ID U3F258_CALJA Unreviewed; 1263 AA.
AC U3F258; F6WC23;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 {ECO:0000256|ARBA:ARBA00034348};
DE EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
DE AltName: Full=Inositol polyphosphate phosphatase-like protein 1 {ECO:0000256|ARBA:ARBA00034353};
DE AltName: Full=Protein 51C {ECO:0000256|ARBA:ARBA00034368};
DE AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2 {ECO:0000256|ARBA:ARBA00034357};
GN Name=INPPL1 {ECO:0000313|EMBL:JAB49219.1,
GN ECO:0000313|Ensembl:ENSCJAP00000028033.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB49219.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000028033.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB49219.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB04768.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB49219.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB17890.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB38681.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000028033.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-
CC 3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate;
CC Xref=Rhea:RHEA:43556, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83420, ChEBI:CHEBI:83422;
CC Evidence={ECO:0000256|ARBA:ARBA00034236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43557;
CC Evidence={ECO:0000256|ARBA:ARBA00034236};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83417; Evidence={ECO:0000256|ARBA:ARBA00034246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43549;
CC Evidence={ECO:0000256|ARBA:ARBA00034246};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000256|ARBA:ARBA00023377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000256|ARBA:ARBA00023377};
CC -!- SUBCELLULAR LOCATION: Basal cell membrane
CC {ECO:0000256|ARBA:ARBA00034304}. Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus speckle
CC {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000256|ARBA:ARBA00008734}.
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DR EMBL; GAMT01007093; JAB04768.1; -; mRNA.
DR EMBL; GAMS01005246; JAB17890.1; -; mRNA.
DR EMBL; GAMQ01003170; JAB38681.1; -; mRNA.
DR EMBL; GAMP01003536; JAB49219.1; -; mRNA.
DR STRING; 9483.ENSCJAP00000028033; -.
DR Ensembl; ENSCJAT00000029621.5; ENSCJAP00000028033.3; ENSCJAG00000015191.6.
DR GeneTree; ENSGT00940000156576; -.
DR HOGENOM; CLU_007493_1_1_1; -.
DR OMA; TERMGTR; -.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000008225; Chromosome 11.
DR Bgee; ENSCJAG00000015191; Expressed in kidney and 6 other cell types or tissues.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR CDD; cd09101; INPP5c_SHIP2-INPPL1; 1.
DR CDD; cd09491; SAM_Ship2; 1.
DR CDD; cd10343; SH2_SHIP; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR46051:SF2; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 5-PHOSPHATASE 2; 1.
DR PANTHER; PTHR46051; SH2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 26..122
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1209..1263
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 124..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 139017 MW; EE60F7677FF51C26 CRC64;
MASACGVPGP GGVAPGGALG SQAPAWYHRD LSRAAAEELL ARAGRDGSFL VRDSESVAGA
FALCVLYQKH VHTYRILPDG EDFLAVQTSQ GVPVRRFQTL GELIGLYAQP NQGLVCALLL
PVEGEREPDP PDDRDASDGE DEKPPLPPRS GSTSISAHTG PSSPLPTPET PTTPAAESAP
NGLSTVSHEY LKGSYGLDLE AVRGGASHLP HLTRTLATSC RRLHSEVDKV LSGLEILSKV
FDQQSSPMVT RLLQQQNLPQ TGEQELESLV LKLSVLKDFL SGIQKKALKA LQDMSSTAPP
ALQPSTRKAK TIPVQAFEVK LDVTLGDLTK IGKSQKFTLS VDVEGGRLVL LRRQRDSQED
WTTFTHDRIR QLIKSQRVQN KLGVVFEKEK DRTQRKDFIF VSARKREAFC QLLQLMKNKH
SKQDEPDMIS VFIGTWNMGS VPPPKNVTSW FTSKGLGKTL DEVTVTIPHD IYVFGTQENS
VGDREWLDLL RGGLKELTDL DYRPIAMQSL WNIKVAVLVK PEHENRISHV STSSVKTGIA
NTLGNKGAVG VSFMFNGTSF GFVNCHLTSG SEKTARRNQN YLDILRLLSL GDRQLSAFDI
SLRFTHLFWF GDLNYRLDMD IQEILNYISR KEFEPLLRVD QLNLEREKHK VFLRFSEEEI
SFPPTYRYER GSRDTYAWHK QKPTGVRTNV PSWCDRILWK SYPETHVICN SYGCTDDIVS
SDHSPVFGTF EVGVTSQFIS KKGLSKTSDQ AYIEFESIEA IVKTASRTKF FIEFYSTCLE
EYKKSFENDA QSSDNINFLK VQWSSRQLPT LKPILADIEY LQDQHLLLTV KSMDGYESYG
ECVVALKSMI GSTAQQFLTF LSHRGEETGN IRGSMKVRVP TERLGTRERL YEWISIDKDE
AGAKSKVPSV SRGSQEPRSG SRKPAFTEAS CPLSRLFEEP DKPPPTGRPP APPRTAAREE
PLTPRLKPEG APEPEGLAAP PPKNSFNNPA YYVLEGVPHQ LLPPEPPSPA RAPVPPATKN
KVAITVPAPQ LGRHRPPRVG EGSSSDEESG GTLPPPDFPP PPLPDSAIFL PPSLDPLPGP
VVRGRGGADA RGPPPPKAHP RPPLPPGPSP SSTFLGEVAS GDDRSCSVLQ MAKTLSEVDY
APAGPARSAL LPGPLELQPP RGLPSDYGRP LSFPPPRIRE SIQEDLAEEA PCPQGGRASG
LGEAGMGAWL RAIGLERYEE GLVHNGWDDL EFLSDITEED LEEAGVQDPA HKRLLLDTLQ
LSK
//
