Full text data of ARCN1
ARCN1
(COPD)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Coatomer subunit delta (Archain; Delta-coat protein; Delta-COP)
Coatomer subunit delta (Archain; Delta-coat protein; Delta-COP)
UniProt
P48444
ID COPD_HUMAN Reviewed; 511 AA.
AC P48444; B4E1X2; E9PEU4; Q52M80;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 115.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7782067; DOI=10.1016/0888-7543(95)80087-3;
RA Radice P., Pensotti V., Jones C., Perry H., Pierotti M.A.,
RA Tunnacliffe A.;
RT "The human archain gene, ARCN1, has highly conserved homologs in rice
RT and Drosophila.";
RL Genomics 26:101-106(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-309, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48444-2; Sequence=VSP_045636;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family. Delta-COP subfamily.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57072.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X81197; CAA57071.1; -; mRNA.
DR EMBL; X81198; CAA57072.1; ALT_INIT; mRNA.
DR EMBL; AK304019; BAG64934.1; -; mRNA.
DR EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093636; AAH93636.1; -; mRNA.
DR EMBL; BC093638; AAH93638.1; -; mRNA.
DR PIR; A56750; A56750.
DR RefSeq; NP_001135753.1; NM_001142281.1.
DR RefSeq; NP_001646.2; NM_001655.4.
DR UniGene; Hs.33642; -.
DR ProteinModelPortal; P48444; -.
DR DIP; DIP-50375N; -.
DR IntAct; P48444; 12.
DR MINT; MINT-3016718; -.
DR STRING; 9606.ENSP00000264028; -.
DR PhosphoSite; P48444; -.
DR DMDM; 1351970; -.
DR OGP; P48444; -.
DR PaxDb; P48444; -.
DR PRIDE; P48444; -.
DR Ensembl; ENST00000264028; ENSP00000264028; ENSG00000095139.
DR Ensembl; ENST00000392859; ENSP00000376599; ENSG00000095139.
DR Ensembl; ENST00000593602; ENSP00000468926; ENSG00000269382.
DR Ensembl; ENST00000596715; ENSP00000471768; ENSG00000269382.
DR GeneID; 372; -.
DR KEGG; hsa:372; -.
DR UCSC; uc010ryg.2; human.
DR CTD; 372; -.
DR GeneCards; GC11P118444; -.
DR HGNC; HGNC:649; ARCN1.
DR HPA; HPA037573; -.
DR MIM; 600820; gene.
DR neXtProt; NX_P48444; -.
DR PharmGKB; PA24931; -.
DR eggNOG; NOG309668; -.
DR HOGENOM; HOG000203984; -.
DR HOVERGEN; HBG005381; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P48444; -.
DR ChiTaRS; ARCN1; human.
DR GenomeRNAi; 372; -.
DR NextBio; 1553; -.
DR PRO; PR:P48444; -.
DR ArrayExpress; P48444; -.
DR Bgee; P48444; -.
DR CleanEx; HS_ARCN1; -.
DR Genevestigator; P48444; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR008968; Clathrin_mu_C.
DR InterPro; IPR027059; Coatomer_dsu.
DR InterPro; IPR011012; Longin-like_dom.
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 Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 511 Coatomer subunit delta.
FT /FTId=PRO_0000193841.
FT DOMAIN 271 511 MHD.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 309 309 N6-acetyllysine.
FT MOD_RES 493 493 Phosphoserine.
FT VAR_SEQ 1 89 MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMN
FT TGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLET
FT LRLFSRV -> M (in isoform 2).
FT /FTId=VSP_045636.
FT VARIANT 186 186 F -> L (in dbSNP:rs682327).
FT /FTId=VAR_011788.
FT VARIANT 309 309 K -> N (in dbSNP:rs1063124).
FT /FTId=VAR_011789.
FT CONFLICT 387 387 N -> D (in Ref. 2; BAG64934).
SQ SEQUENCE 511 AA; 57210 MW; 4ED1F7D2D12A7F75 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 SSSMGKRTSE ATKMHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
IMLRISDDKY GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG
VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP
VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIAG QPNDFFPVQV SFVSKKNYCN
IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L
//
ID COPD_HUMAN Reviewed; 511 AA.
AC P48444; B4E1X2; E9PEU4; Q52M80;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 115.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7782067; DOI=10.1016/0888-7543(95)80087-3;
RA Radice P., Pensotti V., Jones C., Perry H., Pierotti M.A.,
RA Tunnacliffe A.;
RT "The human archain gene, ARCN1, has highly conserved homologs in rice
RT and Drosophila.";
RL Genomics 26:101-106(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-309, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48444-2; Sequence=VSP_045636;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family. Delta-COP subfamily.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57072.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X81197; CAA57071.1; -; mRNA.
DR EMBL; X81198; CAA57072.1; ALT_INIT; mRNA.
DR EMBL; AK304019; BAG64934.1; -; mRNA.
DR EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093636; AAH93636.1; -; mRNA.
DR EMBL; BC093638; AAH93638.1; -; mRNA.
DR PIR; A56750; A56750.
DR RefSeq; NP_001135753.1; NM_001142281.1.
DR RefSeq; NP_001646.2; NM_001655.4.
DR UniGene; Hs.33642; -.
DR ProteinModelPortal; P48444; -.
DR DIP; DIP-50375N; -.
DR IntAct; P48444; 12.
DR MINT; MINT-3016718; -.
DR STRING; 9606.ENSP00000264028; -.
DR PhosphoSite; P48444; -.
DR DMDM; 1351970; -.
DR OGP; P48444; -.
DR PaxDb; P48444; -.
DR PRIDE; P48444; -.
DR Ensembl; ENST00000264028; ENSP00000264028; ENSG00000095139.
DR Ensembl; ENST00000392859; ENSP00000376599; ENSG00000095139.
DR Ensembl; ENST00000593602; ENSP00000468926; ENSG00000269382.
DR Ensembl; ENST00000596715; ENSP00000471768; ENSG00000269382.
DR GeneID; 372; -.
DR KEGG; hsa:372; -.
DR UCSC; uc010ryg.2; human.
DR CTD; 372; -.
DR GeneCards; GC11P118444; -.
DR HGNC; HGNC:649; ARCN1.
DR HPA; HPA037573; -.
DR MIM; 600820; gene.
DR neXtProt; NX_P48444; -.
DR PharmGKB; PA24931; -.
DR eggNOG; NOG309668; -.
DR HOGENOM; HOG000203984; -.
DR HOVERGEN; HBG005381; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P48444; -.
DR ChiTaRS; ARCN1; human.
DR GenomeRNAi; 372; -.
DR NextBio; 1553; -.
DR PRO; PR:P48444; -.
DR ArrayExpress; P48444; -.
DR Bgee; P48444; -.
DR CleanEx; HS_ARCN1; -.
DR Genevestigator; P48444; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR008968; Clathrin_mu_C.
DR InterPro; IPR027059; Coatomer_dsu.
DR InterPro; IPR011012; Longin-like_dom.
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 Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 511 Coatomer subunit delta.
FT /FTId=PRO_0000193841.
FT DOMAIN 271 511 MHD.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 309 309 N6-acetyllysine.
FT MOD_RES 493 493 Phosphoserine.
FT VAR_SEQ 1 89 MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMN
FT TGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLET
FT LRLFSRV -> M (in isoform 2).
FT /FTId=VSP_045636.
FT VARIANT 186 186 F -> L (in dbSNP:rs682327).
FT /FTId=VAR_011788.
FT VARIANT 309 309 K -> N (in dbSNP:rs1063124).
FT /FTId=VAR_011789.
FT CONFLICT 387 387 N -> D (in Ref. 2; BAG64934).
SQ SEQUENCE 511 AA; 57210 MW; 4ED1F7D2D12A7F75 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 SSSMGKRTSE ATKMHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
IMLRISDDKY GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG
VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP
VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIAG QPNDFFPVQV SFVSKKNYCN
IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L
//
MIM
600820
*RECORD*
*FIELD* NO
600820
*FIELD* TI
*600820 ARCHAIN 1; ARCN1
*FIELD* TX
Radice et al. (1995) identified a gene that maps approximately 50-kb
read moretelomeric to MLL (159555) in band 11q23.3, a locus disrupted in certain
leukemia-associated translocation chromosomes. A 200-kb genomic fragment
from a YAC that includes MLL was used to screen a cDNA library of the
R54;11 cell line which carries a translocation chromosome t(4;11)(q21;
q23). The cDNA sequence predicts a 511-amino acid protein which shares
similarity with predicted proteins of unknown function from rice (Oryza
sativa) and Drosophila. Because of this ancient conservation the authors
proposed the name archain (ARCN1). Radice et al. (1995) detected 4-kb
ARCN1 transcripts by Northern blot analysis in all tissues examined.
The protein encoded by the ARCN1 gene, the coatomer protein delta-COP,
probably plays a fundamental role in eukaryotic cell biology.
Tunnacliffe at al. (1996) demonstrated that it is conserved across
diverse eukaryotes. Very close or identical matches were seen in rat and
cow; highly significant matches were seen with 2 plant species, A.
thaliana (cress) and S. tuberosum (potato). Of particular biologic
significance was the match with a sequence on yeast chromosome VI, from
which Tunnacliffe et al. (1996) were able to determine the yeast archain
gene and protein sequence. Unpublished data indicated that in situ
hybridizations on mouse embryo sections showed archain transcripts
throughout the whole animal.
*FIELD* RF
1. Radice, P.; Pensotti, V.; Jones, C.; Perry, H.; Pierotti, M. A.;
Tunnacliffe, A.: The human archain gene, ARCN1, has highly conserved
homologs in rice and Drosophila. Genomics 26: 101-106, 1995.
2. Tunnacliffe, A.; van de Vrugt, H.; Pensotti, V.; Radice, P.: The
coatomer protein delta-COP, encoded by the archain gene, is conserved
across diverse eukaryotes. Mammalian Genome 7: 784-786, 1996.
*FIELD* CD
Alan F. Scott: 10/2/1995
*FIELD* ED
jenny: 12/12/1996
mark: 4/7/1996
joanna: 2/2/1996
mark: 10/2/1995
*RECORD*
*FIELD* NO
600820
*FIELD* TI
*600820 ARCHAIN 1; ARCN1
*FIELD* TX
Radice et al. (1995) identified a gene that maps approximately 50-kb
read moretelomeric to MLL (159555) in band 11q23.3, a locus disrupted in certain
leukemia-associated translocation chromosomes. A 200-kb genomic fragment
from a YAC that includes MLL was used to screen a cDNA library of the
R54;11 cell line which carries a translocation chromosome t(4;11)(q21;
q23). The cDNA sequence predicts a 511-amino acid protein which shares
similarity with predicted proteins of unknown function from rice (Oryza
sativa) and Drosophila. Because of this ancient conservation the authors
proposed the name archain (ARCN1). Radice et al. (1995) detected 4-kb
ARCN1 transcripts by Northern blot analysis in all tissues examined.
The protein encoded by the ARCN1 gene, the coatomer protein delta-COP,
probably plays a fundamental role in eukaryotic cell biology.
Tunnacliffe at al. (1996) demonstrated that it is conserved across
diverse eukaryotes. Very close or identical matches were seen in rat and
cow; highly significant matches were seen with 2 plant species, A.
thaliana (cress) and S. tuberosum (potato). Of particular biologic
significance was the match with a sequence on yeast chromosome VI, from
which Tunnacliffe et al. (1996) were able to determine the yeast archain
gene and protein sequence. Unpublished data indicated that in situ
hybridizations on mouse embryo sections showed archain transcripts
throughout the whole animal.
*FIELD* RF
1. Radice, P.; Pensotti, V.; Jones, C.; Perry, H.; Pierotti, M. A.;
Tunnacliffe, A.: The human archain gene, ARCN1, has highly conserved
homologs in rice and Drosophila. Genomics 26: 101-106, 1995.
2. Tunnacliffe, A.; van de Vrugt, H.; Pensotti, V.; Radice, P.: The
coatomer protein delta-COP, encoded by the archain gene, is conserved
across diverse eukaryotes. Mammalian Genome 7: 784-786, 1996.
*FIELD* CD
Alan F. Scott: 10/2/1995
*FIELD* ED
jenny: 12/12/1996
mark: 4/7/1996
joanna: 2/2/1996
mark: 10/2/1995