ID   NAR5_RAT                Reviewed;         308 AA.
AC   Q5XHY4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ecto-ADP-ribosyltransferase 5;
DE            EC=2.4.2.31;
DE   AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 5;
DE            Short=ARTC5;
DE   AltName: Full=Mono(ADP-ribosyl)transferase 5;
DE   AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 5;
DE   Flags: Precursor;
GN   Name=Art5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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: Secreted {ECO:0000305}. Membrane {ECO:0000305}.
CC       Note=Membrane-associated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC083915; AAH83915.1; -; mRNA.
DR   RefSeq; NP_001013057.1; NM_001013039.1.
DR   RefSeq; XP_017444328.1; XM_017588839.1.
DR   AlphaFoldDB; Q5XHY4; -.
DR   SMR; Q5XHY4; -.
DR   STRING; 10116.ENSRNOP00000052118; -.
DR   GlyGen; Q5XHY4; 3 sites.
DR   PaxDb; Q5XHY4; -.
DR   PRIDE; Q5XHY4; -.
DR   GeneID; 259167; -.
DR   KEGG; rno:259167; -.
DR   UCSC; RGD:628834; rat.
DR   CTD; 116969; -.
DR   RGD; 628834; Art5.
DR   VEuPathDB; HostDB:ENSRNOG00000020242; -.
DR   eggNOG; ENOG502SKQR; Eukaryota.
DR   HOGENOM; CLU_059744_3_0_1; -.
DR   InParanoid; Q5XHY4; -.
DR   OMA; GDLHMKK; -.
DR   OrthoDB; 963174at2759; -.
DR   PhylomeDB; Q5XHY4; -.
DR   PRO; PR:Q5XHY4; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020242; Expressed in skeletal muscle tissue and 5 other tissues.
DR   Genevisible; Q5XHY4; RN.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProt.
DR   GO; GO:0005576; C:extracellular region; 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; PS01291; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Membrane; NAD; NADP;
KW   Nucleotidyltransferase; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..308
FT                   /note="Ecto-ADP-ribosyltransferase 5"
FT                   /id="PRO_0000379472"
FT   DOMAIN          63..253
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..259
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  34201 MW;  45B0063435437D2F CRC64;
     MILEDLLMVL SCLALHILWK VQAVPILPLS LVPDTFDDAY VGCSEEMEEK AGLLLKEEMA
     RHALLRESWE AAQEAWAHGR HKLTLPPGFK AQHGVAVMVY TNSSNTLYWE LNQAVRTGGR
     SRELYMRHFP FKALHFYLTR ALQLLRGTGG CSREAGEVVF RGVSSLHFEP KRLGDSVRLG
     QFASSSVDER VARRFGNATF FNLRTCFGAP IQALSVFPEE REVLIPPHEV FLVTGFSQDG
     AQSIVTLWSY NQTCSHFNCA YLGGEKRRGC VSSRAGQPES FSTEALALQS GKTLLLAPGE
     LQLSRAGP