ID   COPE2_ORYSI             Reviewed;         297 AA.
AC   A2XY73; Q25A84; Q7XTM6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Coatomer subunit epsilon-2;
DE   AltName: Full=Epsilon-coat protein 2;
DE            Short=Epsilon-COP 2;
GN   ORFNames=H0413E07.10, OsI_017016;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Guang-Lu-Ai No.4;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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}.
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DR   EMBL; AL732331; CAJ86157.1; -; Genomic_DNA.
DR   EMBL; CM000129; EAY95783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XY73; -.
DR   SMR; A2XY73; -.
DR   STRING; 39946.A2XY73; -.
DR   HOGENOM; CLU_049363_0_0_1; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..297
FT                   /note="Coatomer subunit epsilon-2"
FT                   /id="PRO_0000291460"
FT   CONFLICT        82
FT                   /note="A -> T (in Ref. 2; EAY95783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  32095 MW;  1765597B2AB55798 CRC64;
     MAGAASPDHL FGLRYSFYVG AYQAVITGVQ AIPARAALSP DALAERDSLL YRSYIAIGSH
     QLVIDEIGPG AATPLQAVRL LAVYLSGGAG GKESAIRKLN ELLADDAVGS NPILRLVAGT
     VLMHERDYAG ALKHTNSGGT MELLAMNVQI CLQMHRSDHA EKQLRIMQQL DEDHTLTQLA
     NAWVDLVMGG SKIQEAHLIF QDLSEKYPAT CLILNGKALC LMHMGNFEDA EGLLLESLNK
     DAKDAETLAN LVVCSLNLGK SASRYLNQLK LAHPDHMLVK RMSSAEDSFD RACQAIS