ID A0A3L8SMR5_CHLGU Unreviewed; 438 AA.
AC A0A3L8SMR5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=DV515_00006182 {ECO:0000313|EMBL:RLW04058.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW04058.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW04058.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW04058.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW04058.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW04058.1}.
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; QUSF01000014; RLW04058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SMR5; -.
DR STRING; 44316.ENSEGOP00005021774; -.
DR Proteomes; UP000276834; 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; 2.
DR PIRSF; PIRSF000894; Acid_phosphatase; 2.
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:UP000276834};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..438
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018039122"
FT DISULFID 59..372
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 438 AA; 49268 MW; DB789E5DE1E52B70 CRC64;
MAPRREAALL LLLLVLPPAS AGLSDYFGTK SRYEEVNPYL VSDPLSLGPE AGGSLPASCT
PLQLRAVLRH GTRYPTAGQI RRLGELHARL LRRAAAAAAC PAAVALADWP MWYEESLDGQ
LAPQGRRDME QLARRMAARF PALFAARRRL QLASSSKHRC LQSGAAFRRG LGPSLDFGGD
EVEIEVNDFL MRFFDHCAKF VAMVEENDKA MCQVTAFKEG PEMKKVLEKV ASALCLPVEE
LNAVRLLRKS APLGKEETIA WVLEYLNDLK QYWKRGYGYD INSRSSCVLF QDIFQHLDKA
VEESKSSKPI SSPLIVQVGH AETLQPLLAL MGYFKDDEPL LASNYAQQAQ RKFRTGRIVP
YAANLVFVLY HCDHVNTSQE EYQVQLLLNE KLLPFHHSNE TISTYTDLKN YYKDILENCH
FKEECELSQV NVTVVDEL
//
