ID   MINP1_PONAB             Reviewed;         487 AA.
AC   Q5R890;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000250|UniProtKB:Q9UNW1};
DE            EC=3.1.3.62 {ECO:0000250|UniProtKB:Q9UNW1};
DE   AltName: Full=2,3-bisphosphoglycerate 3-phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE            Short=2,3-BPG phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE            EC=3.1.3.80 {ECO:0000250|UniProtKB:Q9UNW1};
DE   Flags: Precursor;
GN   Name=MINPP1 {ECO:0000250|UniProtKB:Q9UNW1};
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].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes
CC       1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-
CC       inositol hexakisphosphate (InsP6) to a range of less phosphorylated
CC       inositol phosphates. This regulates the availability of these various
CC       small molecule second messengers and metal chelators which control many
CC       aspects of cell physiology. Has a weak in vitro activity towards 1D-
CC       myo-inositol 1,4,5-trisphosphate which is unlikely to be
CC       physiologically relevant. By regulating intracellular inositol
CC       polyphosphates pools, which act as metal chelators, it may control the
CC       availability of intracellular calcium and iron, which are important for
CC       proper neuronal development and homeostasis. May have a dual substrate
CC       specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase
CC       hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-
CC       bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering
CC       glycolytic bypass and is a regulator of systemic oxygen homeostasis as
CC       the major allosteric effector of hemoglobin.
CC       {ECO:0000250|UniProtKB:Q9UNW1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:58130; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:195535; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC         ChEBI:CHEBI:195537; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol
CC         1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537,
CC         ChEBI:CHEBI:195539; EC=3.1.3.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-
CC         phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539;
CC         EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,3,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:20960,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130,
CC         ChEBI:CHEBI:58747; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20961;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,3,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77111,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58747,
CC         ChEBI:CHEBI:195534; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77112;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,3-trisphosphate + phosphate; Xref=Rhea:RHEA:77123,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195534,
CC         ChEBI:CHEBI:195536; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77124;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol
CC         2,3-bisphosphate + phosphate; Xref=Rhea:RHEA:77127,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195536,
CC         ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77128;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-
CC         phosphate + phosphate; Xref=Rhea:RHEA:77139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195538;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77140;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627,
CC         ChEBI:CHEBI:57733; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77147,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627,
CC         ChEBI:CHEBI:203600; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77148;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate +
CC         phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNW1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O35217}. Secreted
CC       {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma
CC       membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UNW1}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR859864; CAH92020.1; -; mRNA.
DR   RefSeq; NP_001126173.1; NM_001132701.1.
DR   AlphaFoldDB; Q5R890; -.
DR   SMR; Q5R890; -.
DR   STRING; 9601.ENSPPYP00000002842; -.
DR   GlyCosmos; Q5R890; 2 sites, No reported glycans.
DR   GeneID; 100173135; -.
DR   KEGG; pon:100173135; -.
DR   CTD; 9562; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   InParanoid; Q5R890; -.
DR   OrthoDB; 1072311at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016158; F:3-phytase activity; IEA:RHEA.
DR   GO; GO:0008707; F:4-phytase activity; IEA:RHEA.
DR   GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016312; F:inositol bisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052827; F:inositol pentakisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0046030; F:inositol trisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030351; F:inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030352; F:inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004446; F:inositol-hexakisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; ISS:UniProtKB.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF57; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..487
FT                   /note="Multiple inositol polyphosphate phosphatase 1"
FT                   /id="PRO_0000019584"
FT   MOTIF           484..487
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2L6"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   487 AA;  55090 MW;  F95A1B12B4EA1660 CRC64;
     MLRASGCLLR TSVAPAAALA AALFSSLARC SLLEPRDLVA SSLSPYFGTK TRYEDVNPLL
     LSGPEAPWRD PELLEGSCTP VQLVALIRHG TRYPTAKQIR KLRQLHGLLQ ARGSRDGGAG
     STGSRDLGAA LADWPLWYAD WMDGQLVEKG RQDMRQLALR LASLFPALFS RENYGRLRLI
     TSSKHRCMDS SAAFLQGLWQ HYHPGLPPPD VADMEFGPPT VNDKLMRFFD HCEKFLTEVE
     KNATALYHVE AFKTGPEMQN ILKKVAATLQ VPVNDLNADL LQVAFFTCSF DLAIKGVKSP
     WCDVFDIDDA KVLEYLNDLK QYWKRGYGYT INSRSSCTLF QDIFRHLDKA VEQKQRSQPI
     SSPVILQFGH AETLLPLLSL MGYFKDKEPL TAYNYKEQMH RKFRSGLIVP YASNLIFVLY
     HCENAKTPKE QFRVQMLLNE KVLPLAYSQE TVSFYEDLRN HYKDILQSCQ TSEECELARA
     NSTSDEL
//