INP4B_MOUSE
ID INP4B_MOUSE Reviewed; 924 AA.
AC Q6P1Y8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Type II inositol 3,4-bisphosphate 4-phosphatase;
DE EC=3.1.3.66 {ECO:0000250|UniProtKB:Q9QWG5};
DE AltName: Full=Inositol polyphosphate 4-phosphatase type II;
GN Name=Inpp4b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and
CC inositol 3,4-bisphosphate (By similarity). Plays a role in the late
CC stages of macropinocytosis by dephosphorylating phosphatidylinositol
CC 3,4-bisphosphate in membrane ruffles (By similarity). Antagonizes the
CC PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides
CC and thereby modulating cell cycle progression and cell survival (By
CC similarity). {ECO:0000250|UniProtKB:O15327,
CC ECO:0000250|UniProtKB:Q9QWG5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:17193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58088; EC=3.1.3.66;
CC Evidence={ECO:0000250|UniProtKB:Q9QWG5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol
CC 1,3-bisphosphate + phosphate; Xref=Rhea:RHEA:43392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414,
CC ChEBI:CHEBI:83242; Evidence={ECO:0000250|UniProtKB:O15327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4-bisphosphate + H2O = 1D-myo-inositol 3-
CC phosphate + phosphate; Xref=Rhea:RHEA:43388, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58401, ChEBI:CHEBI:83241;
CC Evidence={ECO:0000250|UniProtKB:Q9QWG5};
CC -!- ACTIVITY REGULATION: Strongly inhibited by inositol hexakisphosphate.
CC {ECO:0000250|UniProtKB:Q9QWG5}.
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC {ECO:0000250|UniProtKB:Q9QWG5}.
CC -!- SIMILARITY: Belongs to the inositol 3,4-bisphosphate 4-phosphatase
CC family. {ECO:0000305}.
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DR EMBL; BC064813; AAH64813.1; -; mRNA.
DR CCDS; CCDS22446.1; -.
DR RefSeq; NP_001019788.1; NM_001024617.3.
DR AlphaFoldDB; Q6P1Y8; -.
DR SMR; Q6P1Y8; -.
DR STRING; 10090.ENSMUSP00000044466; -.
DR iPTMnet; Q6P1Y8; -.
DR PhosphoSitePlus; Q6P1Y8; -.
DR EPD; Q6P1Y8; -.
DR jPOST; Q6P1Y8; -.
DR MaxQB; Q6P1Y8; -.
DR PaxDb; Q6P1Y8; -.
DR PRIDE; Q6P1Y8; -.
DR ProteomicsDB; 266992; -.
DR Antibodypedia; 27309; 134 antibodies from 27 providers.
DR DNASU; 234515; -.
DR Ensembl; ENSMUST00000042529; ENSMUSP00000044466; ENSMUSG00000037940.
DR GeneID; 234515; -.
DR KEGG; mmu:234515; -.
DR UCSC; uc009mjh.2; mouse.
DR CTD; 8821; -.
DR MGI; MGI:2158925; Inpp4b.
DR VEuPathDB; HostDB:ENSMUSG00000037940; -.
DR eggNOG; KOG4428; Eukaryota.
DR GeneTree; ENSGT00940000157587; -.
DR InParanoid; Q6P1Y8; -.
DR OMA; CNEMSEQ; -.
DR PhylomeDB; Q6P1Y8; -.
DR TreeFam; TF325637; -.
DR BRENDA; 3.1.3.66; 3474.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00944; -.
DR BioGRID-ORCS; 234515; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Inpp4b; mouse.
DR PRO; PR:Q6P1Y8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P1Y8; protein.
DR Bgee; ENSMUSG00000037940; Expressed in lumbar subsegment of spinal cord and 195 other tissues.
DR ExpressionAtlas; Q6P1Y8; baseline and differential.
DR Genevisible; Q6P1Y8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0017161; F:inositol-1,3,4-trisphosphate 4-phosphatase activity; IEA:RHEA.
DR GO; GO:0052828; F:inositol-3,4-bisphosphate 4-phosphatase activity; IEA:RHEA.
DR GO; GO:0008289; F:lipid binding; IDA:MGI.
DR GO; GO:0034593; F:phosphatidylinositol bisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0034594; F:phosphatidylinositol trisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0016316; F:phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity; ISO:MGI.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:MGI.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:MGI.
DR GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IMP:MGI.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039034; INPP4.
DR PANTHER; PTHR12187; PTHR12187; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid metabolism; Reference proteome.
FT CHAIN 1..924
FT /note="Type II inositol 3,4-bisphosphate 4-phosphatase"
FT /id="PRO_0000190237"
FT DOMAIN 23..148
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104531 MW; 09DF35368F4C1695 CRC64;
MEIKEEGTSE EGQHFLPAAQ ANDPEDIQFT SIQKIPNEPQ LEFILACRDL VAPVSDRKLN
TVVQISVIHP VEQTLTRYSS TEIVEGTKDP LFLTGVTFPP DYPIYEETRI KLTVYDVKDK
SHDTRSFLGC ASFKVGELLK SKEQLLSLSL RTSDGGKVVG TIEVSLVKMG EIEDGDTDHI
TTDVQGQKCA LMYESTAPES LSGKENLPFM NAVLRNPVCK LYRFPTSDNK WMRIREQMSE
SILSFHIPKE LISLHIKEDL CRNQELKELG DLSPHWDNLR KNVLSHCDQM VTMYQDILTE
LSKETGSSFK SSSSKGEKTL EFVPVNLHLQ RMQVHSPHLK DALYDVITVG APAAHFQGFK
NGGLRKLLHR FETERRNTGY QFIYYSPENT AKAKEVLSSI NQLQPLIATH ADLLLTSASQ
RSPDSLKSSL KLLSEKTELF VHAFKDQLVR SALLALYTAR PGGILKKPPS PNVSTEEKST
QHDTPQLRRQ DSIPHHSDYD EEEWDRVWAN VGKSLNCIIA KVDKLIERDS HNEEGAGGSS
SKDGEADHTL EDSITSHPRE DWYEQLHPLI LTLKECMGEV VNRAKQSLTF VLLQELAYSL
PQCLMLTLRR DIVFSQALAG LVCGFIIKLH TSLHDPGFLQ QLHTVGLIVQ YEGLLSTYSD
EIGMLEDMAV GISDLRKVAF KITEATSNDV LPVLTGRREH YVVEVKLPAT VFESLPLQIK
EGQLLHVYPV LFNVGINEQQ TLAERFGDVS LQESINQENF ELVQEYYSIF MEKMPPDYIS
HFQEQTDLKG LLDNLHQNIQ AKKRKNVEIM WLAATICRKL NGIRFTCCKS AKDRTSMSVT
LEQCSILRDE HQLHKDFFIR ALDCMRSRQT QGALNESDDP ETGCLTDNKP TSRHFYPVAL
LLVSSHLLVV WLILSLALLL AKYQ
