ID A0A068S3U4_9FUNG Unreviewed; 511 AA.
AC A0A068S3U4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
GN ORFNames=LCOR_07016.1 {ECO:0000313|EMBL:CDH55921.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55921.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH55921.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH55921.1}.
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DR EMBL; CBTN010000033; CDH55921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S3U4; -.
DR STRING; 1263082.A0A068S3U4; -.
DR VEuPathDB; FungiDB:LCOR_07016.1; -.
DR OrthoDB; 205756at2759; -.
DR Proteomes; UP000027586; 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:UP000027586};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364018}.
FT DOMAIN 270..511
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 208..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..176
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 208..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 57142 MW; 095539032103A906 CRC64;
MVVLAAAIVT KSGKAVISRQ FREMQRSRIE GLLASFPKLT STGHQHTTVE TEHVRYVYQP
LEELFMVLIT NRQSNILQDI ESLHLFARVV TDICRSCDEQ DILRNAFELL CAFDEIISEG
YRENVNLAQV KSIIEMESHE ERIQEIIAKN KEQEAKEELK RRAKQFEMQK KEAQKRGQGF
MQGNFSSQGN YMGGRFSPAL EPTVQTTIDS PAFNSRSSTP PASSGTKARG MQLGRKPKST
DLFEAIKTEV EEPLLKSSRS AASSTITKEV EGLHVWIEER VSMAANRDGG LEQMEVRGVL
TLRVGDAANA RVRLTLQAAD DPAINFKTHP NVDKNAFKND KMVQMRDVSR PFPVQQNLEV
VRWKFSTRDE TAVPLSINCW PSPAGDGTCD VNIEYELEAD HLELRDVVVS IPLPAEPAAT
VHSADGSYFV DRQRRVLDWQ LPVINSSNKS GSLECNVPGE DANGFFPVMV SFVSERLICD
VDVIEAHNLE TDSPAQITKE ILLAADDYTI G
//
