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Database: UniProt
Entry: A0A168EYF2_9HYPO
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Original site: A0A168EYF2_9HYPO 
ID   A0A168EYF2_9HYPO        Unreviewed;       551 AA.
AC   A0A168EYF2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU366052};
GN   ORFNames=AAL_01847 {ECO:0000313|EMBL:KZZ99275.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ99275.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ99275.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ99275.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ99275.1}.
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DR   EMBL; AZGY01000003; KZZ99275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168EYF2; -.
DR   STRING; 1081109.A0A168EYF2; -.
DR   OrthoDB; 205756at2759; -.
DR   Proteomes; UP000078544; 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:UP000078544};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366052}.
FT   DOMAIN          313..551
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          207..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  61104 MW;  B8E1D82FEBFCCCDF CRC64;
     MALPARAEGV LRTKSTYIFY MHDKPPSLPL GLCSLTRWFA VVLAASICTR GGKAVLSRQF
     REMPRSRIEA LLASFPKLAD SGTQHTTVEQ DNVRFVYQPL DELYMVLITN KQSNILQDID
     SLHLFAQVVT SACRTLDERE ILRNAYELLS AFDELVTLGY RENLTMSQIK TFLEMESHEE
     RIQEIIARNK ELEAAEERKR KAKQLEMQRK EAARGSRGMP RPSAYPTYTP PSRPSAADTF
     DSYEAEKNKT FNKPLVVKGK GMQLGKKSRT NDMFERVRGD MGGESDETPL VTPALATAPV
     EAAEPRVSST LDRDAVHVTI SEAISATLTR EGALNSLSIT GDLALRISDP SLTKIKLGLQ
     AIPSHGAAFR THPNVDRNLF NSAKTIQMSN TARGFPVNNA VAVLRWRASP NVSDSSACPI
     TFTVWMNNDG GKFGITVEYE LTGGDALRDV SVVIPYAGSE PVVSSFDAAY EVSGDMLEWN
     IGSVDSDNPN GTFEFEAESS DENDFFPMSI RFSKTTPYID VDVKNVSLLE EDEDITFSKE
     IRSNADNYSV E
//
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