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Q9Z0S1 (BPNT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:Bpnt1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

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.

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.

Sequence similarities

Belongs to the inositol monophosphatase family.

Ontologies

Keywords
   LigandLithium
Magnesium
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular function3'(2'),5'-bisphosphate nucleotidase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 3083073'(2'),5'-bisphosphate nucleotidase 1
PRO_0000142528

Regions

Region119 – 1224Substrate binding By similarity
Region195 – 1984Substrate binding By similarity

Sites

Metal binding741Magnesium 1 By similarity
Metal binding1171Magnesium 1 By similarity
Metal binding1171Magnesium 2 By similarity
Metal binding1191Magnesium 1; via carbonyl oxygen By similarity
Metal binding1201Magnesium 2 By similarity
Metal binding2471Magnesium 2 By similarity
Binding site741Substrate By similarity
Binding site2471Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict1641A → V in AAH11036. Ref.3
Sequence conflict1901H → R in AAH11036. Ref.3
Sequence conflict2761V → A in AAD17330. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z0S1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: D941FEA4C2E59E9D

FASTA30833,196
        10         20         30         40         50         60 
MASSHTVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRLVQMSICS 

        70         80         90        100        110        120 
SLARKFPKLT IIGEEDLPPG EVDQELIEDG QWEEILKQPC PSQYSAIKEE DLVVWVDPLD 

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

       190        200        210        220        230        240 
QLKEAPAGKH IITTTRSHSN QLVTDCISAM NPDTVLRVGG AGNKIIQLIE GKASAYVFAS 

       250        260        270        280        290        300 
PGCKKWDTCA PEVILHAVGG KLTDIHGNAL QYNKEVKHMN SAGVLAALRN YEYYASHVPE 


SVKNALIP

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate."
Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.
J. Biol. Chem. 274:13619-13628(1999) [PubMed: 10224133] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow and Stomach.
[3]"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: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF125043 mRNA. Translation: AAD17330.1.
AK008714 mRNA. Translation: BAB25850.1.
AK151931 mRNA. Translation: BAE30807.1.
AK152009 mRNA. Translation: BAE30872.1.
BC011036 mRNA. Translation: AAH11036.1.
IPIIPI00318545.
RefSeqNP_035924.2. NM_011794.3.
UniGeneMm.227549.

3D structure databases

ProteinModelPortalQ9Z0S1.
SMRQ9Z0S1. Positions 5-308.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Z0S1.

PTM databases

PhosphoSiteQ9Z0S1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z0S1.

Proteomic databases

PRIDEQ9Z0S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027916; ENSMUSP00000027916; ENSMUSG00000026617.
GeneID23827.
KEGGmmu:23827.
UCSCuc007dzc.1. mouse.

Organism-specific databases

CTD10380.
MGIMGI:1338800. Bpnt1.

Phylogenomic databases

GeneTreeENSGT00530000063462.
HOGENOMHBG380847.
HOVERGENHBG050719.
InParanoidQ9Z0S1.
OMAAHAYVFA.
OrthoDBEOG4GXFND.
PhylomeDBQ9Z0S1.

Gene expression databases

ArrayExpressQ9Z0S1.
BgeeQ9Z0S1.
CleanExMM_BPNT1.
GenevestigatorQ9Z0S1.
GermOnlineENSMUSG00000026617. Mus musculus.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
KOK01082.
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303481.
SOURCESearch...

Entry information

Entry nameBPNT1_MOUSE
AccessionPrimary (citable) accession number: Q9Z0S1
Secondary accession number(s): Q3U8Z5, Q91XB9, Q9D7Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 16, 2011
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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