PI5PA_MOUSE
ID PI5PA_MOUSE Reviewed; 1003 AA.
AC P59644; Q3TDM9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A;
DE EC=3.1.3.56;
DE AltName: Full=Inositol polyphosphate 5-phosphatase J;
GN Name=Inpp5j; Synonyms=Pib5pa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF DOMAIN REQUIRED FOR MEMBRANE
RP RUFFLE LOCALIZATION.
RX PubMed=12536145; DOI=10.1074/jbc.m209991200;
RA Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D., Munday A.D.,
RA Prescott M., Whisstock J.C., Mitchell C.A.;
RT "Identification of a novel domain in two mammalian inositol-polyphosphate
RT 5-phosphatases that mediates membrane ruffle localization. The inositol 5-
RT phosphatase SKIP localizes to the endoplasmic reticulum and translocates to
RT membrane ruffles following epidermal growth factor stimulation.";
RL J. Biol. Chem. 278:11376-11385(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-56; ARG-65; ARG-76 AND ARG-83,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Inositol 5-phosphatase, which converts inositol 1,4,5-
CC trisphosphate to inositol 1,4-bisphosphate. Also converts
CC phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-
CC phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-
CC trisphosphate in vitro. May be involved in modulation of the function
CC of inositol and phosphatidylinositol polyphosphate-binding proteins
CC that are present at membranes ruffles (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12536145}.
CC Note=Predominantly localized to membrane ruffles.
CC -!- DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute
CC binding sites for the 14-3-3 protein.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
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DR EMBL; AK034272; BAC28654.1; -; mRNA.
DR EMBL; AK170114; BAE41572.1; -; mRNA.
DR EMBL; BC131634; AAI31635.1; -; mRNA.
DR EMBL; BC131635; AAI31636.1; -; mRNA.
DR EMBL; CH466574; EDL40427.1; -; Genomic_DNA.
DR CCDS; CCDS24364.1; -.
DR RefSeq; NP_766027.2; NM_172439.3.
DR AlphaFoldDB; P59644; -.
DR SMR; P59644; -.
DR BioGRID; 228465; 2.
DR IntAct; P59644; 1.
DR MINT; P59644; -.
DR STRING; 10090.ENSMUSP00000046625; -.
DR iPTMnet; P59644; -.
DR PhosphoSitePlus; P59644; -.
DR MaxQB; P59644; -.
DR PaxDb; P59644; -.
DR PeptideAtlas; P59644; -.
DR PRIDE; P59644; -.
DR ProteomicsDB; 289419; -.
DR Antibodypedia; 5745; 207 antibodies from 30 providers.
DR DNASU; 170835; -.
DR Ensembl; ENSMUST00000044507; ENSMUSP00000046625; ENSMUSG00000034570.
DR GeneID; 170835; -.
DR KEGG; mmu:170835; -.
DR UCSC; uc007hta.2; mouse.
DR CTD; 27124; -.
DR MGI; MGI:2158663; Inpp5j.
DR VEuPathDB; HostDB:ENSMUSG00000034570; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156855; -.
DR HOGENOM; CLU_011711_3_0_1; -.
DR InParanoid; P59644; -.
DR OMA; EWLRPEQ; -.
DR OrthoDB; 772410at2759; -.
DR PhylomeDB; P59644; -.
DR TreeFam; TF317034; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR BioGRID-ORCS; 170835; 5 hits in 76 CRISPR screens.
DR PRO; PR:P59644; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P59644; protein.
DR Bgee; ENSMUSG00000034570; Expressed in cerebellar cortex and 194 other tissues.
DR ExpressionAtlas; P59644; baseline and differential.
DR Genevisible; P59644; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:MGI.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF17751; SKICH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; SH3-binding.
FT CHAIN 1..1003
FT /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
FT A"
FT /id="PRO_0000209739"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..725
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 726..837
FT /note="Required for ruffle localization"
FT REGION 839..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..11
FT /note="RSXSXX motif 1"
FT MOTIF 346..351
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 351..356
FT /note="RSXSXX motif 2"
FT MOTIF 871..876
FT /note="RSXSXX motif 3"
FT MOTIF 882..887
FT /note="RSXSXX motif 4"
FT MOTIF 908..913
FT /note="RSXSXX motif 5"
FT COMPBIAS 33..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 56
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 65
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 76
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 83
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMC1"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15735"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15735"
FT CONFLICT 343
FT /note="P -> R (in Ref. 1; BAC28654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 107544 MW; 3D2E1F6B3D060B4B CRC64;
MEGQTRSGSA RPGTRTGLGP LPGTHGVLQA EIPSKKVNSS FQLPAKNSGP ASSEPRLTLA
PVGPRAAVSP PSERPRLVLS SPRPVLAPLS IAGEQKRPPP PHSSNRAAKS VGQLVVSAAA
ASKPPPVASV SILAPKSLGQ LVISASAMPR PSPAPLGSVL TPTSRDQKQL SPTSVGPKPA
LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQEGHLA AASVTSTPAS ERQLPARQKD
TAVPRPTPPA DKCLYTPERA AGPATSPPRA QAFSDPRLSP SFRARPEAPR HSPEDPVLPP
PPQTLPLDVS PGLPESGTRS PGLLSPTFRP GIPSSQTVPP PLPKPPRSPS RSPSRSPNRS
PCLPPAPEVA LPKPVTQAAG SGRCPSPNLQ AQESPAAATT TTSPTSSWSA QPTCKSDPGF
RITVVTWNVG TAMPPDDVTS LLHLGSGHDN DGADMIAIGL QEVNSMINKR LKDALFTDQW
SELFMDALGP FNFVLVSTVR MQGVILLLFA KYYHLPFLRD VQTDCTRTGL GGYWGNKGGV
SVRLAAFGHM LCFLNCHLPA HMDKAEQRKD NFQTILSLQQ FQGPGAHGIL DHDLVFWFGD
LNFRIESYDL HFVKFAIDSN QLHQLWEKDQ LNMAKNTWPI LKGFQEGPLN FAPTFKFDVG
TNKYDTSAKK RKPAWTDRIL WKVKAPSGGP SPSGRESHRL QVTQHSYRSH MEYTVSDHKP
VAAQFILQFA FRDDVPLVRL EVADEWARPE QAVVRYRVET VFARSSWDWI GLYRVGFRHC
KDYVAYVWAK HEEVDGNIYQ VTFSEESLPK GHGDFILGYY SHHHSILIGV TEPFQISLPT
SESASSSTDS SGTSSEGEDD STLELLAPKS RSPSPGKSKR HRSRSPGLAR FPSLALHPSS
RERRGGSRSP SPQSRQLPRV APDRGHSSSS RGSSEEGPSG LPGPWAFPPS VPRSLGLLPA
LRLETVDPGG GGSWGADQEA PDPNSLSPSP QGRLGLEEGG LGP
