COPA1_ARATH
ID COPA1_ARATH Reviewed; 1216 AA.
AC Q94A40; O80706;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Coatomer subunit alpha-1;
DE AltName: Full=Alpha-coat protein 1;
DE Short=Alpha-COP 1;
GN OrderedLocusNames=At1g62020; ORFNames=F8K4.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 722-1216.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK91416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN46802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC004392; AAC28519.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33914.1; -; Genomic_DNA.
DR EMBL; AY050400; AAK91416.1; ALT_INIT; mRNA.
DR EMBL; BT001048; AAN46802.1; ALT_INIT; mRNA.
DR PIR; T02146; T02146.
DR RefSeq; NP_176393.1; NM_104882.5.
DR AlphaFoldDB; Q94A40; -.
DR SMR; Q94A40; -.
DR BioGRID; 27720; 67.
DR IntAct; Q94A40; 1.
DR STRING; 3702.AT1G62020.1; -.
DR iPTMnet; Q94A40; -.
DR PaxDb; Q94A40; -.
DR PRIDE; Q94A40; -.
DR ProteomicsDB; 242287; -.
DR EnsemblPlants; AT1G62020.1; AT1G62020.1; AT1G62020.
DR GeneID; 842497; -.
DR Gramene; AT1G62020.1; AT1G62020.1; AT1G62020.
DR KEGG; ath:AT1G62020; -.
DR Araport; AT1G62020; -.
DR TAIR; locus:2036823; AT1G62020.
DR eggNOG; KOG0292; Eukaryota.
DR HOGENOM; CLU_007565_1_0_1; -.
DR InParanoid; Q94A40; -.
DR OMA; ICAEYIV; -.
DR OrthoDB; 139008at2759; -.
DR PhylomeDB; Q94A40; -.
DR PRO; PR:Q94A40; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94A40; baseline and differential.
DR Genevisible; Q94A40; AT.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF06957; COPI_C; 1.
DR Pfam; PF00400; WD40; 3.
DR PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF51004; SSF51004; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1216
FT /note="Coatomer subunit alpha-1"
FT /id="PRO_0000285599"
FT REPEAT 7..48
FT /note="WD 1"
FT REPEAT 49..88
FT /note="WD 2"
FT REPEAT 91..132
FT /note="WD 3"
FT REPEAT 133..172
FT /note="WD 4"
FT REPEAT 202..241
FT /note="WD 5"
FT REPEAT 246..285
FT /note="WD 6"
FT REPEAT 288..326
FT /note="WD 7"
FT REPEAT 363..404
FT /note="WD 8"
SQ SEQUENCE 1216 AA; 136566 MW; 79FC84DC14A481B5 CRC64;
MLTKFETKSN RVKGLSFHPK RPWILASLHS GVIQLWDYRM GTLIDRFDEH EGPVRGVHFH
NSQPLFVSGG DDYKIKVWNY KNHRCLFTLL GHLDYIRTVQ FHHEYPWIVS ASDDQTIRIW
NWQSRTCVSV LTGHNHYVMC ASFHPKEDLV VSASLDQTVR VWDIGALRKK TVSPADDIMR
LTQMNSDLFG GVDAIVKYVL EGHDRGVNWA AFHPTLPLIV SGADDRQVKL WRMNETKAWE
VDTLRGHMNN VSSVMFHAKQ DIIVSNSEDK SIRVWDATKR TGLQTFRREH DRFWILAVHP
EMNLLAAGHD SGMIVFKLER ERPAFALSGD SLFYAKDRFL RYYEYSTQRD SQVIPIRRPG
TPSLNQSPRT LSYSPTENAV LICSDLDGGS YELYIIPKDS VGRSDVVQDA KRGTGGSAVF
IARNRFAVLE KSTSQVLVKN LKNEVVKKSP LPIPTDAIFY AGTGNLLCRS EDKVVIFDLQ
QRLVLGELQT PFVRYVVWSS DMESVALLSK HTIIIASKKL VLQCTLHETI RVKSGAWDDN
GVFIYTTLNH IKYCLPNGDS GIIRTLDVPI YITKVSGNTI FCLDRDGKNK AITINATEYI
FKLSLLRKRY DHVMSMIKNS QLCGQAMIAY LQQKGFPEVA LHFVEDERIR FNLALESGNI
SVAVASATQI NEKDHWYRLG VEALRQGNSG IVEFAYQQTK NFERLSFLYL ITGNLDKLSK
LMKIAEVKNN VMGQFHNALY LGDVKERVKI LENAGHLPLA YITASVHGLN DIAERLATEL
GDNVPSLPEG KTPSLLMPPT PIMCGGDWPL LRVMKGIFEG GLESADRGGT VDEEDVEGDW
GEELDINVDG MENRDIEDIL AAAEAGEEEN DEEGGWGLED LVLPPELDTP KASANARSSV
FVTPPQGMPV SQSWSQKSSL AAEQAAAGSF DTAMRLLHRQ LGIKNFTPLK SMFLDLFNGS
HSYLRAFSSC PVVPLAIERG WSESSSPNVR SPPALVYDFS QLDEKLKSGY KATTTGKFTE
ALRLFLSILH TIPLVVVETR REVDEVKELI VIVKEYVLGL QMELKRREMK DDPVRQQELA
AYFTHCNLQT PHLRLALLSA MGVCYKAKNL ATASNFARRL LETSPVDSQA KMARQVVQAA
ERNMTDETKL NYDFRNPFVV CGSTYVPIYR GQKDVSCPYC TARFVPNQEG NICTVCDLAV
IGADASGLLC SPSQVR
