NAR3_MOUSE
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 03-AUG-2022, entry version 148.
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};
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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.ENSMUSP00000113493; -.
DR PhosphoSitePlus; Q8R2G4; -.
DR CPTAC; non-CPTAC-3404; -.
DR CPTAC; non-CPTAC-3483; -.
DR MaxQB; Q8R2G4; -.
DR PaxDb; Q8R2G4; -.
DR PeptideAtlas; Q8R2G4; -.
DR PRIDE; Q8R2G4; -.
DR ProteomicsDB; 252767; -. [Q8R2G4-5]
DR ProteomicsDB; 252768; -. [Q8R2G4-7]
DR ProteomicsDB; 252769; -. [Q8R2G4-8]
DR Antibodypedia; 2182; 407 antibodies from 29 providers.
DR DNASU; 109979; -.
DR Ensembl; ENSMUST00000113083; ENSMUSP00000108706; ENSMUSG00000034842. [Q8R2G4-8]
DR Ensembl; ENSMUST00000119587; ENSMUSP00000112648; ENSMUSG00000034842. [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 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; IYSFQFK; -.
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 73 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 164 other tissues.
DR ExpressionAtlas; Q8R2G4; baseline and differential.
DR Genevisible; Q8R2G4; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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; IEA:UniProtKB-EC.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
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
