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Database: UniProt
Entry: G7E172_MIXOS
LinkDB: G7E172_MIXOS
Original site: G7E172_MIXOS 
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
//
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