COPE2_ARATH
ID COPE2_ARATH Reviewed; 293 AA.
AC O64748;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Coatomer subunit epsilon-2;
DE AltName: Full=Epsilon-coat protein 2;
DE Short=Epsilon-COP 2;
GN OrderedLocusNames=At2g34840; ORFNames=F19I3.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O64748-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
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DR EMBL; AC004238; AAC12824.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09028.1; -; Genomic_DNA.
DR EMBL; AY075627; AAL91638.1; -; mRNA.
DR EMBL; AY142051; AAM98315.1; -; mRNA.
DR PIR; T00466; T00466.
DR RefSeq; NP_181030.1; NM_129037.6. [O64748-1]
DR AlphaFoldDB; O64748; -.
DR SMR; O64748; -.
DR BioGRID; 3395; 18.
DR STRING; 3702.AT2G34840.1; -.
DR PaxDb; O64748; -.
DR PRIDE; O64748; -.
DR ProteomicsDB; 241168; -. [O64748-1]
DR DNASU; 818049; -.
DR EnsemblPlants; AT2G34840.1; AT2G34840.1; AT2G34840. [O64748-1]
DR GeneID; 818049; -.
DR Gramene; AT2G34840.1; AT2G34840.1; AT2G34840. [O64748-1]
DR KEGG; ath:AT2G34840; -.
DR Araport; AT2G34840; -.
DR TAIR; locus:2044792; AT2G34840.
DR eggNOG; KOG3081; Eukaryota.
DR HOGENOM; CLU_049363_0_0_1; -.
DR InParanoid; O64748; -.
DR OMA; SWVGMRE; -.
DR OrthoDB; 1161199at2759; -.
DR PhylomeDB; O64748; -.
DR PRO; PR:O64748; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64748; baseline and differential.
DR Genevisible; O64748; 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: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 Alternative splicing; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..293
FT /note="Coatomer subunit epsilon-2"
FT /id="PRO_0000193854"
SQ SEQUENCE 293 AA; 32658 MW; DF770789DC2EE5FD CRC64;
MSAMGAGPDH LFNLRNNFYL GAYQTAINNS EIANLSPENA VERDCLVFRS YIALGSYQLV
ISEIDESAAT PLQAVKLLAM YLSTPQNKES TISSLKEWLA DSTIGNNDTL RLIAGIIFMH
EEDYNETLKH THAGGTMDLY ALNVQIFIKM HRAEYAEKQL RVMQQIDEDH TLTQLASAWL
NLAVGGSKIQ EAYLIFEDFS EKYPMTCLIL NGKAVCCMQM GNFDEAETLL LEALNKDAKD
PETLANLVVC SLHVGKSSSR HLSQLKLSHP EHILVKRVSS AEDNFERAVQ LVA