ID A0A395GNS8_9EURO Unreviewed; 955 AA.
AC A0A395GNS8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN ORFNames=BO80DRAFT_364878 {ECO:0000313|EMBL:RAK97034.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK97034.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK97034.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK97034.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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|PIRNR:PIRNR005727}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|PIRNR:PIRNR005727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR005727}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR005727}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane
CC protein {ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR005727}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; KZ824467; RAK97034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GNS8; -.
DR STRING; 1448316.A0A395GNS8; -.
DR VEuPathDB; FungiDB:BO80DRAFT_364878; -.
DR OrthoDB; 151169at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR011710; Coatomer_bsu_C.
DR InterPro; IPR016460; COPB1.
DR InterPro; IPR029446; COPB1_appendage_platform_dom.
DR PANTHER; PTHR10635; COATOMER SUBUNIT BETA; 1.
DR PANTHER; PTHR10635:SF0; COATOMER SUBUNIT BETA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF07718; Coatamer_beta_C; 1.
DR Pfam; PF14806; Coatomer_b_Cpla; 1.
DR PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR005727};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR005727};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005727};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 21..492
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 679..815
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 820..946
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
SQ SEQUENCE 955 AA; 106467 MW; 8844DAA4E00BD5EC CRC64;
MASFLENAYS LVHQDNTADQ PSLQELKLQL EKGTDETKME TMRRIITIML NGDPMPQLLM
HIIRFVMPSR SKPLKKLLYF YYEICPKLDA NGKLKQEMIL VCNGIRNDLQ HANEYIRGNT
LRFLCKLREP ELIEPLLSSA RSCLDHRHAY VRKNAVWAVA SIFQHSESLI PDAPELIQAF
LDTETDGTCK RNAFAALMSI SHQKSLEYLS STFDSIPNTD ELLQLAELEF IRKDAVQNAQ
NKARYLRLIF DLLDASTSTV IYEAATSLTA LTSNPVAVKA AASKLIELCI KEADNNVKLI
VLDRVDQLRI RNEGVLDDLT MEILRVLSSP DIDVRRKALG IALEMVSSKN VEEIVMLLKK
ELAKTVDEQY EKNSEYRQLL IQSIHNCAIK FSEIAASVVD LLMDFIADFN NNSAVDVISF
VKEVVEKFPA LRTSIVDRLV STLSEVRAGK VYRGVLWVVG EYSLEERDIR EAWKRIRASL
GEIPILASEQ RLLDEVPEDA ALKEQVNGHS KPSAPTGSRK VLADGTYATE SALTSQSAAA
ARLEAVKAAQ KPPLRQLILD GDYYLATVLS STLTKLVMRH SEVSEDVART NALRAEAMLI
MISIIRVGQS HFVKAPIDED SVDRVMCCVR SLAEFSQRKE LETTFLEDTR TAFRAMVQVE
DKKRAAKEAV EKAKTAVQVD DAIPIRQFTK KAALEGAEEI ELDLVKATGG DSTVETVSSK
LSRVVQLTGF SDPVYAEAYV TVHQFDIVLD VLLVNQTLET LQNLSVEFAT LGDLKVVERP
TTHNLGPRDF LNVQATVKVS STDTGVIFGN IVYDGASSTE SHVVILNDIH ADIMDYIQPA
HCTETQFRTM WTEFEWENKV NINSKAKSLR EFLKQLMEST NMACLTPEAS LKGDCRFLSA
NLYARSVFGE DALANLSIEK EGEDGPITGF VRIRSRSQGL ALSLGSLKGL KATAA
//