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Protein

3'(2'),5'-bisphosphate nucleotidase 1

Gene

Bpnt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 InsP6.1 Publication

Catalytic activityi

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

Cofactori

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi74Magnesium 11 Publication1
Binding sitei74SubstrateBy similarity1
Metal bindingi117Magnesium 11 Publication1
Metal bindingi117Magnesium 21 Publication1
Metal bindingi119Magnesium 1; via carbonyl oxygen1 Publication1
Metal bindingi120Magnesium 21 Publication1
Binding sitei242Substrate; via carbonyl oxygen1
Metal bindingi247Magnesium 21 Publication1
Binding sitei247Substrate1

GO - Molecular functioni

  • 3'(2'),5'-bisphosphate nucleotidase activity Source: RGD
  • inositol-1,4-bisphosphate 1-phosphatase activity Source: RGD
  • magnesium ion binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.57. 5301.
ReactomeiR-RNO-156584. Cytosolic sulfonation of small molecules.
SABIO-RKQ9Z1N4.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Bpnt1
Synonyms:Sal3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi621833. Bpnt1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001425292 – 3083'(2'),5'-bisphosphate nucleotidase 1Add BLAST307

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei122PhosphothreonineBy similarity1
Modified residuei240PhosphoserineBy similarity1
Modified residuei244N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z1N4.
PRIDEiQ9Z1N4.

PTM databases

iPTMnetiQ9Z1N4.
PhosphoSitePlusiQ9Z1N4.
SwissPalmiQ9Z1N4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000002378.
ExpressionAtlasiQ9Z1N4. baseline and differential.
GenevisibleiQ9Z1N4. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003249.

Structurei

Secondary structure

1308
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 32Combined sources26
Beta strandi38 – 42Combined sources5
Beta strandi45 – 47Combined sources3
Helixi49 – 65Combined sources17
Beta strandi69 – 75Combined sources7
Helixi84 – 86Combined sources3
Helixi93 – 96Combined sources4
Helixi102 – 104Combined sources3
Helixi109 – 111Combined sources3
Beta strandi112 – 120Combined sources9
Helixi122 – 126Combined sources5
Helixi130 – 132Combined sources3
Beta strandi134 – 141Combined sources8
Beta strandi144 – 152Combined sources9
Turni153 – 158Combined sources6
Beta strandi167 – 172Combined sources6
Turni173 – 175Combined sources3
Beta strandi176 – 180Combined sources5
Beta strandi191 – 198Combined sources8
Helixi201 – 208Combined sources8
Beta strandi213 – 219Combined sources7
Helixi221 – 229Combined sources9
Beta strandi234 – 238Combined sources5
Helixi245 – 257Combined sources13
Beta strandi261 – 263Combined sources3
Beta strandi284 – 289Combined sources6
Helixi291 – 297Combined sources7
Helixi300 – 305Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JP4X-ray1.69A1-308[»]
ProteinModelPortaliQ9Z1N4.
SMRiQ9Z1N4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z1N4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni119 – 122Substrate binding4
Regioni195 – 198Substrate binding4
Regioni220 – 224Substrate5

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG3099. Eukaryota.
ENOG410XNMV. LUCA.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000293205.
HOVERGENiHBG050719.
InParanoidiQ9Z1N4.
KOiK01082.
PhylomeDBiQ9Z1N4.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z1N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSHNVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA
60 70 80 90 100
DRMVQMSICS SLSRKFPKLT IIGEEDLPPG EVDQELIEDG QSEEILKQPC
110 120 130 140 150
PSQYSAIKEE DLVVWVDPVD GTKEYTEGLL DNVTVLIGIA YEGKAIAGII
160 170 180 190 200
NQPYYNYQAG PDAVLGRTIW GVLGLGAFGF QLKEAPAGKH IITTTRSHSN
210 220 230 240 250
KLVTDCIAAM NPDNVLRVGG AGNKIIQLIE GKASAYVFAS PGCKKWDTCA
260 270 280 290 300
PEVILHAVGG KLTDIHGNPL QYDKEVKHMN SAGVLAALRN YEYYASRVPE

SVKSALIP
Length:308
Mass (Da):33,174
Last modified:May 1, 1999 - v1
Checksum:i478C375057E88EC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000347 mRNA. Translation: CAA04022.1.
BC085692 mRNA. Translation: AAH85692.1.
RefSeqiNP_741987.1. NM_171990.2.
XP_006250493.1. XM_006250431.3.
UniGeneiRn.8453.

Genome annotation databases

EnsembliENSRNOT00000003249; ENSRNOP00000003249; ENSRNOG00000002378.
GeneIDi64473.
KEGGirno:64473.
UCSCiRGD:621833. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000347 mRNA. Translation: CAA04022.1.
BC085692 mRNA. Translation: AAH85692.1.
RefSeqiNP_741987.1. NM_171990.2.
XP_006250493.1. XM_006250431.3.
UniGeneiRn.8453.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JP4X-ray1.69A1-308[»]
ProteinModelPortaliQ9Z1N4.
SMRiQ9Z1N4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003249.

PTM databases

iPTMnetiQ9Z1N4.
PhosphoSitePlusiQ9Z1N4.
SwissPalmiQ9Z1N4.

Proteomic databases

PaxDbiQ9Z1N4.
PRIDEiQ9Z1N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003249; ENSRNOP00000003249; ENSRNOG00000002378.
GeneIDi64473.
KEGGirno:64473.
UCSCiRGD:621833. rat.

Organism-specific databases

CTDi10380.
RGDi621833. Bpnt1.

Phylogenomic databases

eggNOGiKOG3099. Eukaryota.
ENOG410XNMV. LUCA.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000293205.
HOVERGENiHBG050719.
InParanoidiQ9Z1N4.
KOiK01082.
PhylomeDBiQ9Z1N4.

Enzyme and pathway databases

BRENDAi3.1.3.57. 5301.
ReactomeiR-RNO-156584. Cytosolic sulfonation of small molecules.
SABIO-RKQ9Z1N4.

Miscellaneous databases

EvolutionaryTraceiQ9Z1N4.
PROiQ9Z1N4.

Gene expression databases

BgeeiENSRNOG00000002378.
ExpressionAtlasiQ9Z1N4. baseline and differential.
GenevisibleiQ9Z1N4. RN.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBPNT1_RAT
AccessioniPrimary (citable) accession number: Q9Z1N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.