ID A7THZ2_VANPO Unreviewed; 973 AA.
AC A7THZ2;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN ORFNames=Kpol_1031p61 {ECO:0000313|EMBL:EDO18154.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO18154.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480393; EDO18154.1; -; Genomic_DNA.
DR RefSeq; XP_001646012.1; XM_001645962.1.
DR AlphaFoldDB; A7THZ2; -.
DR STRING; 436907.A7THZ2; -.
DR GeneID; 5546427; -.
DR KEGG; vpo:Kpol_1031p61; -.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; A7THZ2; -.
DR OMA; MDYIIPA; -.
DR OrthoDB; 151169at2759; -.
DR PhylomeDB; A7THZ2; -.
DR Proteomes; UP000000267; 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:UP000000267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 25..531
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 684..824
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 829..958
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
FT REGION 499..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 108629 MW; AF21BFCBCDF7B5B1 CRC64;
MTVSSKQPAY TLVFDPSPMA VSYTVADFQK ALEKGSDEDK IETMKEILVT MLEGNPLPEL
LMHIIRFVMP SKNKRLKKLL YFYWEIVPKL DSEGKLRHEM ILVCNAIQHD LQHPNEFIRG
NTLRFLTKLK EAELLEQMVP SVLACLDYRH AYVRKYAILA VLSIYKVSDH LIPDAKEIIH
SFLAAETDPV CKRNSFIGLS ELDRDAALTY LEDNMTSIES LDPLLQVSLV QFIRKDAINT
PSLKAQYIEL LSEILSSTSS NEVIFEACLA LTSLSSNPVV LNSAASKLID LAVKESDNNV
KLIVLDRIQD INNKNPGTLE DLTLDILRVL SAEDLDVRAK ALDISMNLVA SRNVDAVVKL
LKKEFQQTVN NGEKDKSMQY RQLLIKSIHS VAIRFVEAAG DVISLLLGFI GELGTAGASE
VISFVKEVVE KFPQLRATIL NNLISSMEEI KSAKAYRGAL WILGEYATSE QEIQNSWKHI
RASIGEVPIL QSELRRLNKK NEDDEAEKEE SESKPTGPVI LPDGTYATEN AFDSVKTNKD
DSSEEIESRP PLRRFILSGD FYTASILAST IIKLVIRFKN LSKDTKIINA FVAEGLLILV
SIIRVGQSNL VEKRIDEDSQ ERIMNAISIL MDENNSKTEE IESQLLKLAF LDATKSSFQA
QVARSKKELA KRSAKNIKKN AEAVDKAMNF RQFAGSISTS NTEDTIEEDL NLAIKGDDSM
AKANLVSSKL RKIVQLTGFS DPVYAEAYIT TNQFDVVFDV LLVNQTKETL KNLHVQFATL
GDLKIIDNPP STNIIAHGFH KISVTVKVSS ADTGVIFGNI IYDGGHGQDA RYVILNDVHV
DIMDYIKPAK TTDENFRTMW NAFEWENKIS VKAQLPTLHA YLRELVEGTN MGILTEENSL
GEEDCRFLSC NLYAKSSFGE DALANLCIEK EPSTGQVVGH VRIRSKGQGL ALSLGDRVAL
IAKQNNKVKL DRI
//
