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Entry: A0A0D2F478_9EURO
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ID   A0A0D2F478_9EURO        Unreviewed;       523 AA.
AC   A0A0D2F478;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN   ORFNames=Z517_04467 {ECO:0000313|EMBL:KIW81442.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW81442.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW81442.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW81442.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) 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. 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}.
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DR   EMBL; KN846971; KIW81442.1; -; Genomic_DNA.
DR   RefSeq; XP_013285250.1; XM_013429796.1.
DR   AlphaFoldDB; A0A0D2F478; -.
DR   STRING; 1442368.A0A0D2F478; -.
DR   GeneID; 25303957; -.
DR   VEuPathDB; FungiDB:Z517_04467; -.
DR   HOGENOM; CLU_019988_3_0_1; -.
DR   OrthoDB; 205756at2759; -.
DR   Proteomes; UP000053029; 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   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364018}.
FT   DOMAIN          277..523
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          179..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          136..176
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   523 AA;  57982 MW;  5FA6F53C758B442B CRC64;
     MVVLAASICT RGGKPLLSRS FREIPKSRIE ALLASFPKLA DSSTQHTTVE QENVRFVYQP
     LDELYLVLIT NKQSNILQDI DSLHLFGQVV TSICKKAEER EILRNAFELL SAFDELVTMG
     YRENLSLSQI KTFLEMESHE ERIQEIIARN KELEASEERK RKAKQLELQR KEAARSAAYG
     RGIAPKMPQQ PVYTPPTRPE SSYDSYEAEK NKTSNKFTAR STKGMQLGKK SKTSNAFAQV
     QQEIGTEEVP AVEPSAELPV RGLPTASTHD ATLSSPTTPI LVTIAETFSA KLSREGALKS
     MEVKGDLQLK ISDSALTKLA LSVQAVEGPL KAQFRTHPNV DKGLFTSQKI IQLKDTTKRF
     PLNNSIGVLR WRVTAPADHN TDVLPLTLTA WVNKSSSDGT YTITIEYELT NPASTTLRDV
     TLTIPYSSSE PSVSSFDAVY QVTGDSLEWT IGVIDAETSS GSFEFEAQAD DDAEFFPMTV
     NFEMSRTFVD VDVTGVKLLE GGLDEEVNFE KVIKARSEGF AIE
//
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