INPP_BOVIN
ID INPP_BOVIN Reviewed; 400 AA.
AC P21327; Q1RMJ2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Inositol polyphosphate 1-phosphatase {ECO:0000250|UniProtKB:P49441};
DE Short=IPP;
DE Short=IPPase;
DE EC=3.1.3.57 {ECO:0000269|PubMed:8107142};
GN Name=INPP1 {ECO:0000250|UniProtKB:P49441};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=2175905; DOI=10.1073/pnas.87.24.9548;
RA York J.D., Majerus P.W.;
RT "Isolation and heterologous expression of a cDNA encoding bovine inositol
RT polyphosphate 1-phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9548-9552(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=8107142; DOI=10.1006/jmbi.1994.1167;
RA York J.D., Chen Z.W., Ponder J.W., Chauhan A.K., Mathews F.S.,
RA Majerus P.W.;
RT "Crystallization and initial X-ray crystallographic characterization of
RT recombinant bovine inositol polyphosphate 1-phosphatase produced in
RT Spodoptera frugiperda cells.";
RL J. Mol. Biol. 236:584-589(1994).
RN [4] {ECO:0007744|PDB:1INP}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP COFACTOR.
RX PubMed=7947723; DOI=10.1021/bi00249a002;
RA York J.D., Ponder J.W., Chen Z.-W., Mathews F.S., Majerus P.W.;
RT "Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A
RT resolution.";
RL Biochemistry 33:13164-13171(1994).
RN [5] {ECO:0007744|PDB:6WRO, ECO:0007744|PDB:6WRR, ECO:0007744|PDB:6WRY, ECO:0007744|PDB:6X25, ECO:0007744|PDB:7KIO, ECO:0007744|PDB:7KIR}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH 1D-MYO-INOSITOL
RP 1,4-BISPHOSPHATE, MUTAGENESIS OF ASP-54, ACTIVITY REGULATION, AND LITHIUM
RP BINDING.
RX PubMed=33172890; DOI=10.1074/jbc.ra120.014057;
RA Dollins D.E., Xiong J.P., Endo-Streeter S., Anderson D.E., Bansal V.S.,
RA Ponder J.W., Ren Y., York J.D.;
RT "A structural basis for lithium and substrate binding of an inositide
RT phosphatase.";
RL J. Biol. Chem. 296:100059-100069(2021).
CC -!- FUNCTION: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of
CC the 1-position phosphate from inositol 1,4-bisphosphate and inositol
CC 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
CC {ECO:0000269|PubMed:8107142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-
CC phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57;
CC Evidence={ECO:0000269|PubMed:8107142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554;
CC Evidence={ECO:0000305|PubMed:8107142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol
CC 3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414,
CC ChEBI:CHEBI:83241; Evidence={ECO:0000269|PubMed:8107142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320;
CC Evidence={ECO:0000305|PubMed:8107142};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7947723};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+). {ECO:0000269|PubMed:33172890,
CC ECO:0000269|PubMed:8107142}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.85 uM for 1D-myo-inositol 1,4-bisphosphate
CC {ECO:0000269|PubMed:8107142};
CC KM=30.7 uM for 1D-myo-inositol 1,3,4-trisphosphate
CC {ECO:0000269|PubMed:8107142};
CC Vmax=50.6 umol/min/mg enzyme toward 1D-myo-inositol 1,4-bisphosphate
CC {ECO:0000269|PubMed:8107142};
CC Vmax=59.7 umol/min/mg enzyme toward 1D-myo-inositol 1D-myo-inositol
CC 1,3,4-trisphosphate {ECO:0000269|PubMed:8107142};
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC {ECO:0000269|PubMed:8107142}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7947723}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; M55916; AAA30588.1; -; mRNA.
DR EMBL; BC114863; AAI14864.1; -; mRNA.
DR PIR; A39254; A39254.
DR RefSeq; NP_776789.1; NM_174364.2.
DR RefSeq; XP_005202248.1; XM_005202191.3.
DR RefSeq; XP_005202249.1; XM_005202192.2.
DR RefSeq; XP_010800089.1; XM_010801787.2.
DR RefSeq; XP_010800090.1; XM_010801788.2.
DR RefSeq; XP_010800091.1; XM_010801789.2.
DR RefSeq; XP_010800092.1; XM_010801790.2.
DR PDB; 1INP; X-ray; 2.30 A; A=1-400.
DR PDB; 6WRO; X-ray; 3.00 A; A=1-400.
DR PDB; 6WRR; X-ray; 2.50 A; A=1-400.
DR PDB; 6WRY; X-ray; 2.80 A; A=2-389.
DR PDB; 6X25; X-ray; 3.20 A; A=1-400.
DR PDB; 7KIO; X-ray; 2.40 A; A=1-400.
DR PDB; 7KIR; X-ray; 2.60 A; A=1-400.
DR PDBsum; 1INP; -.
DR PDBsum; 6WRO; -.
DR PDBsum; 6WRR; -.
DR PDBsum; 6WRY; -.
DR PDBsum; 6X25; -.
DR PDBsum; 7KIO; -.
DR PDBsum; 7KIR; -.
DR AlphaFoldDB; P21327; -.
DR SMR; P21327; -.
DR STRING; 9913.ENSBTAP00000009977; -.
DR PaxDb; P21327; -.
DR PeptideAtlas; P21327; -.
DR PRIDE; P21327; -.
DR Ensembl; ENSBTAT00000009977; ENSBTAP00000009977; ENSBTAG00000007584.
DR Ensembl; ENSBTAT00000084681; ENSBTAP00000070119; ENSBTAG00000007584.
DR GeneID; 281869; -.
DR KEGG; bta:281869; -.
DR CTD; 3628; -.
DR VEuPathDB; HostDB:ENSBTAG00000007584; -.
DR VGNC; VGNC:30208; INPP1.
DR eggNOG; KOG3099; Eukaryota.
DR GeneTree; ENSGT00940000156785; -.
DR HOGENOM; CLU_043868_2_0_1; -.
DR InParanoid; P21327; -.
DR OMA; ANIARVC; -.
DR OrthoDB; 1096950at2759; -.
DR TreeFam; TF314300; -.
DR Reactome; R-BTA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; P21327; -.
DR UniPathway; UPA00944; -.
DR EvolutionaryTrace; P21327; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000007584; Expressed in oocyte and 103 other tissues.
DR GO; GO:0052829; F:inositol-1,3,4-trisphosphate 1-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR Gene3D; 4.10.460.10; -; 1.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR044897; INPP1_dom_1.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Lithium; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..400
FT /note="Inositol polyphosphate 1-phosphatase"
FT /id="PRO_0000142509"
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Li(+)"
FT /ligand_id="ChEBI:CHEBI:49713"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000305|PubMed:33172890"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7947723,
FT ECO:0000312|PDB:1INP"
FT BINDING 80
FT /ligand="Li(+)"
FT /ligand_id="ChEBI:CHEBI:49713"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000305|PubMed:33172890"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7947723,
FT ECO:0000312|PDB:1INP"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7947723,
FT ECO:0000312|PDB:1INP"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7947723,
FT ECO:0000312|PDB:1INP"
FT BINDING 156
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 157
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 158
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 268
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 270
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 290
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 291
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 294
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 312
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000269|PubMed:33172890,
FT ECO:0007744|PDB:7KIR"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7947723,
FT ECO:0000312|PDB:1INP"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49441"
FT MUTAGEN 54
FT /note="D->A: Does not alter affinity for 1D-myo-inositol
FT 1,3,4-trisphosphate. Decreases about 100-fold Li(+)
FT sensitivity. Loss of inositol polyphosphate 1-phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:33172890"
FT CONFLICT 84
FT /note="F -> L (in Ref. 1; AAA30588)"
FT /evidence="ECO:0000305"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 48..68
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 215..230
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6WRY"
FT TURN 359..364
FT /evidence="ECO:0007829|PDB:1INP"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1INP"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:1INP"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1INP"
SQ SEQUENCE 400 AA; 43965 MW; 27917063A224D6A8 CRC64;
MSDILQELLR VSEKAANIAR ACRQQETLFQ LLIEEKKEGE KNKKFAVDFK TLADVLVQEV
IKENMENKFP GLGKKIFGEE SNEFTNDLGE KIIMRLGPTE EETVALLSKV LNGNKLASEA
LAKVVHQDVF FSDPALDSVE INIPQDILGI WVDPIDSTYQ YIKGSADITP NQGIFPSGLQ
CVTVLIGVYD IQTGVPLMGV INQPFVSQDL HTRRWKGQCY WGLSYLGTNI HSLLPPVSTR
SNSEAQSQGT QNPSSEGSCR FSVVISTSEK ETIKGALSHV CGERIFRAAG AGYKSLCVIL
GLADIYIFSE DTTFKWDSCA AHAILRAMGG GMVDLKECLE RNPDTGLDLP QLVYHVGNEG
AAGVDQWANK GGLIAYRSEK QLETFLSRLL QHLAPVATHT
