ID G3T812_LOXAF Unreviewed; 487 AA.
AC G3T812;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000009787.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000009787.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009787.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000009787.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009787.3};
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}.
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DR RefSeq; XP_003409300.1; XM_003409252.2.
DR AlphaFoldDB; G3T812; -.
DR STRING; 9785.ENSLAFP00000009787; -.
DR Ensembl; ENSLAFT00000011712.3; ENSLAFP00000009787.3; ENSLAFG00000011711.3.
DR GeneID; 100661711; -.
DR KEGG; lav:100661711; -.
DR CTD; 9562; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_029165_3_1_1; -.
DR InParanoid; G3T812; -.
DR OMA; ANSPWFA; -.
DR OrthoDB; 1072311at2759; -.
DR TreeFam; TF324072; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 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 3: Inferred from homology;
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:UP000007646};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..487
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003454750"
FT DISULFID 78..422
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 288..302
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 487 AA; 54755 MW; 3D8F5BB9B893B208 CRC64;
MLRGPCGLLR AQVAPAAVLA AALLSSLGRC SFLESGDPVA SALSPYFGTK TRYEDVNPGL
LPNPEAPRRD PELLEGTCTP VQLVAVIRHG TRYPTAKQIR KLRHLHGLLQ ARGPGGGRPR
GTGGRDVGAA LADRPLWYAD WMDGQLVEKG RQDMRQLALR LASLFPALFC PENFGRLRLV
TSSKHRCVDS GAAFLQGLWQ HYHPGLPPPD VADMECGPPR INDKLMRFFD HCKKFLTEVE
SNATALYHVE AFKTGPEMQS ILKKVAATLE VPVNDLNADL IQVAFFTCSF DLAIKDIKSP
WCDVFDIDDA KVLEYLNDLK QYWKRGYGYT INSRSSCILF EDIFQHLDKA VEQKQRSQPI
SSPVILQFGH AETLLPLLSL MGYFKDKEPL TAYNYKEQVH RKFRSGHIVP YASNLIFLLY
HCENAKTAKE EFQVQMLLNE KVLPFAYSQE TVSLYEDLKN HYKDILRSCH ASNECELPKV
NSTSDEL
//
