ID A0A0S3SDV9_PHAAN Unreviewed; 1221 AA.
AC A0A0S3SDV9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN Name=Vigan.06G226800 {ECO:0000313|EMBL:BAT90969.1};
GN ORFNames=VIGAN_06226800 {ECO:0000313|EMBL:BAT90969.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT90969.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT90969.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015039; BAT90969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SDV9; -.
DR Proteomes; UP000291084; Chromosome 6.
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; SSF101908; Putative isomerase YbhE; 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 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:UP000291084};
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 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..771
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 818..1221
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
SQ SEQUENCE 1221 AA; 136939 MW; BF41872F6DA3991D CRC64;
MLTKFETKSN RVKGLSFHSK RPWILASLHS GVIQLWDYRM GTLIDRFDEH DGPVRGVHFH
NSQPLFVSGG DDYKIKVWNY KMHRCLFTLL GHLDYIRTVQ FHHENPWIVS ASDDQTIRIW
NWQSRTCISV LTGHNHYVMC ATFHPKEDIV VSASLDQTVR VWDIGSLKRK AGPPADDILR
LSQMNTDLFG GVDAVVKYVL EGHDRGVNWA AFHPTLPLIV SGADDRQVKL WRMNDTKAWE
VDTLRGHMNN VSCVMFHAKQ DIIVSNSEDK SIRVWDATKR TGIQTFRREH DRFWILATHP
EMNLLAAGHD SGMIVFKLER ERPAFAVSGD SLFYTKDRFL RFYEFSTQRE TQVLTIRRPG
SSTLNQCPKT LSYSPSENAI LLCSDVDGGS YELYCISKDS TKDSFGRGDM QDPKKGVGGS
AVFVARNRFA VLDKGSNQVS VKNLKNELVK KSALPTAADA IFYAGTGNLL CRSEDRVFIF
DLQQRIVLGD LQTPFIKYVV WSNDMENVAL LSKHAIVIAS KKLVHQCTLH ETIRVKSGAW
DDNGIFIYTT LNHIKYCLPN GDSGIIKTLD VPIYITKVMG NTIFCLGRDG KNKAITVDAT
EYIFKLSLLK KKYDQVMNMI RNSQLCGQAV IAYLQQKGFP EVALHFVKDE RIRFNLALES
GNIQIAVASA TAIDEKDHWY RLGVEALRQG NSGIVEYAYQ RTKNFERLSF LYLITGNVDK
LSKMLKIAEV KNDVMGQFHN ALYMGDIRER VKILENVGHL PLAYVTASVH GLHDVAERLA
AELGDNVPSV PKGKVQSLLI PPSPVSCGGD WPLLRVMRGI FDGGFNNTDR DADDEEYEAA
DGDWGEELDM VDVDALQNGD VSAILDEVEM AEEDDEEGGW DLEDLELPPE AETPKVSVSS
RSSVFVAPTA GMAVSQIWIQ RSSLAADHVA AGNFDTAMRL LNRQLGIRNF VPLKSMFLDL
HTGSHSYLRA FSSAPVVAIA VERGWTESSS PNVRGPPALP FKLSQLDEKL KAGYKSTTAG
KFSDALRTFI NILHTIPLIV VESRREVDDV KELIVIVKEY VLGLRMELKR REIKDSPARQ
QELAAYFTHC NLQVPHLRLA LLNAMTVCYK AKNLSTAANF ARRLLETNPT VENQAKTARQ
VLAAAERNMT DALQLNYDFR NPFVICGATY VPIYRGQKDV SCPYCTSRFV PTQEGQLCAV
CELSVVGADA SGLLCSPSQI R
//
