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Reviewed, UniProtKB/Swiss-Prot P29240 (5NTD_DISOM)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    5'-nucleotidase
    EC=3.1.3.5
Alternative name(s):
    Ecto-nucleotidase
OrganismDiscopyge ommata (Electric ray)
Taxonomic identifier7785 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Narcinoidei › Narcinidae › Discopyge

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Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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 By similarity.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor.

Sequence similarities

Belongs to the 5'-nucleotidase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – 5525225'-nucleotidase
PRO_0000000024
Propeptide553 – 57725Removed in mature form
PRO_0000000025

Regions

Region500 – 5067Substrate binding By similarity

Sites

Metal binding391Zinc 1 By similarity
Metal binding411Zinc 1 By similarity
Metal binding861Zinc 1 By similarity
Metal binding861Zinc 2 By similarity
Metal binding1181Zinc 2 By similarity
Metal binding2211Zinc 2 By similarity
Metal binding2441Zinc 2 By similarity
Binding site4171Substrate By similarity
Site1191Transition state stabilizer By similarity
Site1221Transition state stabilizer By similarity

Amino acid modifications

Lipidation5521GPI-anchor amidated serine By similarity
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P29240-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 3B52535C2F70C0DB

FASTA57763,613
        10         20         30         40         50         60 
MPRVPSASAT GSSALLSLLC AFSLGRAAPF QLTILHTNDV HARVEETNQD SGKCFTQSFA 

        70         80         90        100        110        120 
GVARRWTKIE ELRARDKNVL LLDAGDQYQG TIWFNYYKGA EAAHFIEAVG YNAMALGNHE 

       130        140        150        160        170        180 
FDNGAEGLLD PFLLNVSFPV LSANLEQGED QVPSLIGYYK PSTVLDVNGE KIGVVGYTSK 

       190        200        210        220        230        240 
ETPTLSSPGP HLIFKDEIQA VQHEVDILVS QGIDKIIALG HSGFETDKLI AQKVRGVDVV 

       250        260        270        280        290        300 
VGGHSNTFLY TGKAPSNDVP VGPYPFLVNS DDQRTIPVVQ AYAYGKYLGY LKLTFDKGEV 

       310        320        330        340        350        360 
IKREGNPILL NSSIIQDPVL LAEVNKWKES LANFGKEVIG RTVVYLNGTT EECRNRECNM 

       370        380        390        400        410        420 
GNLICDAMIQ QNIRNPDEKF WNHVSICIFQ GGGIRAPINE QNNGTIQVDS LLAVLPFGST 

       430        440        450        460        470        480 
IDLLEVYGST LRAAFDHSVR RYGQNTGEFL QVSGIQVQFN LKRPPGSRVV KIDVLCADCR 

       490        500        510        520        530        540 
VPHYQPLLDN KIYKIVTNSY IAEGGDGFTM LKNERLRYDT GSTDISVVSS YIKQMKVVYP 

       550        560        570 
AVEGRILFVE NSATLPIINL KIGLSLFAFL TWFLHCS

« Hide

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References

[1]"5'-nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes."
Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., Zimmermann H.
Eur. J. Biochem. 202:855-861(1991) [PubMed: 1765099] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Electric lobe.

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Cross-references

Sequence databases

X62278 mRNA. Translation: CAA44168.1.
PIRS19564.

3D structure databases

HSSPHSSP built from PDB template 2USH based on UniProtKB P07024.
ModBaseSearch...

Phylogenomic databases

HOVERGENP29240.

Enzyme and pathway databases

BRENDA3.1.3.5. 290228.

Family and domain databases

InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase.
IPR004843. M-pesterase.
[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.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry name5NTD_DISOM
AccessionPrimary (citable) accession number: P29240
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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