ID A0A094EEK3_9PEZI Unreviewed; 515 AA.
AC A0A094EEK3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN ORFNames=V498_09450 {ECO:0000313|EMBL:KFY76969.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY76969.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY76969.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY76969.1}.
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DR EMBL; JPKA01004108; KFY76969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EEK3; -.
DR HOGENOM; CLU_019988_3_0_1; -.
DR Proteomes; UP000029270; 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 276..515
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 154..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57516 MW; CE8EA2A30CDB8B0C CRC64;
MVVLAASICT RGGKAIVSRQ FREMQRSRVE ALLAGFPKLA DRGTQHTTVE QDNVRFVYQP
LDELYMVLIT NRQSNILQDI DSLHLFAQVV TSICRSLDER EILRNAYELL SAFDEIVTLG
YRENLSISQI KTFLEMESHE ERIQEIISRN KELEATEERK RKAKQLEMQR KEVSRTGRNA
PPRAPNYPTY TPAARTPTTE TYDSYEAEKN KSFKTTAPKG KGMQLGKKSK TTDMFERVRG
EMGVEAEDTS PLVPVQTPTA PAGHARSSSL QSGLDRDAIH VTIAETINAK LTREGSVNSI
EVKGDLQLRI SDESFTKVKL ELTANASHGA QFKTHPNVDR PLFNSSKAIQ MSNASKGFPV
NNSVGVLRWR ATPKVDDSSA IPITFTVWVN KGSDNNYTVT VEYELTGGDA LKDTAVIIPF
ATSEPVVASF DATYEVSGDS LEWTIGMVDD DNATGSFEFE AQAEDENEFF PMHIRFSKTT
PYVDVDVTAV SLVEMDEEVT FSKEIKSITE SYVIE
//
