NAR1_MOUSE
ID NAR1_MOUSE Reviewed; 325 AA.
AC Q60935; P70688;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
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: Full=YAC-1;
DE AltName: CD_antigen=CD296;
DE Flags: Precursor;
GN Name=Art1; Synonyms=Art2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=8704249;
RA Okazaki I.J., Kim H.-J., McElvaney N.G., Lesma E., Moss J.;
RT "Molecular characterization of a glycosylphosphatidylinositol-linked ADP-
RT ribosyltransferase from lymphocytes.";
RL Blood 88:915-921(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8812442; DOI=10.1006/geno.1996.0451;
RA Koch-Nolte F., Kuehl M., Haag F., Cetkovic-Cvrlje M., Leiter E.H.,
RA Thiele H.-G.;
RT "Assignment of the human and mouse genes for muscle ecto mono
RT (ADPribosyl)transferase to a conserved linkage group on human chromosome
RT 11p15 and mouse chromosome 7.";
RL Genomics 36:215-216(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9052744; DOI=10.1089/dna.1997.16.235;
RA Yu Y., Okamoto S., Nemoto E., Dennert G.;
RT "Molecular cloning of a functional murine arginine-specific mono-ADP-
RT ribosyltransferase and its expression in lymphoid cells.";
RL DNA Cell Biol. 16:235-244(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R.
CC {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Abundantly expressed in cardiac and skeletal
CC muscle. Low levels also found in lung.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U31510; AAB18628.1; -; mRNA.
DR EMBL; X95825; CAA65094.1; -; Genomic_DNA.
DR EMBL; X95842; CAA65099.1; -; mRNA.
DR EMBL; BC063760; AAH63760.1; -; mRNA.
DR CCDS; CCDS21526.1; -.
DR RefSeq; NP_033840.2; NM_009710.4.
DR RefSeq; XP_011239959.1; XM_011241657.1.
DR AlphaFoldDB; Q60935; -.
DR SMR; Q60935; -.
DR IntAct; Q60935; 1.
DR STRING; 10090.ENSMUSP00000033300; -.
DR GlyGen; Q60935; 2 sites.
DR iPTMnet; Q60935; -.
DR PhosphoSitePlus; Q60935; -.
DR MaxQB; Q60935; -.
DR PaxDb; Q60935; -.
DR PRIDE; Q60935; -.
DR ProteomicsDB; 287437; -.
DR Antibodypedia; 23357; 217 antibodies from 22 providers.
DR DNASU; 11870; -.
DR Ensembl; ENSMUST00000033300; ENSMUSP00000033300; ENSMUSG00000030996.
DR Ensembl; ENSMUST00000209809; ENSMUSP00000147911; ENSMUSG00000030996.
DR GeneID; 11870; -.
DR KEGG; mmu:11870; -.
DR UCSC; uc009iqu.1; mouse.
DR CTD; 417; -.
DR MGI; MGI:107511; Art1.
DR VEuPathDB; HostDB:ENSMUSG00000030996; -.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_1_0_1; -.
DR InParanoid; Q60935; -.
DR OMA; DKQCKSG; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; Q60935; -.
DR TreeFam; TF335356; -.
DR BRENDA; 2.4.2.31; 3474.
DR Reactome; R-MMU-1462054; Alpha-defensins.
DR BioGRID-ORCS; 11870; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Art1; mouse.
DR PRO; PR:Q60935; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q60935; protein.
DR Bgee; ENSMUSG00000030996; Expressed in temporalis muscle and 133 other tissues.
DR ExpressionAtlas; Q60935; baseline and differential.
DR Genevisible; Q60935; MM.
DR GO; GO:0031225; C:anchored component of membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:MGI.
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 1: Evidence at protein 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..290
FT /note="GPI-linked NAD(P)(+)--arginine ADP-
FT ribosyltransferase 1"
FT /id="PRO_0000019313"
FT PROPEP 291..325
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019314"
FT DOMAIN 73..268
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 290
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 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..272
FT /evidence="ECO:0000250"
FT DISULFID 169..219
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="P -> Q (in Ref. 2; CAA65094)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="R -> L (in Ref. 2; CAA65094)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..290
FT /note="Missing (in Ref. 2; CAA65094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35898 MW; 763EB891F2A49474 CRC64;
MKIPAMMSLL LVSVGLRDGV QVQSYSISQL DIFSQETPLD MAPASFDDQY AGCLADMTAA
LPDLNHSEFQ ANKVYADGWA QANNQWQERR AWGSVWGSLP PSPPGFRDEH GVALLAYTAN
SPLHKEFNAA VREAGRSRAH YLHHFSFKTL HFLLTEALQL LRSHRSRGCQ QVYRGVHGLR
FRPAGPGATV RLGGFASASL KNVAAQQFGE DTFFGIWTCL GAPIRGYSFF PEEEEVLIPP
FETFQVINTS RPTQGPARIY LRALGKRSTY NCEYIKEKKC RSGPCWLGSS APGSISASCS
LLLLLLFLVL SALPENPGLQ QLTRC
