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Database: UniProt
Entry: A0A1Y2VVI1_9PEZI
LinkDB: A0A1Y2VVI1_9PEZI
Original site: A0A1Y2VVI1_9PEZI 
ID   A0A1Y2VVI1_9PEZI        Unreviewed;       959 AA.
AC   A0A1Y2VVI1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=M426DRAFT_323290 {ECO:0000313|EMBL:OTB01663.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB01663.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB01663.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB01663.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111579; OTB01663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VVI1; -.
DR   STRING; 1001833.A0A1Y2VVI1; -.
DR   InParanoid; A0A1Y2VVI1; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000242955; 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:UP000242955};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          24..490
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          680..816
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          821..947
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
FT   REGION          498..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  106701 MW;  5A58C4C5C0AEFA81 CRC64;
     MSTFLENAYS LVHQDNTADV PSMSDLRMQL EKGTDETKVD TMKRILTVML NGDPMPQLLM
     HIIRFVMPSR YKPLKKLLYF YYEICPKLDS TGKLKQEMIL VCNGIRNDLQ HPNEYIRGNT
     LRFLCKLREP ELIEPLLSSA RACLEHRHAY VRKNAVFAVA SIFQHSPSLI PDASELIATF
     LEGESDATCK RNAFAALASI DHDKALVFLS SVFEGIPNAE ELLQLVELEF IRKDAIQNSQ
     HKARYLRLIF DLLEAPTSTV VYEAASSLTA LTNNPVAVKA AAAKFIELSI KEADNNVKLI
     VLDRVDQLRQ KNEGVLDDLV MEILRALSSP DIDVRRKALT IALEMVSSKN VEEVILLLKK
     ELSKTVDQEY EKNAEYRQLL IHSIHQCAIK FSEVAASVVD LLMDFIADFS NTSAVDVISF
     VKEVVEKFPK LRPSIVARLV DTLSEVRAGK VYRGIIWIIG EYSLEESDIR DAWKRIRASL
     GEIPILASEQ RLLDNVDGDE EKEKEQVNGH SKPAAPSGSR RVLADGTYAT ETALTSSSAA
     AAKLEAVKAA QKPPLRQLIL EGDYYLAAVL SATLTKLVMR HSEISSDTAR TNALKAEAML
     IMISIIRVGQ SQFVKAPIDE DSVDRIMSCV RSLAEFSQRK ELESVFLDDT RKAFRAMVQV
     EEKKRAAKAA FEKAKTAIQV DDVVQIRQLS KKNVGDGTDE IELDLEKATG GESVSEDLSS
     KLSRVVQLTG FSDPVYAEAY VKVHQFDIVL DVLLVNQTTE TLQNLSVEFA TLGDLKVVER
     PTTQNLGPHD FHNVQCTIKV SSTDTGVIFG NVVYDGAHST DTNVVILNDL HVDIMDYIQP
     ATCTETQFRT MWTEFEWENK VNINSKAKSL RDFLEQLMAC TNMNCLTPEA SMKGDCQFLS
     ANLYARSVFG EDALANLSIE QDGEDGPITG FVRIRSRSQG LALSLGSLKG LNKIGTAAA
//
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