NAR5_BOVIN
ID NAR5_BOVIN Reviewed; 316 AA.
AC Q0VC22;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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: Secreted {ECO:0000305}. Membrane {ECO:0000305}.
CC Note=Membrane-associated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC120389; AAI20390.1; -; mRNA.
DR RefSeq; NP_001069983.1; NM_001076515.1.
DR AlphaFoldDB; Q0VC22; -.
DR SMR; Q0VC22; -.
DR STRING; 9913.ENSBTAP00000039644; -.
DR PaxDb; Q0VC22; -.
DR PRIDE; Q0VC22; -.
DR GeneID; 618664; -.
DR KEGG; bta:618664; -.
DR eggNOG; ENOG502SKQR; Eukaryota.
DR InParanoid; Q0VC22; -.
DR OrthoDB; 963174at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Membrane; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..316
FT /note="Ecto-ADP-ribosyltransferase 5"
FT /id="PRO_0000379471"
FT DOMAIN 70..261
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..266
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 34894 MW; 7209F0A5540E33BF CRC64;
MIQATLLISL SCLSFYTLGS GVRRYDPGQG VTIQYLSLAP DTFDDAYVGC SEEMEEKAVL
LLEKEMANHT RLRESWETAQ KAWEQKRAGL TLPPGFRSQH GIAIMVYTNS SNTLYRELNQ
AVRTGGGSWE SYMKHFPFKA LHFYLTRALQ LLRGGGGCSR EPRQEVFRGV RRIHFVPKSV
GDSIRLGQFA SSSLDEAVAC GFGSATFFSL RTCSGAPIQA LSVFPEEREV LIPPYEVFVV
SNFSKDGNKS LMTLSSSDQM CSHFNCAYLG EKKRPSCEFV PIGGQGDSLS KGAFSLLSWK
TLLLASWGFQ LLGAGL