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Database: UniProt
Entry: A0A1Q5UF78_9EURO
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ID   A0A1Q5UF78_9EURO        Unreviewed;       579 AA.
AC   A0A1Q5UF78;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU366052};
GN   ORFNames=PENSUB_3352 {ECO:0000313|EMBL:OKP11131.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP11131.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKP11131.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP11131.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) 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.
CC       {ECO:0000256|RuleBase:RU366052}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000256|RuleBase:RU366052}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366052}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|RuleBase:RU366052};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|RuleBase:RU366052}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000256|RuleBase:RU366052}; Peripheral membrane
CC       protein {ECO:0000256|RuleBase:RU366052}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU366052}. Membrane
CC       {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:RU366052}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKP11131.1}.
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DR   EMBL; MNBE01000298; OKP11131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5UF78; -.
DR   STRING; 1316194.A0A1Q5UF78; -.
DR   OrthoDB; 205756at2759; -.
DR   Proteomes; UP000186955; 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:RU366052};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU366052};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU366052}; Membrane {ECO:0000256|RuleBase:RU366052};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU366052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366052}.
FT   DOMAIN          339..579
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          195..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  64411 MW;  5B0DE2EC0DBC708F CRC64;
     MARRKGRVGS LYLSAGRHGM SIPGLYVCCP ANHLSHIIQV VLAASICTRG GKAVLSRQFR
     DIPRSRIEAL LASFPKLADS QTQHTTVEQD NVRFVYQPLN ELYIVLITNR QSNILQDIDS
     LHLFAQVTTS ICKSLDEREI LRNAFELLSA YDELVTLGYR ENLSLSQIKT FLEMESHEER
     IQEIIERNKE LEASEERKRK AKQLEMQRKE AARTGRGAAP RAPNYPVYTP PSRPAVPDTY
     DSYEAEKKKT FAKYVHDYTR WEIVTMDLLV SNSVILSRPL PTRGKGMQLG KKSKATDIYE
     KVRGDLGPGI EESSPLVTPQ ASTPVQEPAS ARESLTADRE SIHVTIAETI SATLTREGAL
     KSFEVKGDLQ LRITDPAFTK LRLDLRANPT QGAQFRTHPN VDKALFTSTS AIQLKDTTKR
     FPANNAIGVL RWRVASSADN AEILPITFTV WVNKGSDTTT VTVEYELTGT DSLRDVVVTI
     PYGASEPAVA SFDAVYEVSG DSLDWNLGVV DESNPSGSFE FESTGDGDEN EFFPMSVRFT
     KTQPFVDVDV LDASLLEMEG ESAGFSKDIR SVAENFLIE
//
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