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   03-AUG-2022, entry version 69.
DE   RecName: Full=Multiple inositol polyphosphate phosphatase 1;
DE            EC=3.1.3.62;
DE   AltName: Full=2,3-bisphosphoglycerate 3-phosphatase;
DE            Short=2,3-BPG phosphatase;
DE            EC=3.1.3.80;
DE   AltName: Full=Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase;
DE            Short=Ins(1,3,4,5)P(4) 3-phosphatase;
DE   Flags: Precursor;
GN   Name=MINPP1;
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: Acts as a phosphoinositide 5- and phosphoinositide 6-
CC       phosphatase and regulates cellular levels of inositol pentakisphosphate
CC       (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-
CC       bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation
CC       of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate
CC       without formation of 3-phosphoglycerate. May play a role in bone
CC       development (endochondral ossification). May play a role in the
CC       transition of chondrocytes from proliferation to hypertrophy (By
CC       similarity). Through the regulation of intracellular inositol
CC       polyphosphates, may control intracellular cation homeostasis, including
CC       that of calcium and iron, hence affecting free cation availability
CC       required for neural cell signaling (By similarity).
CC       {ECO:0000250|UniProtKB:F1NPQ2, ECO:0000250|UniProtKB:Q9UNW1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol hexakisphosphate + H2O = myo-inositol
CC         pentakisphosphate (mixed isomers) + phosphate.; EC=3.1.3.62;
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O35217}.
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   GeneID; 100173135; -.
DR   KEGG; pon:100173135; -.
DR   CTD; 9562; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   InParanoid; Q5R890; -.
DR   OrthoDB; 1046588at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Reference proteome; 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