COPE1_ARATH
ID COPE1_ARATH Reviewed; 292 AA.
AC Q9SA78; Q8LB21;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Coatomer subunit epsilon-1;
DE AltName: Full=Epsilon-coat protein 1;
DE Short=Epsilon-COP 1;
GN OrderedLocusNames=At1g30630; ORFNames=T5I8.8;
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].
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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. The 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 -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007060; AAD25750.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31254.1; -; Genomic_DNA.
DR EMBL; AF348588; AAK15559.1; -; mRNA.
DR EMBL; AF370325; AAK44140.1; -; mRNA.
DR EMBL; AY063113; AAL34287.1; -; mRNA.
DR EMBL; AY087474; AAM65018.1; ALT_INIT; mRNA.
DR PIR; F86431; F86431.
DR RefSeq; NP_174351.1; NM_102800.4.
DR AlphaFoldDB; Q9SA78; -.
DR SMR; Q9SA78; -.
DR BioGRID; 25178; 18.
DR STRING; 3702.AT1G30630.1; -.
DR iPTMnet; Q9SA78; -.
DR PaxDb; Q9SA78; -.
DR PRIDE; Q9SA78; -.
DR ProteomicsDB; 241167; -.
DR DNASU; 839943; -.
DR EnsemblPlants; AT1G30630.1; AT1G30630.1; AT1G30630.
DR GeneID; 839943; -.
DR Gramene; AT1G30630.1; AT1G30630.1; AT1G30630.
DR KEGG; ath:AT1G30630; -.
DR Araport; AT1G30630; -.
DR TAIR; locus:2204644; AT1G30630.
DR eggNOG; KOG3081; Eukaryota.
DR HOGENOM; CLU_049363_0_0_1; -.
DR InParanoid; Q9SA78; -.
DR OMA; MIVLSQH; -.
DR OrthoDB; 1161199at2759; -.
DR PhylomeDB; Q9SA78; -.
DR PRO; PR:Q9SA78; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA78; baseline and differential.
DR Genevisible; Q9SA78; 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:0000325; C:plant-type vacuole; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006822; Coatomer_esu.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10805; PTHR10805; 1.
DR PIRSF; PIRSF016478; Coatomer_esu; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..292
FT /note="Coatomer subunit epsilon-1"
FT /id="PRO_0000285624"
SQ SEQUENCE 292 AA; 32602 MW; C4B2104F6BB8A22E CRC64;
MASMAGPDHL FNLRNHFYLG AYQAAINNSE IPNLSQEDIV ERDCLVHRAY IALGSYQLVI
SEIDEAAATP LQAVKLLAMY LSSPENKEST ISSLREWLAD PTVGNNAIIR LIAGTIFMHE
EDYNEALKHT HSGGTMDLHA LNVQIFIKMH RSDFAEKQLR VMQQIDEDHT LTQLASAWLN
LAVGGSKIQE AYLIFQDFSE KYPMTSLILN GKAVCCMHMG NFEEAETLLL EALNKDAKDP
ETLANLVVCS LHVGKSSSRY LNQLKLSHPE HVLVKRAASA EDNFERALQS FA
