ID A0A2C5WVT2_9PEZI Unreviewed; 959 AA.
AC A0A2C5WVT2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN Name=sec26 {ECO:0000313|EMBL:PHH49744.1};
GN ORFNames=CFIMG_006293RA {ECO:0000313|EMBL:PHH49744.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH49744.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH49744.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49744.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH49744.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49744.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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}.
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:PHH49744.1}.
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DR EMBL; APWK03000171; PHH49744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5WVT2; -.
DR STRING; 1035309.A0A2C5WVT2; -.
DR OrthoDB; 151169at2759; -.
DR Proteomes; UP000222788; 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:UP000222788};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 24..492
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 494..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 106661 MW; BD06F017B935DE5E CRC64;
MATFLENAYS LVHQDNAADV PTLSDLRTQL EKGTDESKVE TMKHILTIML NGDPMPSLLM
HIIRFVMPSK YKPLKKLLYF YYEICPKLDA SGKLKQEMIL VCNGIRNDLQ HPNEYIRGNT
LRFLCKLREA ELIEPLLSSA RSCLEHRHAY VRKNAVFAIA SIYQHSQFLI PDAPELIANF
LEAETDSTCK RNAFAALSSI SHDAALQYLS AVFEGVVNAE ELLQLVELEF IRKDAVQNTQ
NKAKYLRLIF DLLEAGASTV IYEAASSLTA LTNNPVAVKA AASKFIELSI KEPDNNVKLI
VLDKVDQLRR KNEGILDDLT MEILRALSSP DIDVRRKALT IAMEMVSSKN VEEVVLLLKK
ELAKTVDQEF EKNSEYRQLL IHSIHQCAIK FSEVAASVVD LLMDFIADFN NASAVDVINF
AKEVVEKFPE LRPSIVQRLT STLGEVRAGK VYRGILWIVG EYALEEKDIR DAWKRIRASL
GEIPIVASEQ RLLDAQDDDE EKKEADESSR EKPATSSGSR RVLADGTYAT ETALTSQSSA
AAKLEAVKAA SKPPLRQLIL DGDYYLATVL ASTLVKLVMR HSELSSDEAR TNALRAEAML
IMISIVRVGQ SHFAKQPIDE DSVDRIMTCI RSLAEFTKRK ELETVFLDDT RKAFRAMVVA
EESKRAAKEA VEKAKTAVQV DDVVNIRQLA KKNAGDGTDE MHRDLERATG GDAAAEDLSS
KLSRVVQLTG FSDPVYAEAY VKVHQFDIVL DVLLVNQTTE TLQNLSVEFA TLGDLKVVER
PTTQNLGPHD FHNVQCTIKV SSTDTGVIFG NVVYDGAHST DTNVVILNDV HVDIMDYIQP
ATCTETQFRT MWTEFEWENK VNINSKATSL REFLSQLMAC TNMNCLTPEA SLKGDCQFLS
ANLYARSVFG EDALANLSIE QKGENGPITG FVRIRSRSQG LALSLGSLKG LNKIGSVGN
//
