I5P1_RAT
ID I5P1_RAT Reviewed; 412 AA.
AC D3ZZX1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Inositol polyphosphate-5-phosphatase A;
DE EC=3.1.3.56 {ECO:0000269|PubMed:8626616};
DE AltName: Full=Type I inositol 1,4,5-trisphosphate 5-phosphatase;
DE Short=5PTase;
DE Flags: Precursor;
GN Name=Inpp5a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8626616; DOI=10.1074/jbc.271.17.10419;
RA De Smedt F., Boom A., Pesesse X., Schiffmann S.N., Erneux C.;
RT "Post-translational modification of human brain type I inositol-1,4,5-
RT trisphosphate 5-phosphatase by farnesylation.";
RL J. Biol. Chem. 271:10419-10424(1996).
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:8626616). Plays a crucial role in the survival of cerebellar
CC Purkinje cells (By similarity). {ECO:0000250|UniProtKB:Q7TNC9,
CC ECO:0000269|PubMed:8626616}.
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:8626616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19798;
CC Evidence={ECO:0000305|PubMed:8626616};
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:8626616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393;
CC Evidence={ECO:0000305|PubMed:8626616};
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:0000269|PubMed:8626616}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellar Purkinje cells (at protein
CC level). {ECO:0000269|PubMed:8626616}.
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; AABR07005980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07005981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07005982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07005983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473953; EDM11850.1; -; Genomic_DNA.
DR RefSeq; NP_001102393.1; NM_001108923.2.
DR AlphaFoldDB; D3ZZX1; -.
DR STRING; 10116.ENSRNOP00000051774; -.
DR PhosphoSitePlus; D3ZZX1; -.
DR SwissPalm; D3ZZX1; -.
DR PaxDb; D3ZZX1; -.
DR PeptideAtlas; D3ZZX1; -.
DR Ensembl; ENSRNOT00000054890; ENSRNOP00000051774; ENSRNOG00000017635.
DR GeneID; 365382; -.
DR KEGG; rno:365382; -.
DR UCSC; RGD:1306168; rat.
DR CTD; 3632; -.
DR RGD; 1306168; Inpp5a.
DR eggNOG; KOG1976; Eukaryota.
DR GeneTree; ENSGT00390000015226; -.
DR HOGENOM; CLU_057709_1_0_1; -.
DR InParanoid; D3ZZX1; -.
DR OMA; GDHKPVM; -.
DR OrthoDB; 642737at2759; -.
DR PhylomeDB; D3ZZX1; -.
DR TreeFam; TF314246; -.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000017635; Expressed in heart and 20 other tissues.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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:0042731; F:PH domain binding; ISO:RGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:RGD.
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_0000451146"
FT PROPEP 410..412
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q14642"
FT /id="PRO_0000451147"
FT LIPID 409
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14642"
SQ SEQUENCE 412 AA; 47622 MW; 1304F5691FA9832B CRC64;
MAGKAAAPGT AVLLVTANVG SLFDDPENLQ KNWLREFYQV LHTHKPHFMA LHCQEFGGKN
YEASMSHVDK FVKELLSSDA MKEYNRARVY LDENYKSQEH FTALGSFYFL HESLKNIYQF
DFKAKKYKKV TGKEIYSDTL ESTPMLEKEK FPQDYFPECK WSRKGFIRTR WCIADCAFDL
VNIHLFHDAS NLVAWETSPS VYSGVRHKAL GYVLDRIIDQ RFEKVSYFVF GDFNFRLDSK
SVVETLCTKA TMQTVRAADT NEVVKLIFRE SDNDRKVVLQ LEKKLFDYFN QDVFRDNNGT
ALLEFDKELS VFKDRLYELD ISFPPSYPYS EDSSQGEQYM NTRCPAWCDR ILMSLSAKEL
VLKSESEEKV ATYDHIGPNV CMGDHKPVFL AFRIAPGAGK PHAHVHKCCV VQ
