NAR3_HUMAN
ID NAR3_HUMAN Reviewed; 389 AA.
AC Q13508; Q53XW3; Q6FHT7; Q8WVJ7; Q93069; Q96HL1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 181.
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; Synonyms=TMART;
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).
RC TISSUE=Testis;
RX PubMed=8605984; DOI=10.1016/0014-5793(96)00183-4;
RA Levy I., Wu Y.-Q., Roeckel N., Bulle F., Pawlak A., Siegrist S.,
RA Mattei M.-G., Guellaen G.;
RT "Human testis specifically expresses a homologue of the rodent T
RT lymphocytes RT6 mRNA.";
RL FEBS Lett. 382:276-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9119374; DOI=10.1006/geno.1996.4520;
RA Koch-Nolte F., Haag F., Braren R., Kuehl M., Hoovers J.,
RA Balasubramanian S., Bazan J.F., Thiele H.-G.;
RT "Two novel human members of an emerging mammalian gene family related to
RT mono-ADP-ribosylating bacterial toxins.";
RL Genomics 39:370-376(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-363.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-363.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP LEU-363.
RC TISSUE=Skeletal muscle;
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 [7]
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).
RN [8]
RP GLYCOSYLATION AT THR-346, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [9]
RP VARIANT SER-334.
RX PubMed=28718531; DOI=10.1111/andr.12378;
RA Nakamura S., Miyado M., Saito K., Katsumi M., Nakamura A., Kobori Y.,
RA Tanaka Y., Ishikawa H., Yoshida A., Okada H., Hata K., Nakabayashi K.,
RA Okamura K., Ogata H., Matsubara Y., Ogata T., Nakai H., Fukami M.;
RT "Next-generation sequencing for patients with non-obstructive azoospermia:
RT implications for significant roles of monogenic/oligogenic mutations.";
RL Andrology 5:824-831(2017).
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; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=3;
CC IsoId=Q13508-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q13508-2; Sequence=VSP_003375;
CC Name=2;
CC IsoId=Q13508-3; Sequence=VSP_003374;
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC {ECO:0000269|PubMed:22171320}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U47054; AAB01894.1; -; mRNA.
DR EMBL; X95827; CAA65096.1; -; Genomic_DNA.
DR EMBL; BT007249; AAP35913.1; -; mRNA.
DR EMBL; CR541664; CAG46465.1; -; mRNA.
DR EMBL; CH471057; EAX05765.1; -; Genomic_DNA.
DR EMBL; BC008397; AAH08397.1; -; mRNA.
DR EMBL; BC017913; AAH17913.1; -; mRNA.
DR CCDS; CCDS3575.1; -. [Q13508-3]
DR CCDS; CCDS47079.1; -. [Q13508-1]
DR CCDS; CCDS47080.1; -. [Q13508-2]
DR PIR; S62906; S62906.
DR RefSeq; NP_001123488.1; NM_001130016.2. [Q13508-1]
DR RefSeq; NP_001123489.1; NM_001130017.2. [Q13508-2]
DR RefSeq; NP_001170.2; NM_001179.5. [Q13508-3]
DR AlphaFoldDB; Q13508; -.
DR SMR; Q13508; -.
DR BioGRID; 106912; 28.
DR IntAct; Q13508; 2.
DR STRING; 9606.ENSP00000348064; -.
DR GlyConnect; 2924; 1 O-Linked glycan (1 site).
DR GlyConnect; 808; 2 N-Linked glycans (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; Q13508; 2 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; Q13508; -.
DR PhosphoSitePlus; Q13508; -.
DR BioMuta; ART3; -.
DR DMDM; 22261808; -.
DR jPOST; Q13508; -.
DR MassIVE; Q13508; -.
DR MaxQB; Q13508; -.
DR PaxDb; Q13508; -.
DR PeptideAtlas; Q13508; -.
DR PRIDE; Q13508; -.
DR ProteomicsDB; 59507; -. [Q13508-1]
DR ProteomicsDB; 59508; -. [Q13508-2]
DR ProteomicsDB; 59509; -. [Q13508-3]
DR Antibodypedia; 2182; 407 antibodies from 29 providers.
DR DNASU; 419; -.
DR Ensembl; ENST00000341029.9; ENSP00000343843.5; ENSG00000156219.17. [Q13508-2]
DR Ensembl; ENST00000349321.7; ENSP00000304313.5; ENSG00000156219.17. [Q13508-3]
DR Ensembl; ENST00000355810.9; ENSP00000348064.4; ENSG00000156219.17. [Q13508-1]
DR GeneID; 419; -.
DR KEGG; hsa:419; -.
DR MANE-Select; ENST00000355810.9; ENSP00000348064.4; NM_001130016.3; NP_001123488.1.
DR UCSC; uc003hjk.4; human. [Q13508-1]
DR CTD; 419; -.
DR DisGeNET; 419; -.
DR GeneCards; ART3; -.
DR HGNC; HGNC:725; ART3.
DR HPA; ENSG00000156219; Group enriched (heart muscle, skeletal muscle, testis, tongue).
DR MIM; 603086; gene.
DR neXtProt; NX_Q13508; -.
DR OpenTargets; ENSG00000156219; -.
DR PharmGKB; PA25016; -.
DR VEuPathDB; HostDB:ENSG00000156219; -.
DR eggNOG; ENOG502SHYX; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR HOGENOM; CLU_059744_3_1_1; -.
DR InParanoid; Q13508; -.
DR OMA; IYSFQFK; -.
DR PhylomeDB; Q13508; -.
DR TreeFam; TF335356; -.
DR PathwayCommons; Q13508; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q13508; -.
DR BioGRID-ORCS; 419; 12 hits in 1054 CRISPR screens.
DR ChiTaRS; ART3; human.
DR GeneWiki; ART3; -.
DR GenomeRNAi; 419; -.
DR Pharos; Q13508; Tbio.
DR PRO; PR:Q13508; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q13508; protein.
DR Bgee; ENSG00000156219; Expressed in gastrocnemius and 125 other tissues.
DR ExpressionAtlas; Q13508; baseline and differential.
DR Genevisible; Q13508; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 GO; GO:0006471; P:protein ADP-ribosylation; TAS:ProtInc.
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 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; Repeat; Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..362
FT /note="Ecto-ADP-ribosyltransferase 3"
FT /id="PRO_0000019325"
FT PROPEP 363..389
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019326"
FT DOMAIN 64..251
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT REPEAT 283..292
FT /note="1"
FT REPEAT 293..302
FT /note="2"
FT REPEAT 303..312
FT /note="3"
FT REGION 283..312
FT /note="3 X 10 AA tandem repeats of [GS]-E-K-N-[QW]-K-L-E-D-
FT H"
FT REGION 325..362
FT /note="Disordered"
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 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 362
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT DISULFID 43..256
FT /evidence="ECO:0000250"
FT VAR_SEQ 324..346
FT /note="GMKIPEPFPLPEDKSQGNINNPT -> A (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8605984"
FT /id="VSP_003375"
FT VAR_SEQ 324..334
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003374"
FT VARIANT 334
FT /note="P -> S (found in patients with non-obstructive
FT azoospermia; unknown pathological significance;
FT dbSNP:rs143599971)"
FT /evidence="ECO:0000269|PubMed:28718531"
FT /id="VAR_081146"
FT VARIANT 363
FT /note="S -> L (in dbSNP:rs1128864)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_060072"
FT CONFLICT 357
FT /note="S -> C (in Ref. 2; CAA65096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43923 MW; EE1311304BB2F41D CRC64;
MKTGHFEIVT MLLATMILVD IFQVKAEVLD MADNAFDDEY LKCTDRMEIK YVPQLLKEEK
ASHQQLDTVW ENAKAKWAAR KTQIFLPMNF KDNHGIALMA YISEAQEQTP FYHLFSEAVK
MAGQSREDYI YGFQFKAFHF YLTRALQLLR KPCEASSKTV VYRTSQGTSF TFGGLNQARF
GHFTLAYSAK PQAANDQLTV LSIYTCLGVD IENFLDKESE RITLIPLNEV FQVSQEGAGN
NLILQSINKT CSHYECAFLG GLKTENCIEN LEYFQPIYVY NPGEKNQKLE DHSEKNWKLE
DHGEKNQKLE DHGVKILEPT QIPGMKIPEP FPLPEDKSQG NINNPTPGPV PVPGPKSHPS
ASSGKLLLPQ FGMVIILISV SAINLFVAL
