LOCUS INP4B_RAT 928 aa linear ROD 27-NOV-2024
DEFINITION RecName: Full=Type II inositol 3,4-bisphosphate 4-phosphatase;
AltName: Full=Inositol polyphosphate 4-phosphatase type II.
ACCESSION Q9QWG5
VERSION Q9QWG5.1
DBSOURCE UniProtKB: locus INP4B_RAT, accession Q9QWG5;
class: standard.
extra accessions:O35825
created: Aug 30, 2005.
sequence updated: May 1, 2000.
annotation updated: Nov 27, 2024.
xrefs: U96920.1, AAB72151.1, U96921.1, AAB72152.1, NP_446369.1,
XP_008770684.1, XP_008770686.1, XP_017456652.1, XP_017456653.1
xrefs (non-sequence databases): AlphaFoldDB:Q9QWG5, SMR:Q9QWG5,
STRING:10116.ENSRNOP00000025013, SwissLipids:SLP:000000896,
iPTMnet:Q9QWG5, PhosphoSitePlus:Q9QWG5,
PaxDb:10116-ENSRNOP00000025013, Ensembl:ENSRNOT00000024981.7,
Ensembl:ENSRNOP00000024981.4, Ensembl:ENSRNOG00000018382.7,
Ensembl:ENSRNOT00000025013.5, Ensembl:ENSRNOP00000025013.4,
Ensembl:ENSRNOT00055013428, Ensembl:ENSRNOP00055010753,
Ensembl:ENSRNOG00055007963, Ensembl:ENSRNOT00060020295,
Ensembl:ENSRNOP00060015957, Ensembl:ENSRNOG00060011966,
Ensembl:ENSRNOT00065016487, Ensembl:ENSRNOP00065012532,
Ensembl:ENSRNOG00065010215, GeneID:116699, KEGG:rno:116699,
AGR:RGD:620470, CTD:8821, RGD:620470, eggNOG:KOG4428,
GeneTree:ENSGT00940000157587, HOGENOM:CLU_007802_1_0_1,
InParanoid:Q9QWG5, OMA:VITGRRX, OrthoDB:5490552at2759,
PhylomeDB:Q9QWG5, TreeFam:TF325637, BRENDA:3.1.3.66,
Reactome:R-RNO-1660499, Reactome:R-RNO-1660516,
Reactome:R-RNO-1855183, UniPathway:UPA00944, PRO:PR:Q9QWG5,
Proteomes:UP000002494, Bgee:ENSRNOG00000018382, GO:0005737,
GO:0017161, GO:0052828, GO:0008289, GO:0034593, GO:0034594,
GO:0016316, GO:0006874, GO:0045671, GO:0046856, GO:0046850,
GO:0046822, GO:0051896, CDD:cd04048, FunFam:2.60.40.150:FF:000143,
Gene3D:2.60.40.150, InterPro:IPR000008, InterPro:IPR035892,
InterPro:IPR039034, PANTHER:PTHR12187, PANTHER:PTHR12187:SF3,
SUPFAM:SSF49562, PROSITE:PS50004
KEYWORDS Alternative splicing; Hydrolase; Lipid metabolism; Reference
proteome.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (residues 1 to 928)
AUTHORS Norris,F.A., Atkins,R.C. and Majerus,P.W.
TITLE The cDNA cloning and characterization of inositol polyphosphate
4-phosphatase type II. Evidence for conserved alternative splicing
in the 4-phosphatase family
JOURNAL J Biol Chem 272 (38), 23859-23864 (1997)
PUBMED 9295334
REMARK NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY,
ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
FUNCTION.;
TISSUE=Brain
COMMENT On Mar 21, 2006 this sequence version replaced gi:81861214.
[FUNCTION] Catalyzes the hydrolysis of the 4-position phosphate of
phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate
and inositol 3,4-bisphosphate (PubMed:9295334). Plays a role in the
late stages of macropinocytosis by dephosphorylating
phosphatidylinositol 3,4-bisphosphate in membrane ruffles (By
similarity). The lipid phosphatase activity is critical for tumor
suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway
by dephosphorylating phosphoinositides and thereby modulating cell
cycle progression and cell survival (By similarity).
{ECO:0000250|UniProtKB:O15327, ECO:0000269|PubMed:9295334}.
[CATALYTIC ACTIVITY] Reaction=a
1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate)
+ H2O = a
1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) +
phosphate; Xref=Rhea:RHEA:17193, ChEBI:CHEBI:15377,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:58088;
EC=3.1.3.66; Evidence={ECO:0000269|PubMed:9295334}.
[CATALYTIC ACTIVITY] Reaction=1D-myo-inositol 3,4-bisphosphate +
H2O = 1D-myo-inositol 3-phosphate + phosphate;
Xref=Rhea:RHEA:43388, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:58401, ChEBI:CHEBI:83241;
Evidence={ECO:0000269|PubMed:9295334}.
[CATALYTIC ACTIVITY] Reaction=1D-myo-inositol 1,3,4-trisphosphate +
H2O = 1D-myo-inositol 1,3-bisphosphate + phosphate;
Xref=Rhea:RHEA:43392, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:58414, ChEBI:CHEBI:83242;
Evidence={ECO:0000269|PubMed:9295334}.
ACTIVITY REGULATION: Strongly inhibited by inositol
hexakisphosphate. {ECO:0000269|PubMed:9295334}.
[BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=39 uM for
inositol 3,4-bisphosphate {ECO:0000269|PubMed:9295334}; KM=34 uM
for inositol 1,3,4-trisphosphate {ECO:0000269|PubMed:9295334};
Vmax=26 umol/min/mg enzyme with inositol 3,4-bisphosphate as
substrate {ECO:0000269|PubMed:9295334}; Vmax=22 umol/min/mg enzyme
with inositol 1,3,4-trisphosphate as substrate
{ECO:0000269|PubMed:9295334}; pH dependence: Optimum pH is 7-8.
{ECO:0000269|PubMed:9295334}.
[PATHWAY] Signal transduction; phosphatidylinositol signaling
pathway. {ECO:0000269|PubMed:9295334}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=2; Name=1; Synonyms=Alpha; IsoId=Q9QWG5-1;
Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=Q9QWG5-2;
Sequence=VSP_015249.
[MISCELLANEOUS] [Isoform 2]: Inactive. {ECO:0000305}.
[SIMILARITY] Belongs to the inositol 3,4-bisphosphate 4-phosphatase
family. {ECO:0000305}.
FEATURES Location/Qualifiers
source 1..928
/organism="Rattus norvegicus"
/db_xref="taxon:10116"
gene 1..928
/gene="Inpp4b"
Protein 1..928
/product="Type II inositol 3,4-bisphosphate 4-phosphatase"
/EC_number="3.1.3.66"
/note="Inositol polyphosphate 4-phosphatase type II"
/UniProtKB_evidence="Evidence at protein level"
Region 1..928
/region_name="Mature chain"
/note="Type II inositol 3,4-bisphosphate 4-phosphatase.
/id=PRO_0000190239."
Region 1..23
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 23..165
/region_name="Domain"
/note="C2.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00041."
Region 39..175
/region_name="C2A_Copine"
/note="C2 domain first repeat in Copine; cd04048"
/db_xref="CDD:176013"
Site order(54,60,116,118,143)
/site_type="other"
/note="putative Ca2+ binding site [ion binding]"
/db_xref="CDD:176013"
Region 481..516
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 488..516
/region_name="Compositionally biased region"
/note="Basic and acidic residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 548..575
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 885..928
/region_name="Splicing variant"
/note="REGCRIENVLKNIKCRRYAFNMLQLMAFPKCYRPPEGTYGKADT ->
SRQTQGALNESDDPETGCLSDNKPTSRHFYPVALLLVSSHLLVVWLILSLALLLAKYQ
(in isoform 2). /evidence=ECO:0000303|PubMed:9295334.
/id=VSP_015249."
ORIGIN
1 meikeegtse egqhflpaaq andpediqft siqkspnepq lefilackdl vapvsdrkln
61 tvvqvsvihp veqtltryss teivegtkdp lfltgvtfps dypiyeetri kltvydvkdk
121 phdtirtsvl pehkdpppev arsflgcasf kvgellkske qllslslrts dggkvvgtie
181 vslvkmgeie dgdtdhittd vqgqkcalvy dstapeslsg kenlpfmnav lrnpvcklyr
241 fptsdnkwmr ireqmsesil sfhipkelis lhikedlcrn qelkelgdls phwdnlrnnv
301 lshcdqmvtm yqdiltelsk etgssfksss skgektlefv pinlhlqrmq vhsphlkdal
361 ydvitvgapa ahfqgfkngg lrkllhrfet errntgyqfi yyspentaka kevlssinql
421 qplvathadl lltsasqhsp dslrsslkll sektelfvha fkdqlvrsal lalytarpgg
481 ilrkppspkv steekssqhd spqqlrrqds iphhsdydee ewdrvwanvg kslnciiakv
541 dklierdsrn dkstggdssk dgdadpnled sltshpredw yeqlhplilt lkecmaevvn
601 rakqsltfvl lqelayslpq clmltlrrdi vfsqalaglv cgfiiklhts lhdpgflqql
661 htvglivqye gllstysdei gmledmavgi sdlrkvafki teatsndvlp vltgrrehyv
721 vevklpatvf eslplqikeg qllhvypvlf nvgineqqtl aerfgdvslq esinqenfel
781 vqeyysifme kmppdyishf qeqndlkgll dnlhqniqak krknveimwl aaticrklng
841 irftccksak drtsmsvtle qcsilrdehq lhkdffiral dcmrregcri envlknikcr
901 ryafnmlqlm afpkcyrppe gtygkadt
//