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P52307 (5NTD_BOOMI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 79. 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:
Protein 5NUC

Including the following 2 domains:

  1. UDP-sugar hydrolase
    EC=3.6.1.45
    Alternative name(s):
    UDP-sugar diphosphatase
    UDP-sugar pyrophosphatase
  2. 5'-nucleotidase
    Short name=5'-NT
    EC=3.1.3.5
OrganismBoophilus microplus (Cattle tick)
Taxonomic identifier6941 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Chelicerata › Arachnida › Acari › Parasitiformes › Ixodida › Ixodoidea › Ixodidae › Rhipicephalinae › Rhipicephalus › Boophilus

Protein attributes

Sequence length580 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.

Catalytic activity

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.

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

Cofactor

Zinc.

Subunit structure

Homodimer.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor.

Tissue specificity

Gut, ovaries and salivary glands.

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 14›14 Ref.2
Chain15 – 555541Protein 5NUC
PRO_0000000021
Propeptide556 – 58025Removed in mature form Potential
PRO_0000000022

Regions

Region502 – 5087Substrate binding By similarity

Sites

Metal binding261Zinc 1 By similarity
Metal binding281Zinc 1 By similarity
Metal binding791Zinc 1 By similarity
Metal binding791Zinc 2 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding2121Zinc 2 By similarity
Metal binding2351Zinc 2 By similarity
Binding site4151Substrate By similarity
Site1121Transition state stabilizer By similarity
Site1151Transition state stabilizer By similarity

Amino acid modifications

Lipidation5551GPI-anchor amidated asparagine Potential
Glycosylation1721N-linked (GlcNAc...) Probable
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict151T → K AA sequence Ref.2
Sequence conflict37 – 393SGT → HXG AA sequence Ref.2
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P52307 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 588EEF2014071AB7

FASTA58063,460
        10         20         30         40         50         60 
GRLLACLLLP GLAATDFTAT VLHTNDVHGR FEQITASGTR CTKQAAEAQQ CVGGIARQKT 

        70         80         90        100        110        120 
VVSQAAASGA NVLFLNAGDY YQGSIWYYVL GAPIVAEAVN YLAHDAMALG NHEFDRGAEG 

       130        140        150        160        170        180 
LVPLLTESRV PIVGCNVDFS EEPTLKPLQP KPSVVVERAG IKIGLIGYTT MNTTYLSSPG 

       190        200        210        220        230        240 
KVRFTDEAEC IQREAQRLRR EEGVQVIIAV GHSGVPRDLE ICERVPEVSL VVGGHTHTFL 

       250        260        270        280        290        300 
YSGPTENGRV SGDKPQGPYP IVVDRAADSR CLVVQDFYMG KYMGNISITW NQRGEVVRWS 

       310        320        330        340        350        360 
GQPVLLDRSI PEDPDGIALL DRYRDRVAQS QASVVAESKV LLDGDKNRCR LDECNLGNLV 

       370        380        390        400        410        420 
MDAFLKKMAS LPSPQASWTR VAAVIANAGG IRASIDEQST GGRITFEDVV NVLPFGNTLV 

       430        440        450        460        470        480 
EMNVTGAQLK GLLEHGVHRH DVKGYVPPAE LVLAAGLRVV YDIQREPYDR VVEAHILCTE 

       490        500        510        520        530        540 
CRVPRYEPLE YARQYRIAAL SYIVHGGDNF DFSFVKPKDM YDTGFQDAEI VMKYMNSTSP 

       550        560        570        580 
ITTALDGRVT FLKTNQASDA CLNLASPFLV LLVLVVFYHL

« Hide

References

[1]"Cloning and expression of ecto 5-nucleotidase from the cattle tick Boophilus microplus."
Liyou N., Hamilton S., Elvin C., Willadsen P.
Insect Mol. Biol. 8:257-266(1999) [PubMed: 10380109] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli."
Willadsen P., Riding G.A., Jarmey J., Atkins A.
Insect Biochem. Mol. Biol. 23:291-295(1993) [PubMed: 8387372] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-40 AND 162-180.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U80634 mRNA. Translation: AAB38963.1.

3D structure databases

ProteinModelPortalP52307.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. False negative.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name5NTD_BOOMI
AccessionPrimary (citable) accession number: P52307
Secondary accession number(s): P90696
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: September 21, 2011
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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