Protein 5NUC precursor - Boophilus microplus (Cattle tick)

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

Last modified January 19, 2010. Version 72. History...

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

Names and origin

Protein names	Recommended name: Protein 5NUC Including the following 2 domains: 1- Recommended name: UDP-sugar hydrolase EC=3.6.1.45 Alternative name(s): UDP-sugar pyrophosphatase UDP-sugar diphosphatase 2- Recommended name: 5'-nucleotidase Short name=5'-NT EC=3.1.3.5
Organism	Boophilus microplus (Cattle tick)
Taxonomic identifier	6941 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Chelicerata › Arachnida › Acari › Parasitiformes › Ixodida › Ixodoidea › Ixodidae › Rhipicephalinae › Rhipicephalus › Boophilus

Protein attributes

Sequence length	580 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC UDP-sugar diphosphatase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

›14

Chain

541

Protein 5NUC

PRO_0000000021

Propeptide

25

Removed in mature form Potential

PRO_0000000022

Regions

Region

7

Substrate binding By similarity

Sites

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Binding site

1

Substrate By similarity

Site

1

Transition state stabilizer By similarity

Site

1

Transition state stabilizer By similarity

Amino acid modifications

Lipidation

1

GPI-anchor amidated asparagine Potential

Glycosylation

1

N-linked (GlcNAc...) Probable

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

T → K AA sequence Ref.2

Sequence conflict

3

SGT → HXG AA sequence Ref.2

Non-terminal residue

1

Sequences

Sequence

Length

Mass (Da)

Tools

P52307-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 588EEF2014071AB7
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580

63,460

        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

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
SMR	P52307. Positions 17-553.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.3.5. 280027. 3.6.1.45. 280027.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. False negative. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

5NTD_BOOMI

Accession

Primary (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:	January 19, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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