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Protein

Type II inositol 1,4,5-trisphosphate 5-phosphatase

Gene

Inpp5b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi355MagnesiumBy similarity1
Metal bindingi383MagnesiumBy similarity1
Binding sitei383SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • flagellated sperm motility Source: MGI
  • in utero embryonic development Source: MGI
  • phosphatidylinositol dephosphorylation Source: UniProtKB
  • regulation of protein processing Source: MGI
  • signal transduction Source: InterPro
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC:3.1.3.36)
Alternative name(s):
Inositol polyphosphate-5-phosphatase B
Phosphoinositide 5-phosphatase
Short name:
5PTase
Gene namesi
Name:Inpp5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:103257. Inpp5b.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • early endosome membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  • integral component of membrane Source: MGI
  • membrane Source: MGI
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004153651 – 990Type II inositol 1,4,5-trisphosphate 5-phosphataseAdd BLAST990
PropeptideiPRO_0000422294991 – 993Removed in mature formSequence analysis3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei990Cysteine methyl esterSequence analysis1
Lipidationi990S-farnesyl cysteineSequence analysis1

Post-translational modificationi

Isoprenylation at Cys-990 may be required for localization at the membrane.By similarity
May be proteolytically cleaved after Lys-320 as inferred from N-terminal protein sequence of the 75 kda form.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ8K337.
PeptideAtlasiQ8K337.
PRIDEiQ8K337.

PTM databases

iPTMnetiQ8K337.
PhosphoSitePlusiQ8K337.

Expressioni

Tissue specificityi

Detected in kidney, liver, brain, lung and testis (at protein level). Detected in kidney and liver, and at lower levels in brain, lung and testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000028894.
ExpressionAtlasiQ8K337. baseline and differential.
GenevisibleiQ8K337. MM.

Interactioni

Subunit structurei

Interacts with APPL1, FAM109A and FAM109B. Interacts with several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may play a dual role in targeting INPP5B to the specific membranes and stimulating the phosphatase activity (By similarity). Interacts with INPP5F (PubMed:25869668).By similarity1 Publication

Protein-protein interaction databases

BioGridi200768. 1 interactor.
IntActiQ8K337. 1 interactor.
MINTiMINT-4105144.
STRINGi10090.ENSMUSP00000092375.

Structurei

Secondary structure

1993
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Beta strandi17 – 19Combined sources3
Beta strandi22 – 27Combined sources6
Beta strandi30 – 43Combined sources14
Beta strandi46 – 56Combined sources11
Helixi61 – 63Combined sources3
Beta strandi69 – 73Combined sources5
Beta strandi88 – 90Combined sources3
Beta strandi94 – 102Combined sources9
Beta strandi107 – 112Combined sources6
Helixi118 – 127Combined sources10
Turni128 – 132Combined sources5
Helixi144 – 146Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KIGNMR-A1-156[»]
ProteinModelPortaliQ8K337.
SMRiQ8K337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K337.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 148PHAdd BLAST127
Domaini821 – 993Rho-GAPPROSITE-ProRule annotationAdd BLAST173

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni342 – 6685-phosphataseBy similarityAdd BLAST327
Regioni459 – 460Substrate bindingBy similarity2
Regioni582 – 583Substrate bindingBy similarity2
Regioni596 – 598Substrate bindingBy similarity3
Regioni669 – 782ASHBy similarityAdd BLAST114

Domaini

The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by FAM109A and FAM109B as endosomes mature, all three interactions relie on F&H motifs, an approximately 12-13 amino-acid sequence centered around Phe and His residues essential for binding (By similarity).By similarity

Sequence similaritiesi

Contains 1 PH domain.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
KOG4270. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000008071.
HOVERGENiHBG000070.
InParanoidiQ8K337.
KOiK01099.
OMAiHIEEYER.
OrthoDBiEOG091G02KE.
PhylomeDBiQ8K337.
TreeFamiTF317034.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR031896. INPP5B_PH_dom.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF16776. INPP5B_PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K337-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDQSVAIQET LVEGEYCVIA VQGVLCKGDS RQSRLLGLVR YRLENDAQEH
60 70 80 90 100
ALFLYTHRRM AITGDDVSLD QIVPLSKDFM LEEVSPDGEL YILGSDVTVQ
110 120 130 140 150
LNTAELKLVF QLPFGSHTRT FLQEVARACP GFDPETRDPE FEWLSRHTCA
160 170 180 190 200
EPDAESPKPR EWNSDPGTRS GFAPIGGSRH QSRNARRGLE DVLPRGPGYI
210 220 230 240 250
LLWGGAAEEP EFLLAEEMHE GGPVRGRRPL AGRRDEALEE ADWEMSAGGG
260 270 280 290 300
SRERDCAGVS NVDSSRPNGR GPDQPSGARC PEKPENSLTR QNKSKSDMSE
310 320 330 340 350
KVRSATVTVS DKAHILSVQK FGLRDTIVRS HLVQKEENYT YIQNFRFFVG
360 370 380 390 400
TYNVNGQSPK ECLRPWLSHS ALAPDVYCVG FQELDLSKEA FFFHDTPKEE
410 420 430 440 450
EWFKAVSESL HPDAKYAKVK FVRLVGIMLL LYVKQEHAAY ISEVEAETVG
460 470 480 490 500
TGIMGRMGNK GGVAIRFQLH NTSICVVNSH LAAHTEEYER RNQDYRDICS
510 520 530 540 550
RMQFPQVDPS QPPLTINKHD VILWLGDLNY RIEELDVGKV KKLVEEKAFQ
560 570 580 590 600
TLYAHDQLKI QVAARTIFDG FTEGEITFQP TYKYDTGSDD WDTSEKCRAP
610 620 630 640 650
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNEELYRK
660 670 680 690 700
TLEEIVRSLD KMENANIPSV TLSKREFCFE NVKYMQLQTE SFTIHNSQVP
710 720 730 740 750
CQFEFINKPD EESYCKQWLT ARPSKGFLLP DSHVEIELEL FVNKSTATKL
760 770 780 790 800
NSGKDTIEDI LVLHLERGKD YFLSVSGNYL PSCFGSPIHT LCYMREPILD
810 820 830 840 850
LPLKTVSDLT LMSVQTADDR SQLENPMEIP KELWMMVDYL YRNAVQQEDL
860 870 880 890 900
FQQPGLRPEF DHIRDCLDTG MIDQLCANNH SVAEALLLFL ESLPEPVICY
910 920 930 940 950
SAYHSCLECS GNYAASKQII LTLPSFHKNV FNYLMAFLQE LLKNSANNHL
960 970 980 990
DENILASIFG SLLLRNPARH QKLDMAEKKK AQEFIHQFLC GPL
Length:993
Mass (Da):112,762
Last modified:October 1, 2002 - v1
Checksum:iC15670755B562878
GO
Isoform 2 (identifier: Q8K337-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     811-825: LMSVQTADDRSQLEN → PGCQCNGAAAVLARG
     826-993: Missing.

Show »
Length:825
Mass (Da):93,161
Checksum:iB173B668AA658BE4
GO
Isoform 3 (identifier: Q8K337-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
     252-258: RERDCAG → MKGKLLC

Show »
Length:742
Mass (Da):84,888
Checksum:iB21751E2A3C40404
GO

Sequence cautioni

The sequence AAB95412 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti993L → P in BAC25089 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0422241 – 251Missing in isoform 3. 1 PublicationAdd BLAST251
Alternative sequenceiVSP_042225252 – 258RERDCAG → MKGKLLC in isoform 3. 1 Publication7
Alternative sequenceiVSP_042226811 – 825LMSVQ…SQLEN → PGCQCNGAAAVLARG in isoform 2. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_042227826 – 993Missing in isoform 2. 1 PublicationAdd BLAST168

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007563 mRNA. Translation: AAG23293.1.
AK004601 mRNA. Translation: BAC25089.1.
AL606933, AL606907 Genomic DNA. Translation: CAM16097.1.
BC028864 mRNA. Translation: AAH28864.1.
AF040094 mRNA. Translation: AAB95412.2. Different initiation.
CCDSiCCDS38876.1. [Q8K337-1]
PIRiT42384.
RefSeqiNP_032411.3. NM_008385.4. [Q8K337-1]
UniGeneiMm.296202.

Genome annotation databases

EnsembliENSMUST00000094782; ENSMUSP00000092375; ENSMUSG00000028894. [Q8K337-1]
ENSMUST00000184454; ENSMUSP00000139221; ENSMUSG00000028894. [Q8K337-2]
GeneIDi16330.
KEGGimmu:16330.
UCSCiuc008uqy.2. mouse. [Q8K337-1]
uc008uqz.1. mouse. [Q8K337-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007563 mRNA. Translation: AAG23293.1.
AK004601 mRNA. Translation: BAC25089.1.
AL606933, AL606907 Genomic DNA. Translation: CAM16097.1.
BC028864 mRNA. Translation: AAH28864.1.
AF040094 mRNA. Translation: AAB95412.2. Different initiation.
CCDSiCCDS38876.1. [Q8K337-1]
PIRiT42384.
RefSeqiNP_032411.3. NM_008385.4. [Q8K337-1]
UniGeneiMm.296202.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KIGNMR-A1-156[»]
ProteinModelPortaliQ8K337.
SMRiQ8K337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200768. 1 interactor.
IntActiQ8K337. 1 interactor.
MINTiMINT-4105144.
STRINGi10090.ENSMUSP00000092375.

PTM databases

iPTMnetiQ8K337.
PhosphoSitePlusiQ8K337.

Proteomic databases

PaxDbiQ8K337.
PeptideAtlasiQ8K337.
PRIDEiQ8K337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094782; ENSMUSP00000092375; ENSMUSG00000028894. [Q8K337-1]
ENSMUST00000184454; ENSMUSP00000139221; ENSMUSG00000028894. [Q8K337-2]
GeneIDi16330.
KEGGimmu:16330.
UCSCiuc008uqy.2. mouse. [Q8K337-1]
uc008uqz.1. mouse. [Q8K337-3]

Organism-specific databases

CTDi3633.
MGIiMGI:103257. Inpp5b.

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
KOG4270. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000008071.
HOVERGENiHBG000070.
InParanoidiQ8K337.
KOiK01099.
OMAiHIEEYER.
OrthoDBiEOG091G02KE.
PhylomeDBiQ8K337.
TreeFamiTF317034.

Enzyme and pathway databases

ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiInpp5b. mouse.
EvolutionaryTraceiQ8K337.
PROiQ8K337.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028894.
ExpressionAtlasiQ8K337. baseline and differential.
GenevisibleiQ8K337. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR031896. INPP5B_PH_dom.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF16776. INPP5B_PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiI5P2_MOUSE
AccessioniPrimary (citable) accession number: Q8K337
Secondary accession number(s): O54996, Q8CF65, Q91ZF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 117 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.