INP4B_PONAB
ID INP4B_PONAB Reviewed; 924 AA.
AC Q5RA60; Q5RCA1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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). 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RA60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RA60-2; Sequence=VSP_015248;
CC -!- SIMILARITY: Belongs to the inositol 3,4-bisphosphate 4-phosphatase
CC family. {ECO:0000305}.
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DR EMBL; CR858378; CAH90606.1; -; mRNA.
DR EMBL; CR859161; CAH91350.1; -; mRNA.
DR RefSeq; NP_001127308.1; NM_001133836.1.
DR AlphaFoldDB; Q5RA60; -.
DR STRING; 9601.ENSPPYP00000016852; -.
DR GeneID; 100174369; -.
DR KEGG; pon:100174369; -.
DR CTD; 8821; -.
DR eggNOG; KOG4428; Eukaryota.
DR InParanoid; Q5RA60; -.
DR OrthoDB; 129165at2759; -.
DR UniPathway; UPA00944; -.
DR Proteomes; UP000001595; 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; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Lipid metabolism; Reference proteome.
FT CHAIN 1..924
FT /note="Type II inositol 3,4-bisphosphate 4-phosphatase"
FT /id="PRO_0000190238"
FT DOMAIN 23..165
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 881..924
FT /note="REGCRIENVLKNIKCRKYAFNMLQLMAFPKYYRPPEGTYGKADT -> SRQT
FT QGALNESDDPETGCLTDNKPTSRHFYPVALLLVSSHLLVVWLILSLALLLAKYQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015248"
FT CONFLICT 137
FT /note="P -> L (in Ref. 1; CAH90606)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="R -> Q (in Ref. 1; CAH90606)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="A -> V (in Ref. 1; CAH90606)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="V -> A (in Ref. 1; CAH90606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 924 AA; 104713 MW; 1463135AEAD9523E CRC64;
MEIKEEGASE EGQHFLPTAQ ASDPGDCQFT SIQKTPNEPQ LEFILACKDL VAPVRDRKLN
TLVQISVIHP VEQSLTRYSS TEIVEGTRDP LFLTGVTFPS EYPIYEETKI KLTVYDVKDK
SHDTVRTSVL PEHKDSPPEI GRSFLGYASF KVGELLKSKE QLLVLSLRTS DGGKVVGTIE
VSVVKMGEIE DGEADHITTD IQGQKCALVC ECTAPESVSG KDNLPFLNSV LKNPVCKLYR
FPTSDNKWMR IREQMSESIL SFHIPKELIS LHIKEDLCRN QEIKELGELS PHWDNLRKNV
LTHCDQMVNM YQDILTELSK ETGSSFKSSS SKGDKTLEFV PINLHLQRMQ VHSPHLKDAL
YDVITVGAPA AHFQGFKNGG LRKLLHRFET ERRNTGYQFI YYSPENTAKA KEVLSNINQL
QPLIATHADL LLNSASQHSP DSLKNSLKML SEKTELFVHA FKDQLVRSAL LALYTARPGG
ILKKPPSPKS STEESSPQDQ PPLMRGQDSI PHHSDYDEEE WDRVWANVGK SLNCIIAMVD
KLIERDGGSE GSGGNNDGEK EPSLADAIPS HPREDWYEQL YPLILTLKDC MGEVVNRAKQ
SLTFVLLQEL AYSLPQCLML TLRRDVVFSQ ALAGLVCGFI IKLQTSLYDP GFLRQLHTVG
LIVQYEGLLS TYSDEIGMLE DMAVGISDLK KVAFKIIEAK SNDVLPVITG RREHYVVEVK
LPARMFESLP LQIKEGQLLH VYPVLFNVGI NEQQTLAERF GDVSLQESIN QENFELLQEY
YKIFMEKMPP DYISHFQEQN DLKALLENLL QNIQSKKRKN VEIMWLAATI CRKLNGIRFT
CCKSAKDRTS MSVTLEQCSI LRDEHQLHKD FFIRALDCMR REGCRIENVL KNIKCRKYAF
NMLQLMAFPK YYRPPEGTYG KADT
