ID U1G4D3_ENDPU Unreviewed; 264 AA.
AC U1G4D3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN ORFNames=EPUS_02938 {ECO:0000313|EMBL:ERF72147.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF72147.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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 -!- 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; KE721112; ERF72147.1; -; Genomic_DNA.
DR RefSeq; XP_007802216.1; XM_007804025.1.
DR AlphaFoldDB; U1G4D3; -.
DR GeneID; 19237987; -.
DR eggNOG; KOG2635; Eukaryota.
DR HOGENOM; CLU_076799_0_0_1; -.
DR OMA; FIAFDEV; -.
DR OrthoDB; 205756at2759; -.
DR Proteomes; UP000019373; 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; cd14830; Delta_COP_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR027059; Coatomer_dsu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR10121; COATOMER SUBUNIT DELTA; 1.
DR PANTHER; PTHR10121:SF0; COATOMER SUBUNIT DELTA; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364018};
KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU364018};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU364018};
KW Golgi apparatus {ECO:0000256|RuleBase:RU364018};
KW Membrane {ECO:0000256|RuleBase:RU364018};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU364018};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364018}.
FT DOMAIN 25..149
FT /note="AP complex mu/sigma subunit"
FT /evidence="ECO:0000259|Pfam:PF01217"
FT REGION 186..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 29966 MW; 82B873F08C21F1E2 CRC64;
MVSLSRTPIY YNTEAFVQVV LAASICTRGG KAVLSRQFRE IARSRVEALL ASFPKLAVSG
TQHTTVEQDN VRFVYQPLDE LYMVLITNRQ SNILQDIDSL HLFAQVVTSI CKKLDEREIS
RNAFELLSAF DELVTLGYRE NLSLTQIKTF LEMESHEERI QEIIARNKEL EVSEERKRKA
KQLEMQRKEA ARSAAFGRGV APKVPQYPTH EPPSRPTVRE THGSYEAEKN KTLNKPLATR
GKGMQLGKKT KTTPFQEVSE AAQP
//
