ID A0A3P9PH46_POERE Unreviewed; 457 AA.
AC A0A3P9PH46;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000021172.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000021172.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000021172.1};
RG Ensembl;
RL Submitted (SEP-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 1,2,4,5,6-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 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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008422}.
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DR AlphaFoldDB; A0A3P9PH46; -.
DR Ensembl; ENSPRET00000021397.1; ENSPREP00000021172.1; ENSPREG00000014288.1.
DR GeneTree; ENSGT00390000018409; -.
DR OMA; LPGCDGE; -.
DR Proteomes; UP000242638; 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:SF41; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..457
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018068230"
FT DISULFID 66..397
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 268..282
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 457 AA; 52880 MW; BF7AA79762AC91DE CRC64;
MMFFHFYCFI IFCCVHCHVA LKDEESIPPI AMYFNTKGRY EEVNPYLRQD ILAVNRSSLQ
PPSSQCREIH LTAIIRHGTR YPTAKTVRDM QQLHNIVLNN FTEEQSWLRE TLTQWTMWYT
EDMDGRLVQK GVEDLKHLAV RLSKLFPTII SEEKLRGGLI KFITSSKHRC VNSTLSFKAG
LTEMWLFVHA DVEFGHEVND ALMRFFDHCT RFVQEVDKNS SAVIEVDRFK QGLEMMRVQK
KIADPRDHVT DHLYVSLTDL AEAAFLLCTY ELAVKAVNSP WCLLFDEDNA KVMEYASDLR
EFWKRGYGHD INSKSSCILF HDLFNNSSLW LHQQVTEVVS VQIGHADTLL PLLTLLGFFK
DAVPLTSANY ASQAQRSFRT SRMLPYAANF LLVLYDCGEE GIRLQPLLNE KPLTFPGLTD
QQASMPLYED VRKHYRFLLS GCDFEAECQL LRNPAEV
//
