NAR4_HUMAN
ID NAR4_HUMAN Reviewed; 314 AA.
AC Q93070; Q9BZ50; Q9BZ51; Q9HB06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ecto-ADP-ribosyltransferase 4;
DE EC=2.4.2.31;
DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 4;
DE Short=ARTC4;
DE AltName: Full=Dombrock blood group carrier molecule;
DE AltName: Full=Mono(ADP-ribosyl)transferase 4;
DE AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 4;
DE AltName: CD_antigen=CD297;
DE Flags: Precursor;
GN Name=ART4; Synonyms=DO, DOK1;
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], POLYMORPHISM, AND VARIANT ASP-265.
RX PubMed=11001920;
RA Gubin A.N., Njoroge J.M., Wojda U., Pack S.D., Rios M., Reid M.E.,
RA Miller J.L.;
RT "Identification of the Dombrock blood group glycoprotein as a polymorphic
RT member of the ADP-ribosyltransferase gene family.";
RL Blood 96:2621-2627(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS VAL-108;
RP ILE-117; ASP-265 AND VAL-300.
RX PubMed=11896313; DOI=10.1046/j.1537-2995.2002.00004.x;
RA Rios M., Hue-Roye K., Oyen R., Miller J., Reid M.E.;
RT "Insights into the Holley- and Joseph- phenotypes.";
RL Transfusion 42:52-58(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-108; ILE-117; GLU-135;
RP MET-189; ASP-265 AND VAL-300.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-314.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-284, POLYMORPHISM, AND VARIANT
RP ASP-265.
RX PubMed=11520417; DOI=10.1046/j.1423-0410.2001.00052.x;
RA Wu G.-G., Jin S.-Z., Deng Z.-H., Zhao T.-M.;
RT "Polymerase chain reaction with sequence-specific primers-based genotyping
RT of the human Dombrock blood group DO1 and DO2 alleles and the DO gene
RT frequencies in Chinese blood donors.";
RL Vox Sang. 81:49-51(2001).
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).
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 -!- TISSUE SPECIFICITY: Expressed in spleen and T-cells.
CC -!- POLYMORPHISM: DO is responsible for the Dombrock blood group system
CC [MIM:616060]. The molecular basis of the Do(a)/Do(b) blood group
CC antigen is a single variation in position 265; Asn-265 corresponds to
CC Do(a) and Asp-265 to Do(b). It is also responsible for the antigens
CC Gregory [Gy(a)], Holley [Hy] and Joseph [Jo(a)].
CC {ECO:0000269|PubMed:11520417, ECO:0000269|PubMed:11896313}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=dombrock";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/do/";
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DR EMBL; AF290204; AAG17845.1; -; mRNA.
DR EMBL; AF382213; AAM21462.1; -; Genomic_DNA.
DR EMBL; AF382211; AAM21462.1; JOINED; Genomic_DNA.
DR EMBL; AF382212; AAM21462.1; JOINED; Genomic_DNA.
DR EMBL; AF382216; AAM21464.1; -; Genomic_DNA.
DR EMBL; AF382214; AAM21464.1; JOINED; Genomic_DNA.
DR EMBL; AF382215; AAM21464.1; JOINED; Genomic_DNA.
DR EMBL; AF382219; AAM21465.1; -; Genomic_DNA.
DR EMBL; AF382217; AAM21465.1; JOINED; Genomic_DNA.
DR EMBL; AF382218; AAM21465.1; JOINED; Genomic_DNA.
DR EMBL; AF382222; AAM21466.1; -; Genomic_DNA.
DR EMBL; AF382220; AAM21466.1; JOINED; Genomic_DNA.
DR EMBL; AF382221; AAM21466.1; JOINED; Genomic_DNA.
DR EMBL; AF382225; AAM21467.1; -; Genomic_DNA.
DR EMBL; AF382223; AAM21467.1; JOINED; Genomic_DNA.
DR EMBL; AF382224; AAM21467.1; JOINED; Genomic_DNA.
DR EMBL; AY899803; AAW65375.1; -; Genomic_DNA.
DR EMBL; BC074727; AAH74727.1; -; mRNA.
DR EMBL; X95826; CAA65095.1; -; Genomic_DNA.
DR EMBL; AF340233; AAK11274.1; -; Genomic_DNA.
DR EMBL; AF340234; AAK11275.1; -; Genomic_DNA.
DR CCDS; CCDS8668.1; -.
DR RefSeq; NP_066549.2; NM_021071.2.
DR AlphaFoldDB; Q93070; -.
DR SMR; Q93070; -.
DR BioGRID; 106913; 23.
DR IntAct; Q93070; 1.
DR STRING; 9606.ENSP00000228936; -.
DR GlyConnect; 1934; 17 N-Linked glycans (3 sites).
DR GlyGen; Q93070; 6 sites, 17 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q93070; -.
DR PhosphoSitePlus; Q93070; -.
DR BioMuta; ART4; -.
DR DMDM; 22261809; -.
DR jPOST; Q93070; -.
DR MassIVE; Q93070; -.
DR PaxDb; Q93070; -.
DR PeptideAtlas; Q93070; -.
DR PRIDE; Q93070; -.
DR ProteomicsDB; 75698; -.
DR Antibodypedia; 23686; 157 antibodies from 22 providers.
DR DNASU; 420; -.
DR Ensembl; ENST00000228936.6; ENSP00000228936.4; ENSG00000111339.12.
DR GeneID; 420; -.
DR KEGG; hsa:420; -.
DR UCSC; uc001rcl.2; human.
DR CTD; 420; -.
DR DisGeNET; 420; -.
DR GeneCards; ART4; -.
DR HGNC; HGNC:726; ART4.
DR HPA; ENSG00000111339; Group enriched (liver, lymphoid tissue).
DR MalaCards; ART4; -.
DR MIM; 110600; gene.
DR MIM; 616060; phenotype.
DR neXtProt; NX_Q93070; -.
DR PharmGKB; PA142672580; -.
DR VEuPathDB; HostDB:ENSG00000111339; -.
DR eggNOG; ENOG502SKQR; Eukaryota.
DR InParanoid; Q93070; -.
DR OrthoDB; 963174at2759; -.
DR PhylomeDB; Q93070; -.
DR TreeFam; TF335356; -.
DR PathwayCommons; Q93070; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q93070; -.
DR BioGRID-ORCS; 420; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; ART4; human.
DR GeneWiki; ART4; -.
DR GenomeRNAi; 420; -.
DR Pharos; Q93070; Tbio.
DR PRO; PR:Q93070; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q93070; protein.
DR Bgee; ENSG00000111339; Expressed in liver and 110 other tissues.
DR ExpressionAtlas; Q93070; baseline and differential.
DR Genevisible; Q93070; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; NAS: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; NAS:UniProtKB.
DR GO; GO:0006525; P:arginine metabolic process; NAS:UniProtKB.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
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 Blood group antigen; Cell membrane; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..285
FT /note="Ecto-ADP-ribosyltransferase 4"
FT /id="PRO_0000019329"
FT PROPEP 286..314
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019330"
FT DOMAIN 91..276
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 285
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..280
FT /evidence="ECO:0000250"
FT DISULFID 182..231
FT /evidence="ECO:0000250"
FT VARIANT 108
FT /note="G -> V (in Hy1 and Hy2; dbSNP:rs28362797)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013707"
FT VARIANT 117
FT /note="T -> I (in Jo(a); dbSNP:rs28362798)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013708"
FT VARIANT 135
FT /note="D -> E (in dbSNP:rs28362799)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022266"
FT VARIANT 189
FT /note="T -> M (in dbSNP:rs28362800)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022267"
FT VARIANT 265
FT /note="N -> D (in Do(b), Hy1 and Hy2; dbSNP:rs11276)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013709"
FT VARIANT 300
FT /note="L -> V (in Hy1; dbSNP:rs3088190)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013710"
FT CONFLICT 48
FT /note="E -> Q (in Ref. 5; CAA65095)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> S (in Ref. 5; CAA65095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35878 MW; 174913890C9D158F CRC64;
MGPLINRCKK ILLPTTVPPA TMRIWLLGGL LPFLLLLSGL QRPTEGSEVA IKIDFDFAPG
SFDDQYQGCS KQVMEKLTQG DYFTKDIEAQ KNYFRMWQKA HLAWLNQGKV LPQNMTTTHA
VAILFYTLNS NVHSDFTRAM ASVARTPQQY ERSFHFKYLH YYLTSAIQLL RKDSIMENGT
LCYEVHYRTK DVHFNAYTGA TIRFGQFLST SLLKEEAQEF GNQTLFTIFT CLGAPVQYFS
LKKEVLIPPY ELFKVINMSY HPRGNWLQLR STGNLSTYNC QLLKASSKKC IPDPIAIASL
SFLTSVIIFS KSRV
