NAR1_HUMAN
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 03-AUG-2022, entry version 166.
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}.
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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 AlphaFoldDB; P52961; -.
DR SMR; P52961; -.
DR BioGRID; 106910; 14.
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 Antibodypedia; 23357; 217 antibodies from 22 providers.
DR DNASU; 417; -.
DR Ensembl; ENST00000250693.2; ENSP00000250693.1; ENSG00000129744.3.
DR GeneID; 417; -.
DR KEGG; hsa:417; -.
DR MANE-Select; ENST00000250693.2; ENSP00000250693.1; NM_004314.3; NP_004305.2.
DR UCSC; uc001lye.1; human.
DR CTD; 417; -.
DR DisGeNET; 417; -.
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 VEuPathDB; HostDB:ENSG00000129744; -.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_1_0_1; -.
DR InParanoid; P52961; -.
DR OMA; DKQCKSG; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; P52961; -.
DR TreeFam; TF335356; -.
DR BRENDA; 2.4.2.31; 2681.
DR PathwayCommons; P52961; -.
DR Reactome; R-HSA-1462054; Alpha-defensins.
DR SignaLink; P52961; -.
DR BioGRID-ORCS; 417; 6 hits in 1073 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 hindlimb stylopod muscle 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:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; TAS:Reactome.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; TAS:ProtInc.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; GPI-anchor; Lipoprotein;
KW Membrane; NAD; NADP; Nucleotidyltransferase; 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 DOMAIN 73..273
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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
