COPD_ARATH
ID COPD_ARATH Reviewed; 527 AA.
AC Q93Y22; Q56WY5; Q93Y42; Q9FF73;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Coatomer subunit delta;
DE AltName: Full=Delta-coat protein;
DE Short=Delta-COP;
GN OrderedLocusNames=At5g05010; ORFNames=MUG13.13;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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] OF 268-527.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC Delta-COP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005245; BAB11523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90817.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90818.1; -; Genomic_DNA.
DR EMBL; AY054464; AAK96656.1; -; mRNA.
DR EMBL; AY054658; AAK96849.1; -; mRNA.
DR EMBL; AY114626; AAM47945.1; -; mRNA.
DR EMBL; AK221894; BAD94247.1; -; mRNA.
DR RefSeq; NP_001031836.1; NM_001036759.2.
DR RefSeq; NP_568147.1; NM_120583.6.
DR AlphaFoldDB; Q93Y22; -.
DR SMR; Q93Y22; -.
DR BioGRID; 15662; 6.
DR STRING; 3702.AT5G05010.1; -.
DR iPTMnet; Q93Y22; -.
DR SwissPalm; Q93Y22; -.
DR PaxDb; Q93Y22; -.
DR PRIDE; Q93Y22; -.
DR ProteomicsDB; 240950; -.
DR EnsemblPlants; AT5G05010.1; AT5G05010.1; AT5G05010.
DR EnsemblPlants; AT5G05010.2; AT5G05010.2; AT5G05010.
DR GeneID; 830383; -.
DR Gramene; AT5G05010.1; AT5G05010.1; AT5G05010.
DR Gramene; AT5G05010.2; AT5G05010.2; AT5G05010.
DR KEGG; ath:AT5G05010; -.
DR Araport; AT5G05010; -.
DR TAIR; locus:2175269; AT5G05010.
DR eggNOG; KOG2635; Eukaryota.
DR HOGENOM; CLU_019988_1_0_1; -.
DR InParanoid; Q93Y22; -.
DR OMA; YDARKHV; -.
DR OrthoDB; 1027200at2759; -.
DR PhylomeDB; Q93Y22; -.
DR PRO; PR:Q93Y22; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Y22; baseline and differential.
DR Genevisible; Q93Y22; 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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0051645; P:Golgi localization; 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; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR027059; Coatomer_dsu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR PANTHER; PTHR10121; PTHR10121; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..527
FT /note="Coatomer subunit delta"
FT /id="PRO_0000285620"
FT DOMAIN 282..527
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 518
FT /note="Q -> H (in Ref. 3; AAK96849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 57719 MW; C32F946714C31702 CRC64;
MVVLAAAIVV KSGKVIVSRH YVDMSRIRIE GLLAAFPKLV GMGKQHTYIE TENVRYVYQP
IEALFLLLVT TKQSNILEDL ATLTLLSKLV PEYSMSLDEE GISRASFELI FAFDEVISLG
HKESVTVAQV KQYCEMESHE EKLHKLVMQS KINDTKDVMK RKANEIDKSK IEKNKPGGFS
SMGSMGSGRL ESGFNELSIS SGGGGGYGSG SGFGMISDVD PINTKPKDRS RSSVTAPPKS
SGMKLGKSGK NQLMESLKAE GEDVIEDVKP TGQSKAAAPP PTDPFTLTVE EKLNVALRRD
GGLSSFDMQG TLSLQILNQE DGFVQVQIAT GENPEILFKT HPNINRDMFN NENILGLKRP
DQPFPTGQGG DGVGLLRWRM QRADESMVPL TINCWPSVSG NETYVSLEYE ASSMFDLTNV
IISVPLPALR EAPSVRQCDG EWRYDPRNSV LEWSILLIDN SNRSGSMEFV VPPVDSSVFF
PISVQFAATS TYSGLKVTGM IPLRGGGGAT PRFVQRTQLI AQNYQVI
