GenomeNet

Database: UniProt
Entry: A0A178AE45_9PLEO
LinkDB: A0A178AE45_9PLEO
Original site: A0A178AE45_9PLEO 
ID   A0A178AE45_9PLEO        Unreviewed;      1221 AA.
AC   A0A178AE45;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN   ORFNames=IQ06DRAFT_340315 {ECO:0000313|EMBL:OAK94737.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK94737.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK94737.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK94737.1,
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.
CC       {ECO:0000256|PIRNR:PIRNR003354}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000256|PIRNR:PIRNR003354}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003354}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR003354}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. 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; KV441724; OAK94737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AE45; -.
DR   STRING; 765868.A0A178AE45; -.
DR   InParanoid; A0A178AE45; -.
DR   OrthoDB; 20819at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:UniProtKB-UniRule.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   CDD; cd22948; Coatomer_WDAD_alpha; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.25.40.470; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR047312; Coatomer_alpha_WD-assoc_reg.
DR   InterPro; IPR016391; Coatomer_asu.
DR   InterPro; IPR010714; Coatomer_asu_C.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19876; COATOMER; 1.
DR   PANTHER; PTHR19876:SF1; COATOMER SUBUNIT ALPHA; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR003354};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003354};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR003354};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          53..94
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          95..136
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          137..178
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          211..252
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          255..296
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          350..778
FT                   /note="Coatomer WD associated region"
FT                   /evidence="ECO:0000259|Pfam:PF04053"
FT   DOMAIN          833..1219
FT                   /note="Coatomer alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06957"
SQ   SEQUENCE   1221 AA;  135912 MW;  5D223ABC64C99AF4 CRC64;
     MSSSPSMLTK FESKSSRAKG IAFHPKRPWI LVSLHSSTIQ LWDYRMGTLI DRFEEHDGPV
     RGIDFHKTQP LFVSGGDDYK IKVWSYQTRR CLFTLNGHLD YVRTVFFHHE LPWIVSSSDD
     QTIRIWNWQN RSLICTMTGH NHYTMCAQFH PKEDLIVSAS LDQSVRVWDI SGLRKKHSAP
     TSMSFEDQLA RSNQNQADMF GNTDAVVKFV LEGHDRGVNW VAFHPTLPLI VSAGDDRLVK
     LWRMSETKAW EVDTCRGHFQ NASACLFHPH QDLILSVGED KTIRVWDLNR RTSVQSFKRE
     NDRFWVIAAH PEINLFAAGH DNGVMVFKLE RERPASSVYQ NNLFYITKEK HVRSYDFQKN
     IESPSMLSLK KLGSAWVPPR TLSYNPAERS ILVTSPADSG TYELISLPRD ASGAVEPTDT
     KRGSGNSAVF VARNRFAVFT QANQQIDIKD LSNSTTKTIK PPHGTTDIYF GGTGNLLLIT
     PTNVVLYDIQ AKKNLAELAV NGVKYVVWSS DGLHVALLSK HNVTIATKNL EQVSTLHETI
     RIKSATWDDT GVLLYSTLNH IKYSLMNGDN GIVRTLEHTV YLVRVKGRNV YCLDRAAKPK
     ILQIDPTEYR FKLALVKRNY DEMLNIIKTS SLVGQSIISY LQKKGYPEIA LQFVQDPQTR
     FELAIECGNL EVAVEMAKQL DRPKLWQRLS TEALAHGNHQ IVEMTYQKLR NFDKLSFLYL
     ATGDQDKLKR MAKIAEHRGD MTARFQNALY LGDVQNRIEM FQEIDLYPLA YATAKANGLD
     EQAQSILEAA GVTEDQINLP SIGGALAPAK PIVPTHKTNW PTRAASSTVF EKALMGEVEG
     VSSDEPAANG YGDEDLLGDA EAPNAAAELG GGDDEDDVGG WDMGDDGDVE AEDEFVEVEG
     AEAGAGSSEA DLWARNSPLA ADHVAAGSFE TAMQLLNRQI GAVNFAPLEE RFQEIYQATR
     TFLPATPNMP SLVNYVRRTV DETDSRKILP IVPRDLESIL STDLTAGKQG LLKNKLEDGI
     VAFKKLLHLL IVNVVASQAE LTEARRAINV AAQYIVAMSI ELERRALLQG ATDVAALSDD
     DKKRALELSA YFTIPELEGP HRSIPLSAAM NFAHKNKQLN TALNFANALL DRTGNAKMKE
     SAKRIKTVAE RNPADVIEID FDQFADFEIC AASHTPIYGG SPSSACPYDG AKYHAKYKGT
     VCKVCEVCQI GAPASGLRLV G
//
DBGET integrated database retrieval system