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P21588 (5NTD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5'-nucleotidase
Short name=5'-NT
EC=3.1.3.5
Alternative name(s):
Ecto-5'-nucleotidase
CD_antigen=CD73
Gene names
Name:Nt5e
Synonyms:Nt5, Nte
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.

Catalytic activity

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

Cofactor

Zinc.

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor Ref.2.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 5515235'-nucleotidase
PRO_0000000019
Propeptide552 – 57625Removed in mature form
PRO_0000000020

Regions

Region502 – 5087Substrate binding By similarity

Sites

Metal binding381Zinc 1 By similarity
Metal binding401Zinc 1 By similarity
Metal binding871Zinc 1 By similarity
Metal binding871Zinc 2 By similarity
Metal binding1191Zinc 2 By similarity
Metal binding2221Zinc 2 By similarity
Metal binding2451Zinc 2 By similarity
Binding site4191Substrate By similarity
Site1201Transition state stabilizer By similarity
Site1231Transition state stabilizer By similarity

Amino acid modifications

Lipidation5511GPI-anchor amidated serine Ref.2
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P21588 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 9EB75DD51E678AA6

FASTA57663,969
        10         20         30         40         50         60 
MRPAAATAPK WLLLALSALL PLWPTAKSWE LTIMHTNDVH SRLEQTSDDS TKCLNASLCV 

        70         80         90        100        110        120 
GGVARLFTKV QQIRKEEPNV LLLDAGDQYQ GTIWFTVYKG LEVAHFMNLL GYDAMALGNH 

       130        140        150        160        170        180 
EFDNGVEGLI DPLLRNVKFP ILSANIKARG PLAPQISGLY LPYKVLSVGG EVVGIVGYTS 

       190        200        210        220        230        240 
KETPFLSNPG TNLVFEDEVT ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDV 

       250        260        270        280        290        300 
VVGGHTNTFL YTGNPPSKEV PAGKYPFIVT SDDGRKVPVV QAYAFGKYLG YLKVEFDDKG 

       310        320        330        340        350        360 
NVVTSYGNPI LLNSTIREDA AIKADINQWR IKLDNYSTQE LGRTIVYLNG SAQECRFREC 

       370        380        390        400        410        420 
NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI DERNNGTITW ENLAAVLPFG 

       430        440        450        460        470        480 
GTFDLVQLKG STLKKAFEHS VHRYGQSTGE FLQVGGIHVV YDISRKPWDR VVQLKVLCTK 

       490        500        510        520        530        540 
CRVPIYEPLE MDKVYKVVLP SYLVNGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVI 

       550        560        570 
YPAVEGRIKF SAASHYQGSF PLIILSFWAV ILVLYQ

« Hide

References

[1]"Primary structure of rat liver 5'-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid."
Misumi Y., Ogata S., Hirose S., Ikehara Y.
J. Biol. Chem. 265:2178-2183(1990) [PubMed: 2298743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Membrane-anchoring domain of rat liver 5'-nucleotidase: identification of the COOH-terminal serine-523 covalently attached with a glycolipid."
Ogata S., Hayashi Y., Misumi Y., Ikehara Y.
Biochemistry 29:7923-7927(1990) [PubMed: 2148114] [Abstract]
Cited for: PROTEIN SEQUENCE OF 538-551, GPI-ANCHOR AT SER-551.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05214 mRNA. Translation: AAA40621.1.
IPIIPI00204348.
PIRA35036.
UniGeneRn.40132.

3D structure databases

ProteinModelPortalP21588.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21588.

Proteomic databases

PRIDEP21588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCNM_021576. rat.

Organism-specific databases

RGD61956. Nt5e.

Phylogenomic databases

eggNOGroNOG05845.
HOVERGENHBG000026.
InParanoidP21588.
OrthoDBEOG4TMR1Q.
PhylomeDBP21588.

Gene expression databases

ArrayExpressP21588.
GenevestigatorP21588.
GermOnlineENSRNOG00000011071. Rattus norvegicus.

Family and domain databases

InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Metallo_PEstase_dom.
[Graphical view]
Gene3DG3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHERPTHR11575. 5_nucleotidase. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. 5'-Nucleotdase_C. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name5NTD_RAT
AccessionPrimary (citable) accession number: P21588
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 19, 2011
This is version 102 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

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