I5P1_CANLF
ID I5P1_CANLF Reviewed; 412 AA.
AC Q29467;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Inositol polyphosphate-5-phosphatase A;
DE EC=3.1.3.56 {ECO:0000269|PubMed:8198557};
DE AltName: Full=Type I inositol 1,4,5-trisphosphate 5-phosphatase;
DE Short=5PTase;
DE Flags: Precursor;
GN Name=INPP5A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Thyroid;
RX PubMed=8198557; DOI=10.1042/bj3000085;
RA Verjans B., de Smedt F., Lecocq R., Vanweyenberg V., Moreau C., Erneux C.;
RT "Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding
RT a novel inositol 1,4,5-trisphosphate 5-phosphatase.";
RL Biochem. J. 300:85-90(1994).
CC -!- FUNCTION: Phosphatase that specifically hydrolyzes the 5-phosphate of
CC inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate, and inositol
CC 1,3,4,5-tetrasphosphate to inositol 1,3,4-trisphosphate
CC (PubMed:8198557). Plays a crucial role in the survival of cerebellar
CC Purkinje cells (By similarity). {ECO:0000250|UniProtKB:Q7TNC9,
CC ECO:0000269|PubMed:8198557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol
CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282,
CC ChEBI:CHEBI:203600; EC=3.1.3.56;
CC Evidence={ECO:0000269|PubMed:8198557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19798;
CC Evidence={ECO:0000305|PubMed:8198557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56;
CC Evidence={ECO:0000269|PubMed:8198557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393;
CC Evidence={ECO:0000305|PubMed:8198557};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and 2,3-bisphosphoglycerate.
CC {ECO:0000269|PubMed:8198557}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.3 uM for inositol 1,4,5- trisphosphate
CC {ECO:0000269|PubMed:8198557};
CC KM=3.4 uM for inositol 1,3,4,5-tetrasphosphate
CC {ECO:0000269|PubMed:8198557};
CC -!- SUBUNIT: Interacts with TASOR. {ECO:0000250|UniProtKB:Q7TNC9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14642};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q14642}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q7TNC9}.
CC -!- PTM: Isoprenylation at Cys-409 is required for localization at the
CC membrane. {ECO:0000250|UniProtKB:Q14642}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type I family. {ECO:0000305}.
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DR EMBL; X75094; CAA52985.1; -; mRNA.
DR PIR; S44357; S44357.
DR RefSeq; NP_001003257.1; NM_001003257.1.
DR AlphaFoldDB; Q29467; -.
DR STRING; 9612.ENSCAFP00000016395; -.
DR PaxDb; Q29467; -.
DR GeneID; 403937; -.
DR KEGG; cfa:403937; -.
DR CTD; 3632; -.
DR eggNOG; KOG1976; Eukaryota.
DR InParanoid; Q29467; -.
DR OrthoDB; 642737at2759; -.
DR BRENDA; 3.1.3.56; 1153.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IBA:GO_Central.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR039737; INPP5A.
DR InterPro; IPR000300; IPPc.
DR PANTHER; PTHR12997; PTHR12997; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Hydrolase; Lipoprotein; Membrane;
KW Prenylation; Reference proteome.
FT CHAIN 1..409
FT /note="Inositol polyphosphate-5-phosphatase A"
FT /id="PRO_0000209718"
FT PROPEP 410..412
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q14642"
FT /id="PRO_0000396779"
FT LIPID 409
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14642"
SQ SEQUENCE 412 AA; 47683 MW; 5FC100C4E135D545 CRC64;
MAGKAAAPGT AVLLVTANVG SLFDDPENLQ KNWLREFYQV VHTHKPHFMA LHCQEFGGKN
YEASMSHVDK FVKELLSSDA MKEYNRARVY LDENFKSQEH FTALGSFYFL HESLKNIYQF
DFKAKKYKKV TGKEIYSDTL ESTPMLEKEK FPQDYFPECK WSRKGFVRTR WCVADCAFDL
VNIHLFHDAS NLVAWETSPS VYSGIRHKAL GYVLDRIIDQ RFEKVSYFVF GDFNFRLDSK
SVVETLCTKA TMQTVRAADT NEVVKLIFRE SDNDRKVMLQ LEKKLFHYFN QEVFRDNNGT
ALLEFDKELS VFKDRLYELD ISFPPSYPYS EDSGQGRQYM NTRCPAWCDR VLMSPSAREL
ILKSESEEKV VTYDHIGPNV CMGDHKPVFL AFRIAPGAGK PHAHVHKCCV VQ
