ID A0A1V8SB29_9PEZI Unreviewed; 521 AA.
AC A0A1V8SB29;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN ORFNames=B0A48_17724 {ECO:0000313|EMBL:OQN96217.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN96217.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQN96217.1}.
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DR EMBL; NAJO01000070; OQN96217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SB29; -.
DR STRING; 1507870.A0A1V8SB29; -.
DR InParanoid; A0A1V8SB29; -.
DR OrthoDB; 205756at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364018}.
FT DOMAIN 282..521
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 168..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..163
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 57174 MW; 2EB720CF8C4FABF2 CRC64;
MVILSAAITT RSGKPILARQ FRQMQRSRVE ALLASFPKLA DTASQHTTVE QDNVRFVYQP
LDELYMVLIT NRQSNILQDI STLHLFAQVV GSICKSLDER EITRCAFELL SAFDEVVTQG
YRENLTLSQI KTFLDMESHE ERIQEIIARN KELEATEERK RRAKQLEMQR KEQTRAARLG
GGTALPRTPT YPTYTAPVTT PAMPDTYDSY TAAKNEKFSK PLASRGKGMQ LGKKTKNTSM
FDQVRSDMGP EAEANTPLAG VPAPTVQPSL PPASRPAASS DKEPIQITIA ETLSAKFSRE
GALESFEVKG DLQLRISDPS LTQVKLSLSV GDTKNAQLNA HPKVDKAVFK SENAVQLTDT
SKGFPANNSI QVVRWRLSAK PDDVPDPPIK FTVWTSELSA NTYSITVEYE LTGGAPLKDV
TVSIPYTTSE PSVTSFDAIY EVSGDSIDWT IGDIDDSNAS GSFEFEASAG SEADFFPMAV
RFAMGRPWVE VDVGSVELIG GGEEVGFGKD VKCVADGYLI V
//
