GenomeNet

Database: UniProt
Entry: U3E199_CALJA
LinkDB: U3E199_CALJA
Original site: U3E199_CALJA 
ID   U3E199_CALJA            Unreviewed;       491 AA.
AC   U3E199; A0A5F4WGI8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000256|ARBA:ARBA00018097};
DE            EC=3.1.3.62 {ECO:0000256|ARBA:ARBA00013040};
DE            EC=3.1.3.80 {ECO:0000256|ARBA:ARBA00012976};
DE   AltName: Full=2,3-bisphosphoglycerate 3-phosphatase {ECO:0000256|ARBA:ARBA00031642};
GN   Name=MINPP1 {ECO:0000313|EMBL:JAB44753.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000076739.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB44753.1};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000076739.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB44753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:JAB44753.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB26020.1}, and Hippocampus
RC   {ECO:0000313|EMBL:JAB17079.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000076739.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00043832};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382;
CC         Evidence={ECO:0000256|ARBA:ARBA00043832};
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:0000256|ARBA:ARBA00043757};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77112;
CC         Evidence={ECO:0000256|ARBA:ARBA00043757};
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:0000256|ARBA:ARBA00043739};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77124;
CC         Evidence={ECO:0000256|ARBA:ARBA00043739};
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:0000256|ARBA:ARBA00043733};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77128;
CC         Evidence={ECO:0000256|ARBA:ARBA00043733};
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:0000256|ARBA:ARBA00043671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000256|ARBA:ARBA00043671};
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:0000256|ARBA:ARBA00043668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000256|ARBA:ARBA00043668};
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:0000256|ARBA:ARBA00043747};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC         Evidence={ECO:0000256|ARBA:ARBA00043747};
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:0000256|ARBA:ARBA00043674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC         Evidence={ECO:0000256|ARBA:ARBA00043674};
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:0000256|ARBA:ARBA00043762};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144;
CC         Evidence={ECO:0000256|ARBA:ARBA00043762};
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:0000256|ARBA:ARBA00043829};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77148;
CC         Evidence={ECO:0000256|ARBA:ARBA00043829};
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:0000256|ARBA:ARBA00043801};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77140;
CC         Evidence={ECO:0000256|ARBA:ARBA00043801};
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:0000256|ARBA:ARBA00043746};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20961;
CC         Evidence={ECO:0000256|ARBA:ARBA00043746};
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:0000256|ARBA:ARBA00043691};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000256|ARBA:ARBA00043691};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008422}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GAMS01006057; JAB17079.1; -; mRNA.
DR   EMBL; GAMR01007912; JAB26020.1; -; mRNA.
DR   EMBL; GAMP01008002; JAB44753.1; -; mRNA.
DR   RefSeq; XP_017834604.1; XM_017979115.1.
DR   Ensembl; ENSCJAT00000092563.2; ENSCJAP00000076739.2; ENSCJAG00000005222.5.
DR   GeneTree; ENSGT00390000018409; -.
DR   HOGENOM; CLU_029165_3_1_1; -.
DR   OMA; ANSPWFA; -.
DR   OrthoDB; 1072311at2759; -.
DR   Proteomes; UP000008225; Chromosome 12.
DR   Bgee; ENSCJAG00000005222; Expressed in ovary and 6 other cell types or tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0030351; F:inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity; IEA:Ensembl.
DR   GO; GO:0030352; F:inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity; IEA:Ensembl.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IEA:Ensembl.
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.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DISULFID        78..426
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        288..302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   491 AA;  55511 MW;  BB58203CCFA6C72F CRC64;
     MLRAPRCLLR ISVAPAAALA AALLSSFARC SLLEPRDPVA SSLSPYFGTK TRYEDVNPGL
     LSGPEAPWRD PELLEGTCTP VQLVALIRHG TRYPTAKQIR KLKQLHGLLQ ARGSREGGAG
     STGSRDLGAA LADWPLWYAD WMDGQLVEKG RQDMRQLALR LASLFPALFS LENYGRLRLI
     TSSKHRCVDS GAAFLQGLWQ HYYPGLPPPD VADMECGPPR VNDKLMRFFD HCEKFLTEVE
     RNATALYHVE AFKTGPEMQN ILKKVSATLE VPVNDLNADL IQVAFFTCSF DLAIKGIKSP
     WCDVFDIDDA KKKGEVLEYL NDLKQYWKRG YGYTINSRSS CTLFQDIFQH LDKAVEQKQR
     SQPVSSPVIL QFGHAETLLP LLSLMGYFKD KEPLTAYNYK EQMHRKFRSG HIVPYASNLI
     FVLYYCENAK TPKEQFRVQM LLNEKVLPLA YSQETVSFYD DLKNHYKDIL QSCQTSEECE
     LAKANSTSDE L
//
DBGET integrated database retrieval system