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Database: UniProt
Entry: A1CQ17_ASPCL
LinkDB: A1CQ17_ASPCL
Original site: A1CQ17_ASPCL 
ID   A1CQ17_ASPCL            Unreviewed;       955 AA.
AC   A1CQ17;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=ACLA_024540 {ECO:0000313|EMBL:EAW07738.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07738.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07738.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07738.1; -; Genomic_DNA.
DR   RefSeq; XP_001269164.1; XM_001269163.1.
DR   AlphaFoldDB; A1CQ17; -.
DR   STRING; 344612.A1CQ17; -.
DR   EnsemblFungi; EAW07738; EAW07738; ACLA_024540.
DR   GeneID; 4700954; -.
DR   KEGG; act:ACLA_024540; -.
DR   VEuPathDB; FungiDB:ACLA_024540; -.
DR   eggNOG; KOG1058; Eukaryota.
DR   HOGENOM; CLU_006949_0_0_1; -.
DR   OMA; MDYIIPA; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000006701; 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:UP000006701};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          21..490
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;  106490 MW;  53DBA15F3DB486FE CRC64;
     MASFLENAYS LVHLDNTADQ PNVQELKMQL EKGTDETKME TMRRIITIML NGDPMSQLLM
     HIIRFVMPSK SKSLKKLLYF YYEICPKHDS NGKLKQEMIL VCNGIRNDLQ HPNEYIRGNT
     LRFLCKLREP ELIEPLLSSA RSCLEHRHAY VRKNAVWAVA SIFQHSESLI PDAPELIQTF
     LESETDSTCK RNAFAALMSI SHQKALEYLA STFDSIPNTD ELLQLAELEF IRKDAVQNTQ
     NKGKYLRLIF DLLEAPTSTV VYEAATSLTA LTSNPVAVKA AASKLIELCI KEADNNVKLI
     VLDRVDQLRS RNEGVLDDLT MEILRVLSSP DIDVRRKALG ITLEMVSSKN VEEVVMLLKK
     ELGKTVDEQY EKNSEYRQLL IQSIHHCAIK FSEIAASVVD LLMDFIADFN NNSAVDVISF
     VKEVVEKFPK LRAAIVGRLV STLSEVRAGK VYRGVLWVVG EYSLEERDIR EAWKRIRASL
     GEIPILASEQ RLLDEVPDET IVNEQVNGHA KASAPTGSRK VLADGTYATE SALTSESAAA
     AKLAAVKAAQ KPPLRQLILD GDYYLATVLS STLTKLVMRH SEVSEDVART NALRAEAMLI
     MISIIRVGQS QFVKAPIDED SIDRIMCCVR SLSEFSQRKE LETTFLEDTR KAFRDMVQVE
     DKKRAAKEAV EKAKTAVQID DAIPIRQFTK KSGVEGAEEI ELDLVKATGG DSTVETTPSK
     LSRVVQLTGF SDPVYAEAYV TVHQFDIVLD VLLVNQTLET LQNLSVEFAT LGDLKVVERP
     TTHNLGARDF LNVQATVKVS STDTGVIFGN IVYDGASSTE THVVILNDIH ADIMDYIQPA
     HCTETQFRTM WTEFEWENKV NINSKAKSLR EFLKQLMEST NMACLTPEAS LKGDCRFLSA
     NLYARSVFGE DALANLSIEK EGDDGPITGF VRIRSRSQGL ALSLGSLKGL KASAA
//
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