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   22-APR-2020, entry version 138.
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   SMR; Q8R2G4; -.
DR   IntAct; Q8R2G4; 1.
DR   STRING; 10090.ENSMUSP00000113493; -.
DR   PhosphoSitePlus; Q8R2G4; -.
DR   CPTAC; non-CPTAC-3404; -.
DR   CPTAC; non-CPTAC-3483; -.
DR   PaxDb; Q8R2G4; -.
DR   PeptideAtlas; Q8R2G4; -.
DR   PRIDE; Q8R2G4; -.
DR   Antibodypedia; 2182; 362 antibodies.
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   eggNOG; ENOG410J8VA; Eukaryota.
DR   eggNOG; ENOG411167J; LUCA.
DR   GeneTree; ENSGT00950000182811; -.
DR   HOGENOM; CLU_059744_3_1_1; -.
DR   InParanoid; Q8R2G4; -.
DR   KO; K00775; -.
DR   PhylomeDB; Q8R2G4; -.
DR   TreeFam; TF335356; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   ChiTaRS; Art3; mouse.
DR   PRO; PR:Q8R2G4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8R2G4; protein.
DR   Bgee; ENSMUSG00000034842; Expressed in testis and 160 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:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR   GO; GO:0006471; P:protein ADP-ribosylation; IBA:GO_Central.
DR   InterPro; IPR000768; ART.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP;
KW   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   ACT_SITE        228
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /note="NAD"
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
//