COPD_MOUSE
ID COPD_MOUSE Reviewed; 511 AA.
AC Q5XJY5; Q91W48;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Coatomer subunit delta;
DE AltName: Full=Archain;
DE AltName: Full=Delta-coat protein;
DE Short=Delta-COP;
GN Name=Arcn1; Synonyms=Copd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Embryonic germ cell, Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241 AND LYS-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (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}.
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DR EMBL; AK028556; BAC26007.1; -; mRNA.
DR EMBL; CH466522; EDL25614.1; -; Genomic_DNA.
DR EMBL; BC017124; AAH17124.1; -; mRNA.
DR EMBL; BC023728; AAH23728.1; -; mRNA.
DR EMBL; BC033387; AAH33387.1; -; mRNA.
DR EMBL; BC034754; AAH34754.1; -; mRNA.
DR EMBL; BC083152; AAH83152.1; -; mRNA.
DR CCDS; CCDS40602.1; -.
DR RefSeq; NP_666097.3; NM_145985.4.
DR PDB; 5A1U; EM; 13.00 A; H=1-511.
DR PDB; 5A1V; EM; 21.00 A; H/P/Y=1-511.
DR PDB; 5A1W; EM; 18.00 A; H=1-511.
DR PDB; 5A1X; EM; 23.00 A; H/P/Q=1-511.
DR PDB; 5A1Y; EM; 21.00 A; H/P=1-511.
DR PDB; 5NZR; EM; 9.20 A; D=1-511.
DR PDB; 5NZS; EM; 10.10 A; D=1-511.
DR PDB; 5NZT; EM; 17.00 A; D/I=1-511.
DR PDB; 5NZU; EM; 15.00 A; D=1-511.
DR PDB; 5NZV; EM; 17.30 A; D/N=1-511.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; Q5XJY5; -.
DR SMR; Q5XJY5; -.
DR BioGRID; 229475; 17.
DR CORUM; Q5XJY5; -.
DR IntAct; Q5XJY5; 2.
DR MINT; Q5XJY5; -.
DR STRING; 10090.ENSMUSP00000034607; -.
DR iPTMnet; Q5XJY5; -.
DR PhosphoSitePlus; Q5XJY5; -.
DR SwissPalm; Q5XJY5; -.
DR REPRODUCTION-2DPAGE; Q5XJY5; -.
DR EPD; Q5XJY5; -.
DR jPOST; Q5XJY5; -.
DR MaxQB; Q5XJY5; -.
DR PaxDb; Q5XJY5; -.
DR PeptideAtlas; Q5XJY5; -.
DR PRIDE; Q5XJY5; -.
DR ProteomicsDB; 283492; -.
DR Antibodypedia; 32504; 215 antibodies from 24 providers.
DR DNASU; 213827; -.
DR Ensembl; ENSMUST00000034607; ENSMUSP00000034607; ENSMUSG00000032096.
DR GeneID; 213827; -.
DR KEGG; mmu:213827; -.
DR UCSC; uc009pei.2; mouse.
DR CTD; 372; -.
DR MGI; MGI:2387591; Arcn1.
DR VEuPathDB; HostDB:ENSMUSG00000032096; -.
DR eggNOG; KOG2635; Eukaryota.
DR GeneTree; ENSGT00390000017207; -.
DR HOGENOM; CLU_019988_3_0_1; -.
DR InParanoid; Q5XJY5; -.
DR OMA; YDARKHV; -.
DR OrthoDB; 1027200at2759; -.
DR PhylomeDB; Q5XJY5; -.
DR TreeFam; TF105760; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 213827; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Arcn1; mouse.
DR PRO; PR:Q5XJY5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5XJY5; protein.
DR Bgee; ENSMUSG00000032096; Expressed in seminal vesicle and 253 other tissues.
DR Genevisible; Q5XJY5; MM.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
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 DisProt; DP01657; -.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
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 Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..511
FT /note="Coatomer subunit delta"
FT /id="PRO_0000193842"
FT DOMAIN 271..511
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 168..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 351
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT CONFLICT 301
FT /note="I -> T (in Ref. 3; AAH83152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 57229 MW; 4C20F48A75330DC8 CRC64;
MVLLAAAVCT KAGKAIVSRQ FVEMTRTRIE GLLAAFPKLM NTGKQHTFVE TESVRYVYQP
MEKLYMVLIT TKNSNILEDL ETLRLFSRVI PEYCRALEEN EISEHCFDLI FAFDEIVALG
YRENVNLAQI RTFTEMDSHE EKVFRAVRET QEREAKAEMR RKAKELQQAR RDAERQGKKA
PGFGGFGSSA VSGGSTAAMI TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD
KLKSEGETIM SSNMGKRTSE ATKVHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
IMLRISDDKF GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG
VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP
VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIPG QPNDFFPVQV SFISKKNYCN
IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L
