GenomeNet

Database: UniProt
Entry: A0A178A9D1_9PLEO
LinkDB: A0A178A9D1_9PLEO
Original site: A0A178A9D1_9PLEO 
ID   A0A178A9D1_9PLEO        Unreviewed;       956 AA.
AC   A0A178A9D1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=IQ06DRAFT_260389 {ECO:0000313|EMBL:OAK94326.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK94326.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK94326.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK94326.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV441725; OAK94326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178A9D1; -.
DR   STRING; 765868.A0A178A9D1; -.
DR   InParanoid; A0A178A9D1; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000077206; 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:UP000077206};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          22..492
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          680..814
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          820..946
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
FT   REGION          497..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   956 AA;  106466 MW;  C7FA9F0C8FA9C3D7 CRC64;
     MATFLENSYS LVHQDNAADV PSQNELKQAL EKGNDEQKIE TMKKILSIML NGDPQTGLLM
     HIIRFVMPSK SKPLKKLMYF FFEVCPKHDA QGKLRQEWIL VCNAIRFDLQ APNEYVRGNT
     LRFVTKLRDA ELVEPLLQPV RQCLTHRHAY VRKNATFAVA SIFTHLPELM PDAPDMLVTF
     LDDENDPTCK RNAFAALVSV SHEKALEYLS TVFDAIPNHE ELLLLAELEF IRKDAVVNPQ
     NKARYMRLIF DLLESQVSTV IYESAHALTT LTSNPVAVKA AAGKFVELAI KEPDNNVKLI
     VLERVDQLRS KHEGVLDDLT MEVLRVLSST DLDVRKKSLN IAMEMISSRN VEEVVLLLKK
     ELMKTVDEQY EKNSEYRSLL ISSIHSAAIK FPEVAASVVG SLMDFISDVS SNASAVDVIS
     FVKEVVERFP DLRPSIIERL VSTLGEVRAG KVYRGVLWII GEFSLEAKDI RDAWKGIRSS
     LGEIPILASE QRLLDDASEG KEDTEQVNGH AKSSAPTGSR KVLADGTYAT ESALTSSAAA
     KAKLEAVKNS QKPPLRQLVL DGDYYLATVL SSTLTKLVMR HSELSQDAAR TNALRAEAML
     IMISIIRVGQ SQFVKTLIDE DSIDRIMSCV RSLSEFSQRK ELETVFLEDT RKSFAAMVQT
     EEKKRAAKEA SERAKSAVNV DDSFNIRQLK KKDADGSDEI EQDLERATGG DTATEDLTSK
     LSRVVQLTGF SDSVYAEAYV KVHQFDIVLD VLLVNQTTET LQNLTVEFAT LGDLKVVERP
     PTQNVGPHDF INIQATVKVS STDTGVIFGN ILYEGEKGVD SNVVILNDVH VDIMDYIKPA
     QCTETQFRTM WTEFEWENKV NINSKAKTLR DFLKQLMAST NMSCLTPEAS MKGDCQFLSA
     NLYARSVFGE DALANLSIEK EGDNGPITGF VRIRSRSQGL ALSLGSLKGL NKVGVA
//
DBGET integrated database retrieval system