INP4B_MACFA
ID INP4B_MACFA Reviewed; 813 AA.
AC Q4R4D7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
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; ORFNames=QtsA-10790;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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). The lipid
CC phosphatase activity is critical for tumor suppressor function.
CC Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating
CC phosphoinositides and thereby modulating cell cycle progression and
CC cell survival (By 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; AB178977; BAE02028.1; -; mRNA.
DR AlphaFoldDB; Q4R4D7; -.
DR SMR; Q4R4D7; -.
DR eggNOG; KOG4428; Eukaryota.
DR UniPathway; UPA00944; -.
DR Proteomes; UP000233100; Unplaced.
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:0016316; F:phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:UniProtKB-EC.
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; 2.
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..813
FT /note="Type II inositol 3,4-bisphosphate 4-phosphatase"
FT /id="PRO_0000190236"
FT DOMAIN 23..165
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 91815 MW; 9A256E8AC42F8162 CRC64;
MEIKEEGASE EGQHFLPAAQ ASDPGDCQFT SIQKTPNEPQ LEFILACKDL VAPVRDRKLN
TLVQISVIHP VEQSLTRYSS TEIVEGTRDP LFLTGVTFPS EYPIYEETKI KLTVYDVKDK
SHDTVRTSVL PEHKDPPPEV GRSFLGYASF KVGELLKSKE QLLALSLRTS DGGKVVGTIE
VSVVKMGEIE DGEADHITTD VRGQKCALVC ECTAPESVSS KGEKTLEFVP VNLHLQRMQV
HSPHLKDALY DVITVGAPAA HFQGFKNGGL RKLLHRFETE RRNTGYQFIY YSPENTAKAK
EVLSNINQLQ PLVATHADLL LNSASQHSPD SLKNSLKMLS EKTELFVHAF KDQLVRSALL
ALYTARPGGV LKKPPSPKSS TEESSPQEQP PLMRRQDSIP HHSDYDEEEW DRVWANVGKS
LNCIIAMVDK LIERDGGSEG SGSNNDGEKE PSLADSIPSH PREDWYEQLY PLILTLKDCM
GEVVNRAKQS LTFVLLQELA YSLPQCLMLT LRRDIVFSQA LAGLVCGFII KLQTSLYDPG
FLQQLHTVGL IVQYEGLLST YSDEIGMLED MAVGISDLKK VAFKIIEAKS NDVLPVVTGR
REHYVVEVKL PARMFESLPL QIKEGQLLHV YPVLFNVGIN EQQTLAERFG DVSLQESINQ
ENFELLQEYY KIFMEKMPPD YISHFQEQND LKALLENLHQ NIQSKKRKNV EIMWLAATIC
RKLNGIRFTC CKSAKDRTSM SVTLEQCSIL RDEHQLHKDF FIRALDCMRR EGCRIENVLK
NIKCRKYAFN MLQLMAFPKY YRPPEGTYGK ADT
