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Database: UniProt
Entry: M9ME72_PSEA3
LinkDB: M9ME72_PSEA3
Original site: M9ME72_PSEA3 
ID   M9ME72_PSEA3            Unreviewed;       984 AA.
AC   M9ME72;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=PANT_14c00014 {ECO:0000313|EMBL:GAC75048.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC75048.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(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}.
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DR   EMBL; DF196780; GAC75048.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9ME72; -.
DR   STRING; 1151754.M9ME72; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000011976; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000011976};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          24..512
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          698..834
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          846..974
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
FT   COILED          709..736
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   984 AA;  108523 MW;  572700413916DE2D CRC64;
     MASSEAIAYT VVAPDPSSDG IELSTQDLRN NLQRGSDEIK LETLRRIIVS TLNGSPQPNL
     LMPIIQYVLP SRNKQLKKML HFYWEVCPKL DEKGNLKQEM ILVCNAIRND LQHPNEYIRG
     STLRFLQKVK EPELLEPLIP TIRQCLEHRH SYVRKNAVFC VYSIYQQNEN LIVDAPELME
     TFLAAEADTT CKRNAFVLLC HTAPERTVQY LLGLGDQIAS QDELMQLAII ELIRKDCRGD
     SPNRPRYIRA VSELLAAPSH SVKYEAATTL TTLTQNAAAV KATASALIEL AVKESDNNVK
     LIVLDRLDAL RSKHEHVIDP LVMDLLRVLS SPDMDVRRKA LRIALEMVSS RNIEEVVLLL
     KKELMKTVDT SQSSQDKNLE YRQLLIQSIH TCAIKFSEVA SNVVHVLMEF LGDSNNPSAV
     DVIAFVREVV EKFPDLRSSI VDKLLRTFTD IKSGKVFRGA LWIVGEYCAS IEDVKEAMQQ
     IRKVIGEVPI LAAEERLLEA SSTGVEAEAA AEQTDAGASS SALGAAAKSS AANRVRADGT
     YATETAFSSE ANQAARLEAV KSASKPPLRS LLLLGDFYTG TVLASTLTKL VLRFAQLSSD
     ATAKNSLRAE AMLIMTSIVR VGQSKFAATP IDEDSVERIM ACVETLASSM QEAEPESEEA
     NEVFLHDTKA AYTKMVEHEQ AKQAEKLAKE TKVVKVQPDD LLSFRQFSKK AADDAAEEYE
     RELTQATGAA EAAKDDFISK LARVVQLTGF SDPVYAEAYV NVHQFDILLD VLVVNQTAET
     LQNLSIEFAT LGDLKLVERP SNYTLAPYSY QSIKATIKVS STETGVIFGN IIYEGAAGTG
     TQSAGDAKCV VLNDIHIDIM DYIAPAYCNE AQFRAMWTEF EWENKVNVNT AITDLREYLA
     HIMKSTNMSC LTPDASLAGE CGFLSANMYA RSLFGEDALA NLSIELLPDG KTIQGHVRIR
     SKTQGIALSL GDKITLAQKA ASKD
//
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