ID B9RHB0_RICCO Unreviewed; 1217 AA.
AC B9RHB0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN ORFNames=RCOM_1449180 {ECO:0000313|EMBL:EEF49472.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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|ARBA:ARBA00025536}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|ARBA:ARBA00011775, 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}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. 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; EQ973778; EEF49472.1; -; Genomic_DNA.
DR RefSeq; XP_002512969.1; XM_002512923.2.
DR AlphaFoldDB; B9RHB0; -.
DR STRING; 3988.B9RHB0; -.
DR GeneID; 8284346; -.
DR KEGG; rcu:8284346; -.
DR eggNOG; KOG0292; Eukaryota.
DR InParanoid; B9RHB0; -.
DR OrthoDB; 20819at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; IPR011048; Haem_d1_sf.
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; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR003354};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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:UP000008311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:EEF49472.1};
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 47..88
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 89..130
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 131..164
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 200..241
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 244..285
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 340..768
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 815..1217
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
FT REGION 823..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1124..1151
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 828..851
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 136577 MW; BABD229433178843 CRC64;
MLTKFETKSN RVKGLSFHSK RPWILASLHS GVIQLWDYRM GTLIDRFDEH DGPVRGVHFH
KSQPLFVSGG DDYKIKVWNY KMHRCLFTLL GHLDYIRTVQ FHHEYPWIVS ASDDQTIRIW
NWQSRTCISV LTGHNHYVMC ASFHPKEDLV VSASLDQTVR VWDIGALRKK TVSPADDILR
LSQMNTDLFG GVDAVVKYVL EGHDRGVNWA AFHPNLPLIV SGADDRQVKL WRMNDTKAWE
VDTLRGHMNN VSCVMFHAKQ DIIVSNSEDK SIRVWDVTKR TGVQTFRREH DRFWILASHP
EMNLLAAGHD SGMIVFKLER ERPAFAVSGD SLFYAKDRFL RFYEFSTQRD TQVIPIRRPG
TTSLNQSPRT LSYSPTENAV LICSDVDGGT YELYVIPKDS ISRGDTVQEA KRGAGGSAIF
VARNRFAVLD KSSNQVLVKN LKNEVVKKSS LPIAADAIFY AGTGNLLCRA EDRVVIFDLQ
QRIVLGDLQT PFVKYVVWSN DMESVALLSK HAIIIASKKL VHQCTLHETI RVKSGAWDDN
GVFIYTTLNH IKYCLPNGDS GIIRTLDVPI YVTKVSGNTI FCLDRDGKSR HIDIDATEYM
FKLSLLRKKY DHVMSMIRNS QLCGQAMIAY LQQKGFPEVA LHFVKDERTR FNLALESGNI
QIAVASAKEI DEKDHWYRLG VEALRQGNSG IVEYAYQRTK NFERLSFLYL ITGNLEKLSK
MLKIAEVKND VMGQFHNALY LGDIQERVKI LENSGHLPLA YITAKVHGLE DVAERLAAEL
GDNVPSLPEG KVPSLLIPPA PIMSGSDWPL LRVMRGIFQG GLDDTGKGAV DEDEEAAEGD
WGGDLDIDDV DGLQNGDVSG ILEDGEVADE NGEGGWDLED LELPPEADTP RASVSARSSV
FVAPTPGMPV SQIWIQRSSL AAEHAAAGNF DTAMRLLNRQ LGIRNFAPLR SMFLDLHTGS
HTYLRAFSST PVISLAVERG WSESASPNVR GPPALVFNFS QLEEKLKAGY RATTAGKFTE
ALRLFLSILH TVPLIVVESR REVDEVKELI IIVKEYVLAS KMELKRREMK DNPIRQQELA
AYFTHCNLQM PHLRLALQNA MTVCFKAKNL ATAANFARRL LETNPTIENQ AKMARQVLQA
AERNMTDASE LNYDFRNPFV TCGATYVPIY RGQKDISCPF CSSRFVPSQE GQLCSVCDLA
VVGADASGLL CSPTQIR
//
