ID A0A3P8WGB9_CYNSE Unreviewed; 479 AA.
AC A0A3P8WGB9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000025482.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000025482.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000025482.1}
RP IDENTIFICATION.
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 RefSeq; XP_008320664.1; XM_008322442.2.
DR AlphaFoldDB; A0A3P8WGB9; -.
DR STRING; 244447.ENSCSEP00000025482; -.
DR Ensembl; ENSCSET00000025819.1; ENSCSEP00000025482.1; ENSCSEG00000016261.1.
DR GeneID; 103387684; -.
DR KEGG; csem:103387684; -.
DR GeneTree; ENSGT00390000018409; -.
DR InParanoid; A0A3P8WGB9; -.
DR OMA; RGRSDWC; -.
DR OrthoDB; 1072311at2759; -.
DR Proteomes; UP000265120; Chromosome 12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DISULFID 88..419
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 285..299
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 479 AA; 55088 MW; 371F2F217C34CBEB CRC64;
MTSSVRVLGR NLPELCVIMT PNFWILVVAL LINITGFYCC LYSEEDPDIP VIAKYFTTKG
RYEEVNPHLR DDILFVNRSA LKPPSPQCRE AHLTAVIRHG TRYPTIKNIQ KMRRLYGLVE
SRASGEESWL REIQSQWTMW YTDDMDGRLA MKGVSDHKHL AVRLSKLFPS LLTEEKLRAG
QVNFMTSSKH RCVNSTLSFM AGLTEQWAIR DVEFEHTLND ALMRFFDKCT RFVEEIDKNA
TALAEMQLFK EGPEMRRVQE KIADRLRVPY QSITEEMAEA AFDLCAYEFA IKAVNSPWCC
LFDEVDALVM EYSNDLKQFW KRSYGHDINS KASCILFHDV FSRLDKAANE IKSGQQVTEA
VTIQIGHAET LLPLLTLLGF FRDSEALKST NFAQQAQRSF RTSYMMPYAA NLLLVLYDCG
NGDLRLQALL NEKPVAFPGL TDLTSSMPRY EDVRSHYREL LRGCDFETEC QLFNKPVDS
//
