NAR5_MOUSE
ID NAR5_MOUSE Reviewed; 309 AA.
AC P70352; E9QM95; Q91VF7; Q91X06; Q91X07; Q921A5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
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 AltName: Full=YAC-2;
DE Flags: Precursor;
GN Name=Art5;
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] (ISOFORM 1).
RC TISSUE=Lymphoma;
RX PubMed=8703012; DOI=10.1074/jbc.271.36.22052;
RA Okazaki I.J., Kim H.-J., Moss J.;
RT "Cloning and characterization of a novel membrane-associated lymphocyte
RT NAD:arginine ADP-ribosyltransferase.";
RL J. Biol. Chem. 271:22052-22057(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=129/Ola; TISSUE=Testis;
RX PubMed=11587854; DOI=10.1016/s0378-1119(01)00608-4;
RA Glowacki G., Braren R., Cetkovic-Cvrlje M., Leiter E.H., Haag F.,
RA Koch-Nolte F.;
RT "Structure, chromosomal localization, and expression of the gene for mouse
RT ecto-mono(ADP-ribosyl)transferase ART5.";
RL Gene 275:267-277(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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. Membrane. Note=Membrane-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P70352-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70352-2; Sequence=VSP_003380;
CC Name=3;
CC IsoId=P70352-3; Sequence=VSP_003381;
CC Name=4;
CC IsoId=P70352-4; Sequence=VSP_003382, VSP_003383;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis. Lower levels in
CC cardiac and skeletal muscle.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U60881; AAC52773.1; -; mRNA.
DR EMBL; AJ295722; CAC48193.1; -; Genomic_DNA.
DR EMBL; AJ297547; CAC50566.1; -; mRNA.
DR EMBL; AJ297548; CAC50567.1; -; mRNA.
DR EMBL; AJ295843; CAC69242.1; -; mRNA.
DR EMBL; AC132297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS21525.1; -. [P70352-1]
DR RefSeq; NP_001278283.1; NM_001291354.1. [P70352-1]
DR RefSeq; NP_031517.2; NM_007491.2. [P70352-1]
DR RefSeq; XP_006507322.1; XM_006507259.3. [P70352-3]
DR RefSeq; XP_006507323.1; XM_006507260.2. [P70352-3]
DR RefSeq; XP_006507326.1; XM_006507263.3. [P70352-4]
DR AlphaFoldDB; P70352; -.
DR SMR; P70352; -.
DR STRING; 10090.ENSMUSP00000102550; -.
DR GlyGen; P70352; 2 sites.
DR iPTMnet; P70352; -.
DR PhosphoSitePlus; P70352; -.
DR PaxDb; P70352; -.
DR PRIDE; P70352; -.
DR ProteomicsDB; 252771; -. [P70352-1]
DR ProteomicsDB; 252772; -. [P70352-2]
DR ProteomicsDB; 252773; -. [P70352-3]
DR Antibodypedia; 23345; 226 antibodies from 25 providers.
DR DNASU; 11875; -.
DR Ensembl; ENSMUST00000094128; ENSMUSP00000091678; ENSMUSG00000070424. [P70352-1]
DR Ensembl; ENSMUST00000106934; ENSMUSP00000102547; ENSMUSG00000070424. [P70352-3]
DR Ensembl; ENSMUST00000106935; ENSMUSP00000102548; ENSMUSG00000070424. [P70352-2]
DR Ensembl; ENSMUST00000106937; ENSMUSP00000102550; ENSMUSG00000070424. [P70352-1]
DR GeneID; 11875; -.
DR KEGG; mmu:11875; -.
DR UCSC; uc009iqp.2; mouse. [P70352-3]
DR UCSC; uc012fqt.1; mouse. [P70352-1]
DR CTD; 116969; -.
DR MGI; MGI:107948; Art5.
DR VEuPathDB; HostDB:ENSMUSG00000070424; -.
DR eggNOG; ENOG502SKQR; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_3_0_1; -.
DR InParanoid; P70352; -.
DR OMA; GDLHMKK; -.
DR PhylomeDB; P70352; -.
DR TreeFam; TF335356; -.
DR BRENDA; 2.4.2.31; 3474.
DR BioGRID-ORCS; 11875; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Art5; mouse.
DR PRO; PR:P70352; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70352; protein.
DR Bgee; ENSMUSG00000070424; Expressed in spermatid and 96 other tissues.
DR ExpressionAtlas; P70352; baseline and differential.
DR Genevisible; P70352; MM.
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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Membrane; NAD; NADP; Nucleotidyltransferase; Reference proteome; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..309
FT /note="Ecto-ADP-ribosyltransferase 5"
FT /id="PRO_0000019334"
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 DISULFID 43..259
FT /evidence="ECO:0000250"
FT VAR_SEQ 115..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003381"
FT VAR_SEQ 120..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003380"
FT VAR_SEQ 120..124
FT /note="GSREL -> VVCLP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003382"
FT VAR_SEQ 125..309
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003383"
FT CONFLICT 65..83
FT /note="LRESWEAAQEAWAHRRHKL -> PAPILGSSTRGLGTPASQA (in Ref.
FT 1; AAC52773)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="W -> S (in Ref. 1; AAC52773 and 2; CAC48193/
FT CAC50567)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="R -> H (in Ref. 1; AAC52773 and 2; CAC48193/
FT CAC50566/CAC50567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34333 MW; 847F80B5F221D049 CRC64;
MILEDLLMVL SCLSLHALWK VRAVPILPLS LVPDTFDDAY VGCSEEMEEK AGLLLKEEMA
RHALLRESWE AAQEAWAHRR HKLTLPPGFK AQHGVAIMVY TNSSNTLYWE LNQAVRTGGG
SRELYMRHFP FKALHFYLTR ALQLLRGSGG CSRGPGEVVF RGVGSLHFEP KRLGDSVRLG
QFTSSSVDER VARRFGNATF FNLRTCFGAP IQALSVFPEE REVLIPPHEV FLVTGFSQDG
AQSIVTLWSY DQTCSHFNCA YLGGEKRRGC VSSRAVGQPE APSTEALALQ SGKTLLLDPR
KLQLSRAGP
