NAR4_PANTR
ID NAR4_PANTR Reviewed; 314 AA.
AC Q95NE0;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 molecule 1;
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;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rios M., Reid M.;
RT "Pan troglodytes Dombrock glycoprotein (DO) gene exon 3.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF373017; AAK53821.1; -; Genomic_DNA.
DR EMBL; AF373016; AAK53821.1; JOINED; Genomic_DNA.
DR EMBL; AF374727; AAK53821.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q95NE0; -.
DR SMR; Q95NE0; -.
DR STRING; 9598.ENSPTRP00000054683; -.
DR PaxDb; Q95NE0; -.
DR PRIDE; Q95NE0; -.
DR eggNOG; ENOG502SKQR; Eukaryota.
DR InParanoid; Q95NE0; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW GPI-anchor; Lipoprotein; Membrane; NAD; NADP; Nucleotidyltransferase;
KW 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_0000019331"
FT PROPEP 286..314
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019332"
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"
SQ SEQUENCE 314 AA; 35862 MW; 1CD76A650B87A423 CRC64;
MGPLINRCKK ILLPTTVPPA TMRIWLLGGP 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
