ID G7E172_MIXOS Unreviewed; 955 AA.
AC G7E172;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN Name=Mo03252 {ECO:0000313|EMBL:GAA96582.1};
GN ORFNames=E5Q_03252 {ECO:0000313|EMBL:GAA96582.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA96582.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
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:GAA96582.1}.
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DR EMBL; BABT02000102; GAA96582.1; -; Genomic_DNA.
DR RefSeq; XP_014567376.1; XM_014711890.1.
DR AlphaFoldDB; G7E172; -.
DR STRING; 764103.G7E172; -.
DR GeneID; 26267283; -.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; G7E172; -.
DR OMA; MDYIIPA; -.
DR OrthoDB; 151169at2759; -.
DR Proteomes; UP000009131; 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:UP000009131};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 20..503
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 676..812
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 817..944
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 105974 MW; B3C8FFE7345148AE CRC64;
MTSESSAFTL ISDDSSESPT SQDLRTALVG ATDETKFEIL RRIIVSSLNG NPHPTLLMPI
IQYVLPSKSK EIKKLLHFYW EICPKHDENG KLKQEMILVC NAIRNDLQHP NEYIRGATLR
FLQKIREPEL LEPLIPTCRS CLEHRHSFVR KNAVFAVYQI YKSFEHLIPD APELIQTFLA
AETDSTCRRN AFVMLIHCSV PRAIEYFNQI YDSIANLDEL LQLAVIELIR KDIKDSKSET
PQKPRYIRAV FELLASTSHS VKYEAASQLT TLTQNPAAVK AAAACFIELI LKESDNNVKL
IVLERVEVLR SKHEYVLNDL VMDILRVISS PDMEVKRKAL ALALDMVSSR NVSEVTSFLK
KELLKTLDQQ LEKNLEYRQL LIQSIHTCAI RYSEVASNVV HTLMEFLGDS NTTSAVDVIA
FVREVVEKFP DLRVSIVEKL LQTFGEIKSG KVFRGALWIS GEYCTSLEGI NETMLQIRKV
LGEVPMLAAE QRLLDEAEAA AQSQADPSVD SKPTTTTTTR VLADGTYATE TVYSDPSAQI
RLAAVKSASK PPLRSLILGG DFYTASVLAS TLTKLVLHFV ELSSDHSAIN ALKAEAMLIM
TSLIRVGQSQ FAAVPIDEDS VDRISTCLRS VASVQPAVKQ VFLHDTQAAY AQMVAHEETK
AAEKRAKDSK ATAVQADDLI TFRQLSKKAG GDADEYDLDL TRATGAAEAV KDDFISKLNR
VVQLTGFSDP VYAEAYVNVH QFDIHLDVLV VNQTVETLQN LSVEFATLGD LKISERPVQY
TLGPHSFQSI KATIKVSSTE TGVIFGNIFY DGPSTSDSHC VVLNDIHIDI LDYINPAHCN
EAQFRSMWTE FEWENKVNVN TSIADLRQYL AHIMSATNMA CLTNDAALKG DCGFLSANLY
AKSLFGEDAL ANLSIEKLAD GTLSGHVRIR SKTQGIALSL GDKISLLARN PQTAT
//