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Protein

5'-nucleotidase

Gene

Nt5e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.

Catalytic activityi

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

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Zinc 1By similarity
Metal bindingi40 – 401Zinc 1By similarity
Metal bindingi87 – 871Zinc 1By similarity
Metal bindingi87 – 871Zinc 2By similarity
Metal bindingi119 – 1191Zinc 2By similarity
Sitei120 – 1201Transition state stabilizerBy similarity
Sitei123 – 1231Transition state stabilizerBy similarity
Metal bindingi222 – 2221Zinc 2By similarity
Metal bindingi245 – 2451Zinc 2By similarity
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei356 – 3561SubstrateBy similarity
Binding sitei392 – 3921SubstrateBy similarity
Binding sitei397 – 3971SubstrateBy similarity
Binding sitei419 – 4191SubstrateBy similarity

GO - Molecular functioni

  • 5'-nucleotidase activity Source: MGI
  • ferrous iron binding Source: Ensembl
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • adenosine biosynthetic process Source: MGI
  • AMP catabolic process Source: MGI
  • brain development Source: Ensembl
  • leukocyte cell-cell adhesion Source: MGI
  • negative regulation of inflammatory response Source: MGI
  • positive regulation of lipid biosynthetic process Source: Ensembl
  • purine nucleotide biosynthetic process Source: Ensembl
  • response to aluminum ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-73621. Pyrimidine catabolism.
R-MMU-74259. Purine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Alternative name(s):
Ecto-5'-nucleotidase
CD_antigen: CD73
Gene namesi
Name:Nt5e
Synonyms:Nt5, Nte
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:99782. Nt5e.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • synaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Chaini29 – 5515235'-nucleotidasePRO_0000000017Add
BLAST
Propeptidei552 – 57625Removed in mature formBy similarityPRO_0000000018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 59By similarity
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi313 – 3131N-linked (GlcNAc...)1 Publication
Glycosylationi335 – 3351N-linked (GlcNAc...)1 Publication
Disulfide bondi355 ↔ 360By similarity
Disulfide bondi367 ↔ 389By similarity
Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi478 ↔ 481By similarity
Lipidationi551 – 5511GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiQ61503.
MaxQBiQ61503.
PaxDbiQ61503.
PeptideAtlasiQ61503.
PRIDEiQ61503.

PTM databases

iPTMnetiQ61503.
PhosphoSiteiQ61503.

Expressioni

Gene expression databases

BgeeiQ61503.
CleanExiMM_NT5E.
ExpressionAtlasiQ61503. baseline and differential.
GenevisibleiQ61503. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ61503. 3 interactions.
MINTiMINT-4086307.
STRINGi10090.ENSMUSP00000034992.

Structurei

3D structure databases

ProteinModelPortaliQ61503.
SMRiQ61503. Positions 29-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 5087Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4419. Eukaryota.
COG0737. LUCA.
GeneTreeiENSGT00530000063775.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
InParanoidiQ61503.
KOiK19970.
OMAiDIMNTMS.
OrthoDBiEOG7TF78T.
PhylomeDBiQ61503.
TreeFamiTF323589.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61503-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPAAAKVPK WLLLALSALL PQWPAASAWE LTILHTNDVH SRLEQTSDDS
60 70 80 90 100
TKCLNASLCV GGVARLFTKV QQIRKEEPNV LFLDAGDQYQ GTIWFTVYKG
110 120 130 140 150
LEVAHFMNIL GYDAMALGNH EFDNGVEGLI DPLLRNVKFP ILSANIKARG
160 170 180 190 200
PLAHQISGLF LPSKVLSVGG EVVGIVGYTS KETPFLSNPG TNLVFEDEIS
210 220 230 240 250
ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDI VVGGHSNTFL
260 270 280 290 300
YTGNPPSKEV PAGKYPFIVT ADDGRQVPVV QAYAFGKYLG YLKVEFDDKG
310 320 330 340 350
NVITSYGNPI LLNSSIPEDA TIKADINQWR IKLDNYSTQE LGRTIVYLDG
360 370 380 390 400
STQTCRFREC NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI
410 420 430 440 450
DEKNNGTITW ENLAAVLPFG GTFDLVQLKG STLKKAFEHS VHRYGQSTGE
460 470 480 490 500
FLQVGGIHVV YDINRKPWNR VVQLEVLCTK CRVPIYEPLE MDKVYKVTLP
510 520 530 540 550
SYLANGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVV YPAVEGRIKF
560 570
SAASHYQGSF PLVILSFWAM ILILYQ
Length:576
Mass (Da):63,864
Last modified:August 1, 1998 - v2
Checksum:i29D697928A5D5915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12059 mRNA. Translation: AAC13542.1.
AK028723 mRNA. Translation: BAC26084.1.
AK029979 mRNA. Translation: BAC26714.1.
AK154614 mRNA. Translation: BAE32714.1.
CCDSiCCDS23386.1.
PIRiJC2001.
RefSeqiNP_035981.1. NM_011851.4.
UniGeneiMm.244235.

Genome annotation databases

EnsembliENSMUST00000034992; ENSMUSP00000034992; ENSMUSG00000032420.
GeneIDi23959.
KEGGimmu:23959.
UCSCiuc009qyj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12059 mRNA. Translation: AAC13542.1.
AK028723 mRNA. Translation: BAC26084.1.
AK029979 mRNA. Translation: BAC26714.1.
AK154614 mRNA. Translation: BAE32714.1.
CCDSiCCDS23386.1.
PIRiJC2001.
RefSeqiNP_035981.1. NM_011851.4.
UniGeneiMm.244235.

3D structure databases

ProteinModelPortaliQ61503.
SMRiQ61503. Positions 29-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61503. 3 interactions.
MINTiMINT-4086307.
STRINGi10090.ENSMUSP00000034992.

PTM databases

iPTMnetiQ61503.
PhosphoSiteiQ61503.

Proteomic databases

EPDiQ61503.
MaxQBiQ61503.
PaxDbiQ61503.
PeptideAtlasiQ61503.
PRIDEiQ61503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034992; ENSMUSP00000034992; ENSMUSG00000032420.
GeneIDi23959.
KEGGimmu:23959.
UCSCiuc009qyj.2. mouse.

Organism-specific databases

CTDi4907.
MGIiMGI:99782. Nt5e.

Phylogenomic databases

eggNOGiKOG4419. Eukaryota.
COG0737. LUCA.
GeneTreeiENSGT00530000063775.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
InParanoidiQ61503.
KOiK19970.
OMAiDIMNTMS.
OrthoDBiEOG7TF78T.
PhylomeDBiQ61503.
TreeFamiTF323589.

Enzyme and pathway databases

ReactomeiR-MMU-73621. Pyrimidine catabolism.
R-MMU-74259. Purine catabolism.

Miscellaneous databases

PROiQ61503.
SOURCEiSearch...

Gene expression databases

BgeeiQ61503.
CleanExiMM_NT5E.
ExpressionAtlasiQ61503. baseline and differential.
GenevisibleiQ61503. MM.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Murine ecto-5'-nucleotidase (CD73): cDNA cloning and tissue distribution."
    Resta R., Hooker S.W., Hansen K.R., Laurent A.B., Park J.L., Blackburn M.R., Knudsen T.B., Thompson L.F.
    Gene 133:171-177(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Kidney.
  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.
    , 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 and NOD.
    Tissue: Skin and Testis.
  3. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313 AND ASN-335.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung and Testis.

Entry informationi

Entry namei5NTD_MOUSE
AccessioniPrimary (citable) accession number: Q61503
Secondary accession number(s): Q3U3S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.