NAR1_RABIT
ID NAR1_RABIT Reviewed; 327 AA.
AC Q03515;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1;
DE EC=2.4.2.31;
DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 1;
DE Short=ARTC1;
DE AltName: Full=Mono(ADP-ribosyl)transferase 1;
DE AltName: CD_antigen=CD296;
DE Flags: Precursor;
GN Name=ART1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=1454819; DOI=10.1073/pnas.89.23.11352;
RA Zolkiewska A., Nightingale M.S., Moss J.;
RT "Molecular characterization of NAD:arginine ADP-ribosyltransferase from
RT rabbit skeletal muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11352-11356(1992).
CC -!- FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R.
CC {ECO:0000250}.
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: Sarcoplasmic reticulum membrane; Lipid-anchor,
CC GPI-anchor.
CC -!- TISSUE SPECIFICITY: Primarily in skeletal and cardiac muscle.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M98764; AAA31418.1; -; mRNA.
DR PIR; A47239; A47239.
DR RefSeq; NP_001076139.1; NM_001082670.1.
DR AlphaFoldDB; Q03515; -.
DR SMR; Q03515; -.
DR STRING; 9986.ENSOCUP00000018587; -.
DR Ensembl; ENSOCUT00000021884; ENSOCUP00000018587; ENSOCUG00000022791.
DR GeneID; 100009387; -.
DR KEGG; ocu:100009387; -.
DR CTD; 417; -.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR GeneTree; ENSGT01030000234601; -.
DR InParanoid; Q03515; -.
DR OrthoDB; 963174at2759; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000022791; Expressed in skeletal muscle tissue and 6 other tissues.
DR ExpressionAtlas; Q03515; baseline.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP;
KW Nucleotidyltransferase; Reference proteome; Sarcoplasmic reticulum; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..295
FT /note="GPI-linked NAD(P)(+)--arginine ADP-
FT ribosyltransferase 1"
FT /id="PRO_0000019315"
FT PROPEP 296..327
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019316"
FT DOMAIN 73..273
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT LIPID 295
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..277
FT /evidence="ECO:0000250"
FT DISULFID 174..224
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 36134 MW; 3D2E4E005264A187 CRC64;
MWVPAVANLL LLSLGLLEAI QAQSHLVTRR DLFSQETPLD MAPASFDDQY VGCAAAMTAA
LPHLNLTEFQ VNKVYADGWA LASSQWRERS AWGPEWGLST TRLPPPPAGF RDEHGVALLA
YTANSPLHKE FNAAVRQAGR SRAHYLQHFS FKTLHFLLTE ALQLLGRDQR MPRCRQVFRG
VHGLRFRPAG PGTTVRLGGF ASASLKNVAA QQFGEDTFFG IWTCLGVPIQ GYSFFPGEEE
VLIPPFETFQ VINASRPAQG PARIYLKALG KRSSYNCEYI KEMQCKSRPC HLDNSASAQE
RLSTAWSLLL LLAFLAVGPF PGSPGLF
