NAR5_HUMAN
ID NAR5_HUMAN Reviewed; 291 AA.
AC Q96L15; C9IYG7; Q6UX84; Q86W02;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 157.
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; ORFNames=UNQ575/PRO1137;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-24 INS.
RC TISSUE=Testis;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-24 INS.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-24 INS.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-24 INS.
RC TISSUE=Liver;
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 [6]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(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: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96L15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96L15-2; Sequence=VSP_013145, VSP_013146;
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Y16835; CAC79987.1; -; mRNA.
DR EMBL; AY358466; AAQ88831.1; -; mRNA.
DR EMBL; AC060812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02556.1; -; Genomic_DNA.
DR EMBL; BC014577; AAH14577.1; -; mRNA.
DR CCDS; CCDS73242.1; -. [Q96L15-2]
DR CCDS; CCDS7743.1; -. [Q96L15-1]
DR RefSeq; NP_001073004.1; NM_001079536.1. [Q96L15-1]
DR RefSeq; NP_001284597.1; NM_001297668.1. [Q96L15-2]
DR RefSeq; NP_443750.2; NM_053017.4. [Q96L15-1]
DR AlphaFoldDB; Q96L15; -.
DR SMR; Q96L15; -.
DR BioGRID; 125545; 91.
DR IntAct; Q96L15; 1.
DR STRING; 9606.ENSP00000380258; -.
DR GlyGen; Q96L15; 3 sites.
DR iPTMnet; Q96L15; -.
DR PhosphoSitePlus; Q96L15; -.
DR BioMuta; ART5; -.
DR DMDM; 296439487; -.
DR EPD; Q96L15; -.
DR MassIVE; Q96L15; -.
DR MaxQB; Q96L15; -.
DR PaxDb; Q96L15; -.
DR PeptideAtlas; Q96L15; -.
DR PRIDE; Q96L15; -.
DR Antibodypedia; 23345; 226 antibodies from 25 providers.
DR DNASU; 116969; -.
DR Ensembl; ENST00000359918.8; ENSP00000352992.4; ENSG00000167311.14. [Q96L15-1]
DR Ensembl; ENST00000397067.7; ENSP00000380257.3; ENSG00000167311.14. [Q96L15-2]
DR Ensembl; ENST00000397068.8; ENSP00000380258.3; ENSG00000167311.14. [Q96L15-1]
DR GeneID; 116969; -.
DR KEGG; hsa:116969; -.
DR MANE-Select; ENST00000397068.8; ENSP00000380258.3; NM_053017.5; NP_443750.2.
DR UCSC; uc001lyb.2; human. [Q96L15-1]
DR CTD; 116969; -.
DR DisGeNET; 116969; -.
DR GeneCards; ART5; -.
DR HGNC; HGNC:24049; ART5.
DR HPA; ENSG00000167311; Tissue enhanced (skeletal muscle, testis).
DR MIM; 610625; gene.
DR neXtProt; NX_Q96L15; -.
DR OpenTargets; ENSG00000167311; -.
DR PharmGKB; PA134887713; -.
DR VEuPathDB; HostDB:ENSG00000167311; -.
DR eggNOG; ENOG502SKQR; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_3_2_1; -.
DR InParanoid; Q96L15; -.
DR OMA; GDLHMKK; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; Q96L15; -.
DR TreeFam; TF335356; -.
DR PathwayCommons; Q96L15; -.
DR SignaLink; Q96L15; -.
DR BioGRID-ORCS; 116969; 18 hits in 1066 CRISPR screens.
DR ChiTaRS; ART5; human.
DR GenomeRNAi; 116969; -.
DR Pharos; Q96L15; Tbio.
DR PRO; PR:Q96L15; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96L15; protein.
DR Bgee; ENSG00000167311; Expressed in left testis and 99 other tissues.
DR ExpressionAtlas; Q96L15; baseline and differential.
DR Genevisible; Q96L15; HS.
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 NAD; NADP; Nucleotidyltransferase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..291
FT /note="Ecto-ADP-ribosyltransferase 5"
FT /id="PRO_0000019333"
FT DOMAIN 62..252
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..258
FT /evidence="ECO:0000250"
FT VAR_SEQ 195..262
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013145"
FT VAR_SEQ 275..291
FT /note="ALGTGDLHMTKRHLQQP -> VQLGSQSEGASSLPPWKTLLLAPGEFQLSGV
FT GP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013146"
FT VARIANT 24
FT /note="P -> PT (in dbSNP:rs72515796)"
FT /evidence="ECO:0000269|PubMed:12070318,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_063143"
FT CONFLICT 43
FT /note="A -> V (in Ref. 5; AAH14577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32054 MW; 9783A0473FB4613E CRC64;
MALAALMIAL GSLGLHTWQA QAVPILPLGL APDTFDDTYV GCAEEMEEKA APLLKEEMAH
HALLRESWEA AQETWEDKRR GLTLPPGFKA QNGIAIMVYT NSSNTLYWEL NQAVRTGGGS
RELYMRHFPF KALHFYLIRA LQLLRGSGGC SRGPGEVVFR GVGSLRFEPK RLGDSVRLGQ
FASSSLDKAV AHRFGNATLF SLTTCFGAPI QAFSVFPKER EVLIPPHEVF LVTRFSQDGA
QSLVTLWSYN QTCSHFNCAY LGGEKRRGCV SAPGALGTGD LHMTKRHLQQ P
