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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Magnesium 11 Publication
Binding sitei74 – 741SubstrateBy similarity
Metal bindingi117 – 1171Magnesium 11 Publication
Metal bindingi117 – 1171Magnesium 21 Publication
Metal bindingi119 – 1191Magnesium 1; via carbonyl oxygen1 Publication
Metal bindingi120 – 1201Magnesium 21 Publication
Binding sitei242 – 2421Substrate; via carbonyl oxygen
Metal bindingi247 – 2471Magnesium 21 Publication
Binding sitei247 – 2471Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 3083073'(2'),5'-bisphosphate nucleotidase 1PRO_0000142529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei122 – 1221PhosphothreonineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei244 – 2441N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z1N4.
PRIDEiQ9Z1N4.

PTM databases

iPTMnetiQ9Z1N4.
PhosphoSiteiQ9Z1N4.
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

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 3226Combined sources
Beta strandi38 – 425Combined sources
Beta strandi45 – 473Combined sources
Helixi49 – 6517Combined sources
Beta strandi69 – 757Combined sources
Helixi84 – 863Combined sources
Helixi93 – 964Combined sources
Helixi102 – 1043Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1209Combined sources
Helixi122 – 1265Combined sources
Helixi130 – 1323Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi144 – 1529Combined sources
Turni153 – 1586Combined sources
Beta strandi167 – 1726Combined sources
Turni173 – 1753Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi191 – 1988Combined sources
Helixi201 – 2088Combined sources
Beta strandi213 – 2197Combined sources
Helixi221 – 2299Combined sources
Beta strandi234 – 2385Combined sources
Helixi245 – 25713Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi284 – 2896Combined sources
Helixi291 – 2977Combined sources
Helixi300 – 3056Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JP4X-ray1.69A1-308[»]
ProteinModelPortaliQ9Z1N4.
SMRiQ9Z1N4. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z1N4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 1224Substrate binding
Regioni195 – 1984Substrate binding
Regioni220 – 2245Substrate

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.
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_006250431.2.
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_006250431.2.
UniGeneiRn.8453.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JP4X-ray1.69A1-308[»]
ProteinModelPortaliQ9Z1N4.
SMRiQ9Z1N4. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003249.

PTM databases

iPTMnetiQ9Z1N4.
PhosphoSiteiQ9Z1N4.
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.
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: September 7, 2016
This is version 119 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.