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Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP)

 COPD_MOUSE              Reviewed;         511 AA.
Q5XJY5; Q91W48;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
07-NOV-2018, entry version 121.
RecName: Full=Coatomer subunit delta;
AltName: Full=Archain;
AltName: Full=Delta-coat protein;
Short=Delta-COP;
Name=Arcn1; Synonyms=Copd;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N;
TISSUE=Embryonic germ cell, Eye, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241 AND LYS-351, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. Delta-COP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK028556; BAC26007.1; -; mRNA.
EMBL; CH466522; EDL25614.1; -; Genomic_DNA.
EMBL; BC017124; AAH17124.1; -; mRNA.
EMBL; BC023728; AAH23728.1; -; mRNA.
EMBL; BC033387; AAH33387.1; -; mRNA.
EMBL; BC034754; AAH34754.1; -; mRNA.
EMBL; BC083152; AAH83152.1; -; mRNA.
CCDS; CCDS40602.1; -.
RefSeq; NP_666097.3; NM_145985.4.
UniGene; Mm.371682; -.
PDB; 5A1U; EM; 13.00 A; H=1-511.
PDB; 5A1V; EM; 21.00 A; H/P/Y=1-511.
PDB; 5A1W; EM; 18.00 A; H=1-511.
PDB; 5A1X; EM; 23.00 A; H/P/Q=1-511.
PDB; 5A1Y; EM; 21.00 A; H/P=1-511.
PDB; 5NZR; EM; 9.20 A; D=1-511.
PDB; 5NZS; EM; 10.10 A; D=1-511.
PDB; 5NZT; EM; 17.00 A; D/I=1-511.
PDB; 5NZU; EM; 15.00 A; D=1-511.
PDB; 5NZV; EM; 17.30 A; D/N=1-511.
PDBsum; 5A1U; -.
PDBsum; 5A1V; -.
PDBsum; 5A1W; -.
PDBsum; 5A1X; -.
PDBsum; 5A1Y; -.
PDBsum; 5NZR; -.
PDBsum; 5NZS; -.
PDBsum; 5NZT; -.
PDBsum; 5NZU; -.
PDBsum; 5NZV; -.
ProteinModelPortal; Q5XJY5; -.
SMR; Q5XJY5; -.
BioGrid; 229475; 4.
CORUM; Q5XJY5; -.
IntAct; Q5XJY5; 3.
MINT; Q5XJY5; -.
STRING; 10090.ENSMUSP00000034607; -.
iPTMnet; Q5XJY5; -.
PhosphoSitePlus; Q5XJY5; -.
SwissPalm; Q5XJY5; -.
REPRODUCTION-2DPAGE; Q5XJY5; -.
EPD; Q5XJY5; -.
MaxQB; Q5XJY5; -.
PaxDb; Q5XJY5; -.
PeptideAtlas; Q5XJY5; -.
PRIDE; Q5XJY5; -.
Ensembl; ENSMUST00000034607; ENSMUSP00000034607; ENSMUSG00000032096.
GeneID; 213827; -.
KEGG; mmu:213827; -.
UCSC; uc009pei.2; mouse.
CTD; 372; -.
MGI; MGI:2387591; Arcn1.
eggNOG; KOG2635; Eukaryota.
eggNOG; ENOG410XRH2; LUCA.
GeneTree; ENSGT00390000017207; -.
HOGENOM; HOG000203984; -.
HOVERGEN; HBG005381; -.
InParanoid; Q5XJY5; -.
KO; K20471; -.
OMA; FLDMESH; -.
OrthoDB; EOG091G08B5; -.
TreeFam; TF105760; -.
Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:Q5XJY5; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032096; Expressed in 298 organ(s), highest expression level in seminal vesicle.
CleanEx; MM_ARCN1; -.
Genevisible; Q5XJY5; MM.
GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IMP:MGI.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
GO; GO:0048193; P:Golgi vesicle transport; IMP:MGI.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
InterPro; IPR036168; AP2_Mu_C_sf.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR027059; Coatomer_dsu.
InterPro; IPR011012; Longin-like_dom_sf.
InterPro; IPR028565; MHD.
PANTHER; PTHR10121; PTHR10121; 1.
Pfam; PF00928; Adap_comp_sub; 1.
Pfam; PF01217; Clat_adaptor_s; 1.
SUPFAM; SSF49447; SSF49447; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS51072; MHD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Transport.
CHAIN 1 511 Coatomer subunit delta.
/FTId=PRO_0000193842.
DOMAIN 271 511 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000250|UniProtKB:P48444}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000250|UniProtKB:P48444}.
MOD_RES 241 241 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:P48444}.
MOD_RES 309 309 N6-acetyllysine.
{ECO:0000250|UniProtKB:P48444}.
MOD_RES 351 351 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:P48444}.
CONFLICT 301 301 I -> T (in Ref. 3; AAH83152).
{ECO:0000305}.
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


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