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Reviewed, UniProtKB/Swiss-Prot Q9Z1N4 (BPNT1_RAT)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    3'(2'),5'-bisphosphate nucleotidase 1
    EC=3.1.3.7
Alternative name(s):
    Bisphosphate 3'-nucleotidase 1
    PAP-inositol-1,4-phosphatase
      Short name=PIP
    scHAL2 analogous 3
Gene names
Name: Bpnt1
Synonyms: Sal3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins1P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. Ref.1

Catalytic activity

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

Cofactor

Magnesium.

Enzyme regulation

Uncompetitive inhibition by micromolar concentrations of lithium. Competitive inhibition by inositol 1,4-bisphosphate. Inhibited by calcium ions. Ref.1

Tissue specificity

Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Ref.1

Sequence similarities

Belongs to the inositol monophosphatase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 3083073'(2'),5'-bisphosphate nucleotidase 1
PRO_0000142529

Regions

Region195 – 1984Substrate binding

Sites

Metal binding741Magnesium 1
Metal binding1171Magnesium 1
Metal binding1171Magnesium 2
Metal binding1191Magnesium 1; via carbonyl oxygen
Metal binding1201Magnesium 2
Metal binding2471Magnesium 2

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Secondary structure

1 ..................................................... 308
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9Z1N4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 478C375057E88EC9

FASTA30833,174
        10         20         30         40         50         60 
MASSHNVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRMVQMSICS 

        70         80         90        100        110        120 
SLSRKFPKLT IIGEEDLPPG EVDQELIEDG QSEEILKQPC PSQYSAIKEE DLVVWVDPVD 

       130        140        150        160        170        180 
GTKEYTEGLL DNVTVLIGIA YEGKAIAGII NQPYYNYQAG PDAVLGRTIW GVLGLGAFGF 

       190        200        210        220        230        240 
QLKEAPAGKH IITTTRSHSN KLVTDCIAAM NPDNVLRVGG AGNKIIQLIE GKASAYVFAS 

       250        260        270        280        290        300 
PGCKKWDTCA PEVILHAVGG KLTDIHGNPL QYDKEVKHMN SAGVLAALRN YEYYASRVPE 


SVKSALIP

« Hide

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References

« Hide 'large scale' references
[1]"A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase."
Lopez-Coronado J.M., Belles J.M., Lesage F., Serrano R., Rodriguez P.L.
J. Biol. Chem. 274:16034-16039(1999) [PubMed: 10347153] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Heart.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[3]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 28-40; 145-167; 202-217; 225-232; 262-274 AND 278-297, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[4]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[5]"Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy."
Patel S., Yenush L., Rodriguez P.L., Serrano R., Blundell T.L.
J. Mol. Biol. 315:677-685(2002) [PubMed: 11812139] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 5-308.

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Cross-references

Sequence databases

AJ000347 mRNA. Translation: CAA04022.1.
BC085692 mRNA. Translation: AAH85692.1.
IPIIPI00209042.
RefSeqNP_741987.1.
UniGeneRn.8453

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JP4X-ray1.69A1-308[»]
ModBaseSearch...

Proteomic databases

PRIDEQ9Z1N4.

Genome annotation databases

EnsemblENSRNOG00000002378. Rattus norvegicus. [Contig view]
GeneID64473.
KEGGrno:64473.

Organism-specific databases

RGD621833. Bpnt1.

Phylogenomic databases

HOVERGENQ9Z1N4.

Enzyme and pathway databases

BRENDA3.1.3.57. 248.
3.1.3.7. 248.

Gene expression databases

ArrayExpressQ9Z1N4.
GermOnlineENSRNOG00000002378. Rattus norvegicus.

Family and domain databases

InterProIPR000760. Inositol_P.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00378. INOSPHPHTASE.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.
NextBio613262.

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Entry information

Entry nameBPNT1_RAT
AccessionPrimary (citable) accession number: Q9Z1N4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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