EKLYQAVRQT QEREARQKMR EKAKELQRQR METAKRGGPM
SGGMGSRSSG GFSSDGFGAN TTNMGMGGIS GGPSIEMDKP IAPKPQKPVS RNALKLGGKT
KDVDSFVDQL NSEGEKIAKL TPASAGNNSA VTAAKAKIIS DVPMDSIHLK MEDKLVVRIG
RDGGLQQFEL SGLLTLRISE ENMGRIKVAL ENNDAHGIQL QTHPNVDKEL FKTRSIIGLK
NPAKPFPLNT DVGVLKWRFV TQDESAIPLT INCWPSENGE GGCDVNIEYE LEAQHLELQD
VSIAIPLPMS VQPQVAEYDG TYNYDARKHI LQWNIPVIDA ANKSGSMEFS CNSSIPGDFF
PVQVTFVSKT PYAAIKAKDV VLVDTEAPVK FSTENILYAD KYEVV
//