ID NAR3_MOUSE Reviewed; 371 AA. AC Q8R2G4; B2RUC2; O54738; Q8R2F9; Q8R2G0; Q8R2G1; Q8R2G2; Q8R2G3; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 20-JAN-2009, sequence version 2. DT 29-MAY-2024, entry version 158. DE RecName: Full=Ecto-ADP-ribosyltransferase 3; DE EC=2.4.2.31; DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 3; DE Short=ARTC3; DE AltName: Full=Mono(ADP-ribosyl)transferase 3; DE AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 3; DE Flags: Precursor; GN Name=Art3; 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 [GENOMIC DNA / MRNA] (ISOFORM 5). RX PubMed=12070318; DOI=10.1110/ps.0200602; RA Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P., RA Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.; RT "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the RT mouse."; RL Protein Sci. 11:1657-1670(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 8). RC TISSUE=Testis; RA Koch-Nolte F., Firner K., Haag F., Khl M., Thiele H.G.; RT "Molecular cloning of two ecto-mono(ADP-ribosyl)transferases operating in RT murine testis."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Lung, and Testis; 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 -!- 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: Cell membrane {ECO:0000250}; Lipid-anchor, GPI- CC anchor {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=8; CC IsoId=Q8R2G4-5; Sequence=Displayed; CC Name=5; CC IsoId=Q8R2G4-7; Sequence=VSP_036193; CC Name=7; CC IsoId=Q8R2G4-8; Sequence=VSP_036199; CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC84526.1; Type=Miscellaneous discrepancy; Note=3'extension leads to out-of-frame translation.; Evidence={ECO:0000305}; CC Sequence=CAC84539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAC84540.1; Type=Miscellaneous discrepancy; Note=3'extension leads to out-of-frame translation.; Evidence={ECO:0000305}; CC Sequence=CAC84541.1; Type=Miscellaneous discrepancy; Note=3'extension leads to out-of-frame translation.; Evidence={ECO:0000305}; CC Sequence=CAC84543.1; Type=Miscellaneous discrepancy; Note=3'extension leads to out-of-frame translation.; Evidence={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; AJ311768; CAC84539.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ311769; CAC84526.1; ALT_SEQ; mRNA. DR EMBL; AJ311770; CAC84540.1; ALT_SEQ; mRNA. DR EMBL; AJ311771; CAC84541.1; ALT_SEQ; mRNA. DR EMBL; AJ311772; CAC84542.1; -; mRNA. DR EMBL; AJ311773; CAC84543.1; ALT_SEQ; mRNA. DR EMBL; Y08027; CAA69284.1; -; Genomic_DNA. DR EMBL; BC141069; AAI41070.1; -; mRNA. DR CCDS; CCDS51546.1; -. [Q8R2G4-8] DR CCDS; CCDS84904.1; -. [Q8R2G4-7] DR RefSeq; NP_001297594.1; NM_001310665.1. [Q8R2G4-7] DR RefSeq; NP_859417.2; NM_181728.3. [Q8R2G4-8] DR RefSeq; XP_006534780.1; XM_006534717.2. DR RefSeq; XP_006534781.1; XM_006534718.3. [Q8R2G4-8] DR AlphaFoldDB; Q8R2G4; -. DR SMR; Q8R2G4; -. DR IntAct; Q8R2G4; 1. DR STRING; 10090.ENSMUSP00000113510; -. DR GlyGen; Q8R2G4; 1 site, 1 O-linked glycan (1 site). DR PhosphoSitePlus; Q8R2G4; -. DR CPTAC; non-CPTAC-3404; -. DR CPTAC; non-CPTAC-3483; -. DR MaxQB; Q8R2G4; -. DR PaxDb; 10090-ENSMUSP00000113493; -. DR PeptideAtlas; Q8R2G4; -. DR ProteomicsDB; 252767; -. [Q8R2G4-5] DR ProteomicsDB; 252768; -. [Q8R2G4-7] DR ProteomicsDB; 252769; -. [Q8R2G4-8] DR Antibodypedia; 2182; 437 antibodies from 29 providers. DR DNASU; 109979; -. DR Ensembl; ENSMUST00000113083.9; ENSMUSP00000108706.3; ENSMUSG00000034842.17. [Q8R2G4-8] DR Ensembl; ENSMUST00000119587.8; ENSMUSP00000112648.2; ENSMUSG00000034842.17. [Q8R2G4-7] DR GeneID; 109979; -. DR KEGG; mmu:109979; -. DR UCSC; uc008ycw.1; mouse. [Q8R2G4-5] DR UCSC; uc008ycy.2; mouse. [Q8R2G4-8] DR UCSC; uc008ydg.2; mouse. [Q8R2G4-7] DR AGR; MGI:1202729; -. DR CTD; 419; -. DR MGI; MGI:1202729; Art3. DR VEuPathDB; HostDB:ENSMUSG00000034842; -. DR eggNOG; ENOG502SHYX; Eukaryota. DR GeneTree; ENSGT01030000234601; -. DR HOGENOM; CLU_059744_3_1_1; -. DR InParanoid; Q8R2G4; -. DR OMA; ANCVENM; -. DR PhylomeDB; Q8R2G4; -. DR TreeFam; TF335356; -. DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR BioGRID-ORCS; 109979; 5 hits in 78 CRISPR screens. DR ChiTaRS; Art3; mouse. DR PRO; PR:Q8R2G4; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q8R2G4; Protein. DR Bgee; ENSMUSG00000034842; Expressed in spermatocyte and 167 other cell types or tissues. DR ExpressionAtlas; Q8R2G4; baseline and differential. DR GO; GO:0005886; C:plasma 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; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR000768; ART. DR PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR10339:SF4; ECTO-ADP-RIBOSYLTRANSFERASE 3; 1. DR Pfam; PF01129; ART; 1. DR PRINTS; PR00970; RIBTRNSFRASE. DR SUPFAM; SSF56399; ADP-ribosylation; 1. DR PROSITE; PS51996; TR_MART; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; KW Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP; KW Nucleotidyltransferase; Reference proteome; Signal; Transferase. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..345 FT /note="Ecto-ADP-ribosyltransferase 3" FT /id="PRO_0000019327" FT PROPEP 346..371 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000019328" FT DOMAIN 64..250 FT /note="TR mART core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340" FT REGION 306..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..325 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 182 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT LIPID 345 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000250" FT DISULFID 43..255 FT /evidence="ECO:0000250" FT VAR_SEQ 271..291 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:12070318" FT /id="VSP_036193" FT VAR_SEQ 321..331 FT /note="DRSRGKANNPT -> A (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_036199" FT CONFLICT 11..15 FT /note="TLLAA -> AAGS (in Ref. 2; CAA69284)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="Missing (in Ref. 3; AAI41070)" FT /evidence="ECO:0000305" SQ SEQUENCE 371 AA; 42015 MW; 52F1B373A928182B CRC64; MKMGHFEMVT TLLAAAVLMD IFQVKAEVLD MAENAFDDEY LKCKSRMESK YIPQMKREEW ANDALLRMVW DNAEIQWEAR KAQLFLPRNF KDTYGIALTA YVNEAQEQTS FYHTFSSAVK MAGLSRRRYI YNFPFKAFHF YLVRALQLLR RPCEKSYKTV VYSTSPDISF TFGEQNQARL GNFTLAYSAK PETADNQRVL TIQTCFGVAV GKFLNKEDDS VVLIPLSEVF QVSRKGTSND LVLQSINSTC SYYECAFLGG LKTENCIANA EYIDPRYLYN PDMDNQKLED SGRNNLDPDR MPEIKVLQTE ENPLLPDEKP DRSRGKANNP TPGLVPGPKS HPSASSGNTL LPSVMASTIL LVASAVNFIE L //