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   24-JAN-2024, entry version 174.
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   GlyCosmos; P52961; 2 sites, No reported glycans.
DR   GlyGen; P52961; 2 sites.
DR   PhosphoSitePlus; P52961; -.
DR   BioMuta; ART1; -.
DR   DMDM; 206729882; -.
DR   MassIVE; P52961; -.
DR   PaxDb; 9606-ENSP00000250693; -.
DR   PeptideAtlas; P52961; -.
DR   Antibodypedia; 23357; 249 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   AGR; HGNC:723; -.
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; FETFQVV; -.
DR   OrthoDB; 2897283at2759; -.
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; 9 hits in 1150 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 87 other cell types or tissues.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000768; ART.
DR   PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10339:SF19; GPI-LINKED NAD(P)(+)--ARGININE ADP-RIBOSYLTRANSFERASE 1; 1.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   PROSITE; PS01291; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
DR   Genevisible; P52961; HS.
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
//