ID A0A2G5EJK1_AQUCA Unreviewed; 1216 AA.
AC A0A2G5EJK1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN ORFNames=AQUCO_00700334v1 {ECO:0000313|EMBL:PIA55942.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA55942.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA55942.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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|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; KZ305024; PIA55942.1; -; Genomic_DNA.
DR EMBL; KZ305024; PIA55943.1; -; Genomic_DNA.
DR STRING; 218851.A0A2G5EJK1; -.
DR OrthoDB; 20819at2759; -.
DR Proteomes; UP000230069; 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; 6.
DR PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
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:UP000230069};
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 5..46
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-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..1216
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
FT REGION 859..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1123..1150
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 862..883
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 136670 MW; 817463FDAE311AE5 CRC64;
MLTKFETKSN RVKGLSFHPK RPWILASLHS GVIQLWDYRM GTLIDRFDEH DGPVRGVHFH
KSQPLFVSGG DDYKIKVWNY KMHRCLFTLL GHLDYIRTVQ FHHEYPWIVS ASDDQTIRIW
NWQSRTCVSV LTGHNHYVMC ATFHPKEDLV VSASLDQTVR VWDIGALRKK TVSPADDLLR
LSQMNTDLFG GVDAVVKYVL EGHDRGVNWA SFHPTLPLIV SGADDRQLKL WRMNDTKAWE
VDTLRGHMNN VSCVMFHAKQ DIIVSNSEDK SIRVWDVTKR TCVQTFRREH DRFWILASHP
EMNLLAAGHD SGMIVFKLER ERPAFSVSGD VLYYVKDRFL RFYEFSTQKD SQVIPIRRPG
TTSLNQSPRT LSYSPSENAV LVCSDVDGGS YELYTIPKDS ISRGDTVQDA KRGVGGSAVF
VARNRFAVLD KSNNQVLVKN LKNEIVKKSI LPIVAEAIFY AGTGNLLCRA EDRVVIFDLQ
QRLVLGDLQT PFIKYVVWSN DMESIALLSK HSIVIASKKL VHRCTLHETI RVKSGAWDDN
GVFIYTTLNH VKYCLPNGDS GIIKTLDVPI YITKISGNTI FCLDRDGKNR AVIIDATEYV
FKLSLLKKKY DQVMSIIRNS QLCGQAMIAY LQQKGFPEVA LHFVKDERTR FNLALESGNI
QIAVASANAI DEKDHWYRLG VEALRQGNAG IVEYAYQRTK NFDRLSFLYL VTGNTSKLSK
MLKIAELKND VMGQFHNALY LGDIHERVKI LENVGHLPLA YMTATVHGLN DVAERLAAKL
GDNVPSLPQG KVSSLLMPPT PILCGGDWPL LRVMKGIFEG GLENIGRGVQ EEDEEAADAD
WGEELDIVDG EVVQNGDVGA VEDGEANDEN DEEGGWDLED LELPPEVDTP KVSNARSSVF
VTPTPGMPVS QIWIQKSSLA GEHAAAGNFD TAMRLLSRQL GIQNFAPLKP MFLDLYTGSH
SYLRAFSSSP IILLAVERGW SETSSPNVRG PPALVFSFSQ LDEKLKAGHK ATSGGKFTEA
LRIFKGILHT IPLIVVESRR EVDEVRELIF KAKEYVVGLQ MEIRRKELRD DPVRQQELAA
YFTHCNLHMT HLRLALMNAM SICYKAKNLS TAANFARRVL ETNPSIENQA KTARQVLQSA
ERNMRDETQL NYDFRNPFVV CGATYVPIYQ GQKDVACPYC GSRFVPSQQG QLCTVCDLSV
VGSDASGLLC SPSQIR
//
