LOCUS       NP_766027               1003 aa            linear   ROD 28-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 5-phosphatase A [Mus
            musculus].
ACCESSION   NP_766027
VERSION     NP_766027.2
DBSOURCE    REFSEQ: accession NM_172439.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Yu,H., Yong,W., Gao,T., Na,M., Zhang,Y., Kuguminkiriza,I.H.,
            Kenechukwu,A.A., Guo,Q., Zhang,G. and Deng,X.
  TITLE     Hormesis of low-dose inhibition of pAkt1 (Ser473) followed by a
            great increase of proline-rich inositol polyphosphate 5-phosphatase
            (PIPP) level in oocytes
  JOURNAL   In Vitro Cell Dev Biol Anim 57 (3), 342-349 (2021)
   PUBMED   33537929
  REMARK    GeneRIF: Hormesis of low-dose inhibition of pAkt1 (Ser473) followed
            by a great increase of proline-rich inositol polyphosphate
            5-phosphatase (PIPP) level in oocytes.
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Ooms,L.M., Binge,L.C., Davies,E.M., Rahman,P., Conway,J.R.,
            Gurung,R., Ferguson,D.T., Papa,A., Fedele,C.G., Vieusseux,J.L.,
            Chai,R.C., Koentgen,F., Price,J.T., Tiganis,T., Timpson,P.,
            McLean,C.A. and Mitchell,C.A.
  TITLE     The Inositol Polyphosphate 5-Phosphatase PIPP Regulates
            AKT1-Dependent Breast Cancer Growth and Metastasis
  JOURNAL   Cancer Cell 28 (2), 155-169 (2015)
   PUBMED   26267533
REFERENCE   4  (residues 1 to 1003)
  AUTHORS   Ooms,L.M., Fedele,C.G., Astle,M.V., Ivetac,I., Cheung,V.,
            Pearson,R.B., Layton,M.J., Forrai,A., Nandurkar,H.H. and
            Mitchell,C.A.
  TITLE     The inositol polyphosphate 5-phosphatase, PIPP, Is a novel
            regulator of phosphoinositide 3-kinase-dependent neurite elongation
  JOURNAL   Mol Biol Cell 17 (2), 607-622 (2006)
   PUBMED   16280363
REFERENCE   5  (residues 1 to 1003)
  AUTHORS   Gurung,R., Tan,A., Ooms,L.M., McGrath,M.J., Huysmans,R.D.,
            Munday,A.D., Prescott,M., Whisstock,J.C. and Mitchell,C.A.
  TITLE     Identification of a novel domain in two mammalian
            inositol-polyphosphate 5-phosphatases that mediates membrane ruffle
            localization. The inositol 5-phosphatase skip localizes to the
            endoplasmic reticulum and translocates to membrane ruffles
            following epidermal growth factor stimulation
  JOURNAL   J Biol Chem 278 (13), 11376-11385 (2003)
   PUBMED   12536145
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY235850.1, BC131634.1 and BY629401.1.
            
            On Oct 30, 2009 this sequence version replaced NP_766027.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK136908.1, AK034272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 2.45 cM"
     Protein         1..1003
                     /product="phosphatidylinositol 4,5-bisphosphate
                     5-phosphatase A"
                     /EC_number="3.1.3.56"
                     /EC_number="3.1.3.36"
                     /note="proline-rich inositol polyphosphate 5-phosphatase;
                     phosphatidylinositol (4,5) bisphosphate 5-phosphatase, A;
                     phosphatidylinositol 1,4,5-trisphosphate 5-phosphatase;
                     phosphatidylinositol 1,3,4,5-tetrakisphosphate
                     5-phosphatase"
                     /calculated_mol_wt=107414
     Region          1..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          6..11
                     /region_name="RSXSXX motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          <50..337
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            56
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Site            65
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Site            76
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Site            83
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Region          147..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMC1; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Region          346..351
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          351..356
                     /region_name="RSXSXX motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          420..727
                     /region_name="INPP5c_INPP5J-like"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of inositol polyphosphate 5-phosphatase J
                     and related proteins; cd09094"
                     /db_xref="CDD:197328"
     Region          422..725
                     /region_name="Catalytic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Site            order(428,430,462,536..537,557,560..561,600,602,604,
                     655..656,671,677,717..718)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197328"
     Site            order(428,462,557,600,602,677,717..718)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197328"
     Site            order(462,536..537,557,560..561,604,655..656,671,717)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197328"
     Site            order(462,717)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197328"
     Site            order(557,602,718)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197328"
     Region          726..837
                     /region_name="Required for ruffle localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          738..836
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     Region          839..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          871..876
                     /region_name="RSXSXX motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Region          882..887
                     /region_name="RSXSXX motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15735; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     Region          908..913
                     /region_name="RSXSXX motif 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P59644.2)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15735; propagated from
                     UniProtKB/Swiss-Prot (P59644.2)"
     CDS             1..1003
                     /gene="Inpp5j"
                     /gene_synonym="Pib5pa; Pipp"
                     /coded_by="NM_172439.3:74..3085"
                     /db_xref="CCDS:CCDS24364.1"
                     /db_xref="GeneID:170835"
                     /db_xref="MGI:MGI:2158663"
ORIGIN      
        1 megqtrsgsa rpgtrtglgp lpgthgvlqa eipskkvnss fqlpaknsgp asseprltla
       61 pvgpraavsp pserprlvls sprpvlapls iageqkrppp phssnraaks vgqlvvsaaa
      121 askpppvasv silapkslgq lvisasampr pspaplgsvl tptsrdqkql sptsvgpkpa
      181 latsglslal asqeqppqsp sspspvpspv lspsqeghla aasvtstpas erqlparqkd
      241 tavprptppa dkclytpera agpatsppra qafsdprlsp sfrarpeapr hspedpvlpp
      301 ppqtlpldvs pglpesgtrs pgllsptfrp gipssqtvpp plpkpprsps rspsrspnrs
      361 pclppapeva lpkpvtqaag sgrcpspnlq aqespaaatt ttsptsswsa qptcksdpgf
      421 ritvvtwnvg tamppddvts llhlgsghdn dgadmiaigl qevnsminkr lkdalftdqw
      481 selfmdalgp fnfvlvstvr mqgvilllfa kyyhlpflrd vqtdctrtgl ggywgnkggv
      541 svrlaafghm lcflnchlpa hmdkaeqrkd nfqtilslqq fqgpgahgil dhdlvfwfgd
      601 lnfriesydl hfvkfaidsn qlhqlwekdq lnmakntwpi lkgfqegpln faptfkfdvg
      661 tnkydtsakk rkpawtdril wkvkapsggp spsgreshrl qvtqhsyrsh meytvsdhkp
      721 vaaqfilqfa frddvplvrl evadewarpe qavvryrvet vfarsswdwi glyrvgfrhc
      781 kdyvayvwak heevdgniyq vtfseeslpk ghgdfilgyy shhhsiligv tepfqislpt
      841 sesassstds sgtssegedd stlellapks rspspgkskr hrsrspglar fpslalhpss
      901 rerrggsrsp spqsrqlprv apdrghssss rgsseegpsg lpgpwafpps vprslgllpa
      961 lrletvdpgg ggswgadqea pdpnslspsp qgrlgleegg lgp
//
