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Q9CRA0 (NAR4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ecto-ADP-ribosyltransferase 4

EC=2.4.2.31
Alternative name(s):
ADP-ribosyltransferase C2 and C3 toxin-like 4
Short name=ARTC4
Mono(ADP-ribosyl)transferase 4
NAD(P)(+)--arginine ADP-ribosyltransferase 4
CD_antigen=CD297
Gene names
Name:Art4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

NAD+ + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Cell membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the Arg-specific ADP-ribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 264241Ecto-ADP-ribosyltransferase 4
PRO_0000416110
Propeptide265 – 30036Removed in mature form Potential
PRO_0000416111

Regions

Topological domain24 – 269246Extracellular Potential
Transmembrane270 – 28617Helical; Potential
Topological domain287 – 30014Cytoplasmic Potential

Sites

Active site2301 By similarity
Binding site1851NAD By similarity
Binding site2191NAD By similarity

Amino acid modifications

Lipidation2641GPI-anchor amidated alanine Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 259 By similarity
Disulfide bond161 ↔ 210 By similarity

Experimental info

Sequence conflict261T → A in CAD31119. Ref.1
Sequence conflict391D → N in CAD31119. Ref.1
Sequence conflict811L → R in CAD31119. Ref.1
Sequence conflict1741G → E in CAD31119. Ref.1
Sequence conflict1951E → G in CAA69608. Ref.1
Sequence conflict2771G → V in CAD31119. Ref.1
Sequence conflict2921A → E in CAD31119. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CRA0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0BB0B42D6AAC3406

FASTA30033,080
        10         20         30         40         50         60 
MALWLPGGQL TLLLLLWVQQ TPAGSTEAPL KVDVDLTPDS FDDQYQGCSE QMVEELNQGD 

        70         80         90        100        110        120 
YFIKEVDTHK YYSRAWQKAH LTWLNQAKAL PESMTPVHAV AIVVFTLNLN VSSDLAKAMA 

       130        140        150        160        170        180 
RAAGSPGQYS QSFHFKYLHY YLTSAIQLLR KDSSTKNGSL CYKVYHGMKD VSIGANVGST 

       190        200        210        220        230        240 
IRFGQFLSAS LLKEETRVSG NQTLFTIFTC LGASVQDFSL RKEVLIPPYE LFEVVSKSGS 

       250        260        270        280        290        300 
PKGDLINLRS AGNMSTYNCQ LLKACSKKCA PAPVVIGCLF LVTVVISSKS RAQRNLLAPF 

« Hide

References

« Hide 'large scale' references
[1]"The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse."
Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P., Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.
Protein Sci. 11:1657-1670(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver and Lung.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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].
Tissue: Olfactory epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ486881 Genomic DNA. Translation: CAD31119.1.
Y08300 Genomic DNA. Translation: CAA69608.1.
AK004744 mRNA. Translation: BAB23525.1.
AK019467 mRNA. Translation: BAB31738.1.
AC122804 Genomic DNA. No translation available.
BC046306 mRNA. Translation: AAH46306.1.
CCDSCCDS20658.1.
RefSeqNP_080915.1. NM_026639.2.
UniGeneMm.31840.

3D structure databases

ProteinModelPortalQ9CRA0.
SMRQ9CRA0. Positions 34-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000032341.

PTM databases

PhosphoSiteQ9CRA0.

Proteomic databases

PRIDEQ9CRA0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032341; ENSMUSP00000032341; ENSMUSG00000030217.
GeneID109978.
KEGGmmu:109978.
UCSCuc009emk.1. mouse.

Organism-specific databases

CTD420.
MGIMGI:1202710. Art4.

Phylogenomic databases

GeneTreeENSGT00530000062975.
HOGENOMHOG000273888.
HOVERGENHBG004464.
InParanoidQ9CRA0.
KOK06717.
OMAHSFHFKY.
OrthoDBEOG7D85WV.
PhylomeDBQ9CRA0.
TreeFamTF335356.

Gene expression databases

BgeeQ9CRA0.
GenevestigatorQ9CRA0.

Family and domain databases

InterProIPR000768. ART.
[Graphical view]
PANTHERPTHR10339. PTHR10339. 1 hit.
PfamPF01129. ART. 1 hit.
[Graphical view]
PRINTSPR00970. RIBTRNSFRASE.
PROSITEPS01291. ART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio363109.
PROQ9CRA0.
SOURCESearch...

Entry information

Entry nameNAR4_MOUSE
AccessionPrimary (citable) accession number: Q9CRA0
Secondary accession number(s): Q80VB5, Q80W56
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot