PI5PA_RAT
ID PI5PA_RAT Reviewed; 1001 AA.
AC Q9JMC1;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A;
DE EC=3.1.3.56;
DE AltName: Full=Inositol polyphosphate 5-phosphatase J;
DE AltName: Full=Proline-rich inositol polyphosphate 5-phosphatase;
GN Name=Inpp5j; Synonyms=Pib5pa, Pipp;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP ENZYME ACTIVITY.
RC TISSUE=Brain;
RX PubMed=10593988; DOI=10.1074/jbc.274.51.36790;
RA Mochizuki Y., Takenawa T.;
RT "Novel inositol polyphosphate 5-phosphatase localizes at membrane
RT ruffles.";
RL J. Biol. Chem. 274:36790-36795(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-15 AND 903-917, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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:10593988};
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:10593988};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10593988}.
CC Note=Predominantly localized to membrane ruffles.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, kidney, stomach, small
CC intestine and lung. Not expressed in spleen, thymus, skeletal muscle,
CC testis and skin. {ECO:0000269|PubMed:10593988}.
CC -!- DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute
CC binding sites for the 14-3-3 protein.
CC -!- PTM: Phosphorylated on Ser/Thr residues.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
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DR EMBL; AB032551; BAA90553.1; -; mRNA.
DR RefSeq; NP_598246.1; NM_133562.1.
DR AlphaFoldDB; Q9JMC1; -.
DR SMR; Q9JMC1; -.
DR STRING; 10116.ENSRNOP00000026293; -.
DR iPTMnet; Q9JMC1; -.
DR PhosphoSitePlus; Q9JMC1; -.
DR PaxDb; Q9JMC1; -.
DR PRIDE; Q9JMC1; -.
DR GeneID; 171088; -.
DR KEGG; rno:171088; -.
DR UCSC; RGD:620541; rat.
DR CTD; 27124; -.
DR RGD; 620541; Inpp5j.
DR VEuPathDB; HostDB:ENSRNOG00000019361; -.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_011711_3_0_1; -.
DR InParanoid; Q9JMC1; -.
DR OMA; EWLRPEQ; -.
DR OrthoDB; 772410at2759; -.
DR PhylomeDB; Q9JMC1; -.
DR TreeFam; TF317034; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:Q9JMC1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000019361; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q9JMC1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
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:MGI.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
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; Direct protein sequencing; Hydrolase; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..1001
FT /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
FT A"
FT /id="PRO_0000209740"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..723
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 724..835
FT /note="Required for ruffle localization"
FT /evidence="ECO:0000250"
FT REGION 837..1001
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 869..874
FT /note="RSXSXX motif 3"
FT MOTIF 880..885
FT /note="RSXSXX motif 4"
FT MOTIF 906..911
FT /note="RSXSXX motif 5"
FT COMPBIAS 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar 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 383..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 56
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 65
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 76
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 83
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15735"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15735"
SQ SEQUENCE 1001 AA; 107208 MW; 7BE7741FEF8F3FAB CRC64;
MEGQSRSGSA KSGTRTGLGP LPGTHGALQT GTPSKKVNSS FQLPAKNTGP TPSEPRLALA
PVGPRAAVSP PSERPRLALS SPRPILAPLS TAGEQKRPPP HRSSKPAPTS VGQLVVSAAA
GPKPPPVASV SILAPKSLGQ LVISASAMPR PTPAPLGPIL SPTSRDQKQL SPTSVGPKPA
LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQESHLA PATVTSTPAS ERQLPARQKD
TAVRRPIPPA DGCLHTPVQA AGLATSPPRA QTSSDPRLSP SFRARPEAPR HSPEDPVLPP
PPQTLPLDVS SGLPESGTRS PGLLSPTFRP GIPSNQTVPP PLPKPPRSPS RSPSRSPNRS
PCVPPAPEVA LPRPVTQGAG PGKCPSPNLQ TQESPVATAT SPTSSWSAQP TCKSDPGFRI
TVVTWNVGTA MPPDDVTSLL HLGGGHDSDG ADMIAIGLQE VNSMINKRLK DALFTDQWSE
LFMDALGPFN FVLVSTVRMQ GVILLLFAKY YHLPFLRDVQ TDCTRTGLGG YWGNKGGVSV
RLAAFGHMLC FLNCHLPAHM DKAEQRKDNF QTILSLQQFQ GPGAHGILDH DLVFWFGDLN
FRIESYDLHF VKFAIDSNQL HQLWEKDQLN MAKNTWPILK GFQEGPLNFA PTFKFDVGTN
KYDTSAKKRK PAWTDRILWK VKAPSGGPSP SGRESHRLQV TQHSYRSHME YTVSDHKPVA
ARFLLQFAFR DDVPLVRLEV ADEWARPEQA VVRYRVETVF ARSSWDWIGL YRVGFRHCKD
YVAYVWAKHE EVDGNIYQVT FSEESLPKGH GDFILGYYSH HHSILIGVTE PFQISLPTSE
SASSSTDSSG TSSEGEDDST LELLAPKSRS PSPGKSKRHR SRSPGLARFP SLALRPSSRE
RRGGSRSPSP QSRQLPRVAP DRGHSSGSRG SSEEGPSGPP GPWAFPPAVP RSLGLLPALR
LETVDPGGGG SWGPDQEAPD PNSLSPSPQG RLGLEDGGLG P
