SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00001204 
UniProt Accession
Theoretical PI
5.42  
Molecular Weight
112762 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Inpp5b 
Gene Synonyms/Alias
 
Protein Name
Type II inositol 1,4,5-trisphosphate 5-phosphatase 
Protein Synonyms/Alias
EC=3.1.3.36 Inositol polyphosphate-5-phosphatase B; Phosphoinositide 5-phosphatase;5PTase 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:4;124419094-124478755;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. 

Abstract
The dynamic nature of cellular interactions during differentiation of germ cells and their translocation from the basement membrane to the lumen of the seminiferous tubules requires the existence of complex and well-regulated cellular adhesion mechanisms in the testis. Successful migration of the developing germ cells is characterized by dynamic breakage and reformation of cadherin-containing adherens junctions between the germ cells and Sertoli cells, the polarized somatic cells of the testis that support and nourish the developing gametes. Here, we demonstrate the accumulation of abnormally swollen, actin-coated, endosome-like structures that contain intact adherens junctions and stain positive for N-cadherin and beta-catenin in the Sertoli cell cytosol of mice deficient in Inpp5b, an inositol polyphosphate 5-phosphatase. Simultaneous to the formation of these abnormal structures, developing germ cells are prematurely released from the seminiferous epithelium and sloughed into the epididymis. Our results demonstrate a role for Inpp5b in the regulation of cell adhesion in the testis and in the formation of junctional complexes with neighboring cells, and they emphasize the important and essential role of phosphoinositides in spermatogenesis. PMID: [11967219] 

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Figures for illustrating the function of this protein/gene
Ref: E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. PMID: [11967219]
Ref: E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. PMID: [11967219]
Ref: E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. PMID: [11967219]
Ref: E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. PMID: [11967219]
Ref: E. Hellsten, D. J. Bernard, J. W. Owens, M. Eckhaus, S. F. Suchy and R. L. Nussbaum (2002) Sertoli cell vacuolization and abnormal germ cell adhesion in mice deficient in an inositol polyphosphate 5-phosphatase. Biol Reprod 66(5): 1522-30. PMID: [11967219]
Function
Hydrolyzes phosphatidylinositol 4,5-bisphosphate(PtIns(4,5)P2) and the signaling molecule phosphatidylinositol1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulatescellular signaling events. 
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Subcellular Location
Cytoplasm, cytosol. Endoplasmic reticulum-Golgi intermediate compartment (By similarity). Early endosomemembrane. Membrane; Peripheral membrane protein; Cytoplasmic side.Cytoplasmic vesicle, phagosome membrane. Golgi apparatus (Bysimilarity). 
Tissue Specificity
Detected in kidney, liver, brain, lung andtestis (at protein level). Detected in kidney and liver, and atlower levels in brain, lung and testis. 
Gene Ontology
GO IDGO termEvidence
GO:0005829 C:cytosol IDA:MGI.
GO:0031901 C:early endosome membrane IEA:UniProtKB-SubCell.
GO:0005793 C:endoplasmic reticulum-Golgi intermediate compartment IEA:UniProtKB-SubCell.
GO:0005794 C:Golgi apparatus IEA:UniProtKB-SubCell.
GO:0016021 C:integral to membrane IDA:MGI.
GO:0015630 C:microtubule cytoskeleton IEA:Compara.
GO:0030670 C:phagocytic vesicle membrane IEA:UniProtKB-SubCell.
GO:0052658 F:inositol-1,4,5-trisphosphate 5-phosphatase activity IDA:UniProtKB.
GO:0004445 F:inositol-polyphosphate 5-phosphatase activity ISA:MGI.
GO:0046872 F:metal ion binding IEA:UniProtKB-KW.
GO:0004439 F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity IDA:UniProtKB.
GO:0001701 P:in utero embryonic development IGI:MGI.
GO:0046856 P:phosphatidylinositol dephosphorylation IDA:UniProtKB.
GO:0046854 P:phosphatidylinositol phosphorylation IEA:InterPro.
GO:0070613 P:regulation of protein processing IMP:MGI.
GO:0007165 P:signal transduction IEA:InterPro.
GO:0030317 P:sperm motility IMP:MGI.
GO:0007283 P:spermatogenesis IMP:MGI.
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Interpro
IPR005135;    Endo/exonuclease/phosphatase.
IPR000300;    IPPc.
IPR008936;    Rho_GTPase_activation_prot.
IPR000198;    RhoGAP_dom.
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Pfam
PF03372;    Exo_endo_phos;    1.
PF00620;    RhoGAP;    1.
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SMART
SM00128;    IPPc;    1.
SM00324;    RhoGAP;    1.
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PROSITE
PS50003;    PH_DOMAIN;    FALSE_NEG.
PS50238;    RHOGAP;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    993       Type II inositol 1,4,5-trisphosphate 5-
                             phosphatase.
                             /FTId=PRO_0000415365.
DOMAIN       22    148       PH.
DOMAIN      821    993       Rho-GAP.
REGION      342    668       5-phosphatase (By similarity).
REGION      459    460       Substrate binding (By similarity).
REGION      582    583       Substrate binding (By similarity).
REGION      596    598       Substrate binding (By similarity).
REGION      669    782       ASH (By similarity).
METAL       355    355       Magnesium (By similarity).
METAL       383    383       Magnesium (By similarity).
BINDING     383    383       Substrate (By similarity).
LIPID       990    990       S-farnesyl cysteine (Potential).
VAR_SEQ       1    251       Missing (in isoform 3).
                             /FTId=VSP_042224.
VAR_SEQ     252    258       RERDCAG -> MKGKLLC (in isoform 3).
                             /FTId=VSP_042225.
VAR_SEQ     811    825       LMSVQTADDRSQLEN -> PGCQCNGAAAVLARG (in
                             isoform 2).
                             /FTId=VSP_042226.
VAR_SEQ     826    993       Missing (in isoform 2).
                             /FTId=VSP_042227.
CONFLICT    993    993       L -> P (in Ref. 2; BAC25089).
HELIX         3     10
STRAND       17     19
STRAND       22     27
STRAND       30     43
STRAND       46     56
HELIX        61     63
STRAND       69     73
STRAND       88     90
STRAND       94    102
STRAND      107    112
HELIX       118    127
TURN        128    132
HELIX       144    146
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Nucleotide Sequence
Length: 3858 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 993 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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