ID NAR1_HUMAN Reviewed; 327 AA. AC P52961; Q6NTD2; Q96KT9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 2. DT 12-AUG-2020, entry version 158. DE RecName: Full=GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; DE EC=2.4.2.31; DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 1; DE Short=ARTC1; DE AltName: Full=Mono(ADP-ribosyl)transferase 1; DE AltName: CD_antigen=CD296; DE Flags: Precursor; GN Name=ART1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-257. RC TISSUE=Skeletal muscle; RX PubMed=7947688; DOI=10.1021/bi00209a014; RA Okazaki I.J., Zolkiewska A., Nightingale M.S., Moss J.; RT "Immunological and structural conservation of mammalian skeletal muscle RT glycosylphosphatidylinositol-linked ADP-ribosyltransferases."; RL Biochemistry 33:12828-12836(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 122-223. RA Kuehl M., Glowacki G., Haag F., Koch-Nolte F.; RT "Conservation of the ART gene family across mammalian species."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NOMENCLATURE. RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003; RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.; RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."; RL Trends Biochem. Sci. 35:208-219(2010). RN [6] RP FUNCTION. RX PubMed=21901419; DOI=10.1007/s11033-011-1225-0; RA Dezelak M., Bavec A.; RT "Glucagon like-peptide-1 receptor is covalently modified by endogenous RT mono-ADP-ribosyltransferase."; RL Mol. Biol. Rep. 39:4375-4381(2012). CC -!- FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R. CC {ECO:0000269|PubMed:21901419}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D- CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:142554; EC=2.4.2.31; CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Lipid-anchor, CC GPI-anchor. CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S74683; AAB32387.1; -; mRNA. DR EMBL; CH471158; EAX02559.1; -; Genomic_DNA. DR EMBL; BC069102; AAH69102.1; -; mRNA. DR EMBL; BC111729; AAI11730.1; -; mRNA. DR EMBL; AJ291430; CAC69964.1; -; mRNA. DR CCDS; CCDS7744.1; -. DR PIR; A55966; A55966. DR RefSeq; NP_004305.2; NM_004314.2. DR RefSeq; XP_011518416.1; XM_011520114.2. DR RefSeq; XP_016873252.1; XM_017017763.1. DR SMR; P52961; -. DR BioGRID; 106910; 6. DR STRING; 9606.ENSP00000250693; -. DR ChEMBL; CHEMBL2158; -. DR DrugBank; DB01854; 5-Bromonicotinamide. DR GlyGen; P52961; 2 sites. DR PhosphoSitePlus; P52961; -. DR BioMuta; ART1; -. DR DMDM; 206729882; -. DR MassIVE; P52961; -. DR PaxDb; P52961; -. DR PeptideAtlas; P52961; -. DR PRIDE; P52961; -. DR ProteomicsDB; 56565; -. DR Antibodypedia; 23357; 206 antibodies. DR Ensembl; ENST00000250693; ENSP00000250693; ENSG00000129744. DR GeneID; 417; -. DR KEGG; hsa:417; -. DR UCSC; uc001lye.1; human. DR CTD; 417; -. DR DisGeNET; 417; -. DR EuPathDB; HostDB:ENSG00000129744.2; -. DR GeneCards; ART1; -. DR HGNC; HGNC:723; ART1. DR HPA; ENSG00000129744; Group enriched (skeletal muscle, tongue). DR MIM; 601625; gene. DR neXtProt; NX_P52961; -. DR OpenTargets; ENSG00000129744; -. DR PharmGKB; PA25014; -. DR eggNOG; ENOG502QUE9; Eukaryota. DR GeneTree; ENSGT01000000214454; -. DR HOGENOM; CLU_059744_1_0_1; -. DR InParanoid; P52961; -. DR KO; K06716; -. DR OMA; NSAMGQG; -. DR OrthoDB; 963174at2759; -. DR PhylomeDB; P52961; -. DR TreeFam; TF335356; -. DR PathwayCommons; P52961; -. DR Reactome; R-HSA-1462054; Alpha-defensins. DR BioGRID-ORCS; 417; 1 hit in 869 CRISPR screens. DR ChiTaRS; ART1; human. DR GenomeRNAi; 417; -. DR Pharos; P52961; Tbio. DR PRO; PR:P52961; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P52961; protein. DR Bgee; ENSG00000129744; Expressed in muscle of leg and 86 other tissues. DR Genevisible; P52961; HS. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; TAS:Reactome. DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central. DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central. DR GO; GO:0006471; P:protein ADP-ribosylation; IBA:GO_Central. DR InterPro; IPR000768; ART. DR Pfam; PF01129; ART; 1. DR PRINTS; PR00970; RIBTRNSFRASE. DR PROSITE; PS01291; ART; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Glycosyltransferase; GPI-anchor; Lipoprotein; KW Membrane; NAD; NADP; Polymorphism; Reference proteome; KW Sarcoplasmic reticulum; Signal; Transferase. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..295 FT /note="GPI-linked NAD(P)(+)--arginine ADP- FT ribosyltransferase 1" FT /id="PRO_0000019311" FT PROPEP 296..327 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000019312" FT ACT_SITE 247 FT /evidence="ECO:0000250" FT BINDING 121 FT /note="NAD" FT /evidence="ECO:0000250" FT BINDING 179 FT /note="NAD" FT /evidence="ECO:0000250" FT BINDING 233 FT /note="NAD" FT /evidence="ECO:0000250" FT LIPID 295 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000255" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 253 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 53..277 FT /evidence="ECO:0000250" FT DISULFID 174..224 FT /evidence="ECO:0000250" FT VARIANT 105 FT /note="P -> L (in dbSNP:rs35123761)" FT /id="VAR_034125" FT VARIANT 126 FT /note="P -> R (in dbSNP:rs35619488)" FT /id="VAR_034126" FT VARIANT 257 FT /note="L -> P (in dbSNP:rs2280134)" FT /evidence="ECO:0000269|PubMed:7947688" FT /id="VAR_053526" SQ SEQUENCE 327 AA; 36335 MW; 8FDC568197031EA5 CRC64; MQMPAMMSLL LVSVGLMEAL QAQSHPITRR DLFSQEIQLD MALASFDDQY AGCAAAMTAA LPDLNHTEFQ ANQVYADSWT LASSQWQERQ ARWPEWSLSP TRPSPPPLGF RDEHGVALLA YTANSPLHKE FNAAVREAGR SRAHYLHHFS FKTLHFLLTE ALQLLGSGQR PPRCHQVFRG VHGLRFRPAG PRATVRLGGF ASASLKHVAA QQFGEDTFFG IWTCLGAPIK GYSFFPGEEE VLIPPFETFQ VINASRLAQG PARIYLRALG KHSTYNCEYI KDKKCKSGPC HLDNSAMGQS PLSAVWSLLL LLWFLVVRAF PDGPGLL //