GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 precursor

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P52961 (NAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
EC=2.4.2.31

Alternative name(s):
ADP-ribosyltransferase C2 and C3 toxin-like 1
Short name=ARTC1
Mono(ADP-ribosyl)transferase 1
CD_antigen=CD296

Gene names

Name:

ART1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Has ADP-ribosyltransferase activity toward GLP1R. Ref.6
Catalytic activity	NAD⁺ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine. NADP⁺ + protein-L-arginine = nicotinamide + N(omega)-((2'-phospho-ADP)-D-ribosyl)-protein-L-arginine.
Subcellular location	Sarcoplasmic reticulum membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the Arg-specific ADP-ribosyltransferase family.

Ontologies

Keywords
Cellular component	Membrane Sarcoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	NAD NADP
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	innate immune response Traceable author statement. Source: Reactome protein ADP-ribosylation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc sarcoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NAD(P)+-protein-arginine ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC NAD+ ADP-ribosyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 295

273

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1

PRO_0000019311

Propeptide

296 – 327

Removed in mature form Potential

PRO_0000019312

Sites

Active site

247

By similarity

Binding site

121

NAD By similarity

Binding site

179

NAD By similarity

Binding site

233

NAD By similarity

Amino acid modifications

Lipidation

295

GPI-anchor amidated serine Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

253

N-linked (GlcNAc...) Potential

Disulfide bond

53 ↔ 277

By similarity

Disulfide bond

174 ↔ 224

By similarity

Natural variations

Natural variant

105

P → L.
Corresponds to variant rs35123761 [ dbSNP | Ensembl ].

VAR_034125

Natural variant

126

P → R.
Corresponds to variant rs35619488 [ dbSNP | Ensembl ].

VAR_034126

Natural variant

257

L → P. Ref.1
Corresponds to variant rs2280134 [ dbSNP | Ensembl ].

VAR_053526

Sequences

Sequence

Length

Mass (Da)

Tools

P52961 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 8FDC568197031EA5
Show »

FASTA

327

36,335

        10         20         30         40         50         60 
MQMPAMMSLL LVSVGLMEAL QAQSHPITRR DLFSQEIQLD MALASFDDQY AGCAAAMTAA 

        70         80         90        100        110        120 
LPDLNHTEFQ ANQVYADSWT LASSQWQERQ ARWPEWSLSP TRPSPPPLGF RDEHGVALLA 

       130        140        150        160        170        180 
YTANSPLHKE FNAAVREAGR SRAHYLHHFS FKTLHFLLTE ALQLLGSGQR PPRCHQVFRG 

       190        200        210        220        230        240 
VHGLRFRPAG PRATVRLGGF ASASLKHVAA QQFGEDTFFG IWTCLGAPIK GYSFFPGEEE 

       250        260        270        280        290        300 
VLIPPFETFQ VINASRLAQG PARIYLRALG KHSTYNCEYI KDKKCKSGPC HLDNSAMGQS 

       310        320 
PLSAVWSLLL LLWFLVVRAF PDGPGLL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases." Okazaki I.J., Zolkiewska A., Nightingale M.S., Moss J. Biochemistry 33:12828-12836(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-257. Tissue: Skeletal muscle.
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Conservation of the ART gene family across mammalian species." Kuehl M., Glowacki G., Haag F., Koch-Nolte F. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-223.
[5]	"Toward a unified nomenclature for mammalian ADP-ribosyltransferases." Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F. Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[6]	"Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase." Dezelak M., Bavec A. Mol. Biol. Rep. 39:4375-4381(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S74683 mRNA. Translation: AAB32387.1. CH471158 Genomic DNA. Translation: EAX02559.1. BC069102 mRNA. Translation: AAH69102.1. BC111729 mRNA. Translation: AAI11730.1. AJ291430 mRNA. Translation: CAC69964.1.
IPI	IPI00006067.
PIR	A55966.
RefSeq	NP_004305.2. NM_004314.2.
UniGene	Hs.382188.
3D structure databases
ProteinModelPortal	P52961.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000250693.
PTM databases
PhosphoSite	P52961.
Polymorphism databases
DMDM	206729882.
Proteomic databases
PaxDb	P52961.
PRIDE	P52961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250693; ENSP00000250693; ENSG00000129744.
GeneID	417.
KEGG	hsa:417.
UCSC	uc001lye.1. human.
Organism-specific databases
CTD	417.
GeneCards	GC11P003666.
H-InvDB	HIX0035913.
HGNC	HGNC:723. ART1.
HPA	HPA051148.
MIM	601625. gene.
neXtProt	NX_P52961.
PharmGKB	PA25014.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG40339.
HOGENOM	HOG000273888.
HOVERGEN	HBG004464.
InParanoid	P52961.
KO	K06716.
OMA	CLGAPIK.
OrthoDB	EOG4G4GQW.
PhylomeDB	P52961.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
Bgee	P52961.
CleanEx	HS_ART1.
Genevestigator	P52961.
GermOnline	ENSG00000129744. Homo sapiens.
Family and domain databases
InterPro	IPR000768. ART. [Graphical view]
PANTHER	PTHR10339. PTHR10339. 1 hit.
Pfam	PF01129. ART. 1 hit. [Graphical view]
PRINTS	PR00970. RIBTRNSFRASE.
PROSITE	PS01291. ART. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2158.
DrugBank	DB00102. Becaplermin.
GenomeRNAi	417.
NextBio	1763.
SOURCE	Search...

Entry information

Entry name

NAR1_HUMAN

Accession

Primary (citable) accession number: P52961
Secondary accession number(s): Q6NTD2, Q96KT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents