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Reviewed, UniProtKB/Swiss-Prot Q3V1L4 (5NTC_MOUSE)

Last modified June 16, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cytosolic purine 5'-nucleotidase
    EC=3.1.3.5
Alternative name(s):
    5'-nucleotidase cytosolic II
Gene names
Name: Nt5c2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides By similarity.

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Allosterically activated by various compounds, including ATP By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 5'(3')-deoxyribonucleotidase family.

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Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function5'-nucleotidase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 560560Cytosolic purine 5'-nucleotidase
PRO_0000310264

Regions

Region202 – 2109Substrate binding Potential
Compositional bias549 – 56012Asp/Glu-rich (acidic)

Sites

Active site521Nucleophile By similarity
Active site541Proton donor By similarity
Metal binding521Magnesium By similarity
Metal binding541Magnesium; via carbonyl oxygen By similarity
Metal binding3511Magnesium By similarity
Binding site1271Allosteric activator 1 By similarity
Binding site1541Allosteric activator 2 By similarity
Binding site3541Allosteric activator 2 By similarity
Binding site4361Allosteric activator 1; via carbonyl oxygen By similarity
Binding site4531Allosteric activator 2 By similarity

Amino acid modifications

Modified residue5021Phosphoserine By similarity
Modified residue5271Phosphoserine Ref.3

Experimental info

Sequence conflict891F → Y in BAE21136. Ref.1
Sequence conflict2171K → R in BAC29555. Ref.1
Sequence conflict5311I → V in AAH64760. Ref.2
Sequence conflict5351N → D in AAH64760. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q3V1L4-1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: BC1EBB45E6E1F357

FASTA56064,809
        10         20         30         40         50         60 
MTTSWSDRLQ NAADVPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

        70         80         90        100        110        120 
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV 

       130        140        150        160        170        180 
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS 

       190        200        210        220        230        240 
CDTGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK 

       250        260        270        280        290        300 
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 

       310        320        330        340        350        360 
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS 

       370        380        390        400        410        420 
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ 

       430        440        450        460        470        480 
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA 

       490        500        510        520        530        540 
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA 

       550        560 
PQEITHCHDE DDDEEEEEEE

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References

[1]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone, Head, Small intestine and Thymus.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, MASS SPECTROMETRY.
Tissue: Liver.

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Cross-references

Sequence databases

AK008045 mRNA. Translation: BAB25428.1.
AK036730 mRNA. Translation: BAC29555.1.
AK132384 mRNA. Translation: BAE21136.1.
AK147901 mRNA. Translation: BAE28216.1.
AK169616 mRNA. Translation: BAE41263.1.
BC064760 mRNA. Translation: AAH64760.1.
IPIIPI00111489.
RefSeqNP_084086.2.
UniGeneMm.248652

3D structure databases

SMRQ3V1L4. Positions 3-488.
ModBaseSearch...

PTM databases

PhosphoSiteQ3V1L4.

Proteomic databases

PRIDEQ3V1L4.

Genome annotation databases

EnsemblENSMUSG00000025041. Mus musculus. [Contig view]
GeneID76952.
KEGGmmu:76952.

Organism-specific databases

MGIMGI:2178563. Nt5c2.

Phylogenomic databases

HOGENOMQ3V1L4.
HOVERGENQ3V1L4.
OMAQ3V1L4. IGAKGKD.

Enzyme and pathway databases

BRENDA3.1.3.5. 244.

Gene expression databases

ArrayExpressQ3V1L4.
BgeeQ3V1L4.
CleanExMM_NT5C2.

Family and domain databases

InterProIPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]
PANTHERPTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.
PfamPF05761. 5_nucleotid. 1 hit.
[Graphical view]
PIRSFPIRSF017434. Purine_5'-nucleotidase. 1 hit.
TIGRFAMsTIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNetSearch...

Other Resources

NextBio346159.
SOURCESearch...

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Entry information

Entry name5NTC_MOUSE
AccessionPrimary (citable) accession number: Q3V1L4
Secondary accession number(s): Q6P223, Q8BZ43, Q9D8G6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: June 16, 2009
This is version 33 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents