ID A0A3B3VSI6_9TELE Unreviewed; 1251 AA.
AC A0A3B3VSI6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase {ECO:0000256|ARBA:ARBA00012981};
DE EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000028750.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000028750.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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: 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 RefSeq; XP_014878056.1; XM_015022570.1.
DR AlphaFoldDB; A0A3B3VSI6; -.
DR STRING; 48699.ENSPLAP00000028750; -.
DR Ensembl; ENSPLAT00000023033.1; ENSPLAP00000028750.1; ENSPLAG00000018457.1.
DR GeneID; 106939971; -.
DR KEGG; plai:106939971; -.
DR CTD; 325179; -.
DR GeneTree; ENSGT00940000156576; -.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000261500; Unplaced.
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:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
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 3: Inferred from homology;
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 SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 19..115
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1185..1249
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 122..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 137920 MW; F05695D6386144A4 CRC64;
MAGGGGGGVS PLGPAPPMWY HRDLSRAAAE ELLARAGRDG SFLVRDSESV NGAYALCVLF
QKHVHTYRIL PDDEGFLAVQ TSQGVQPKRF KTLPELVSLY LQPNQGLVTT LLYAVDREET
AVTDDRDYSD GEDEKPPLPP RSASTSTPPG PETPTESPLA ANGLSTISHE YLKGSYALDL
EAVKQGASSL PHLNKTLVAS CKRLNGEVDK VLSGLEILSK VFDQQSAFMV TKMIQQSVNQ
GGDQELENLV TKLAILKDLL SSIEKKALKA LQDMSLSSPC SPPPFSMRHS KAIPVQAFEV
KLDVYLAELT KIGKSQKYTL SVDVEGGRLV VMKKVKDNQE DWTTFTHDKI RQLIKSQRVQ
NKLGIVFEKE KDKSQRKDFI FASAKKREAF CQLLQLMKNK HSNQDEPDMI SIFIGTWNMG
SVPSPKSVAS WVLCRGLGKT LDEMTVTIPH DLYVFGSQEN SVCDREWVES LRAVLKEQTE
LDYKPIAVQT LWSIKLAVLV KPEHENRISH VGMSSVKTGI ANTLGNKGAV GVSFMFNGTS
FGFVNCHLTS GNEKIARRNQ NYLDILRLLS LGDKQLSSFD ISLRFTHLFW LGDLNYRLDM
DIQEILNYIN RKEFEPLLKV DQLNLEREKN KVFLRFAEEE ISFPPTYRYE RGSRDTYVWQ
KQKATGMRTN VPSWCDRILW KSYPETHIVC NSYGCTDDIV TSDHSPVFGT FEVGVTSQFV
SKKGLPKSSE QAYIEFESIE AIVKTASRTK FFIEFYSTCL EEFKKSYEND SQSSDNVNFL
RVGWSNKQLT TLKPLLSEIE YLQDQHLLLT VKSVDGYESY GECVLALKSM IGSTAQQFHT
YLSHRGEETG NIRGSMRVRV PAERMGTRER LYEWISVDQD ETSGPKGKST MMSRVGHEYV
KQSVVRKQLG ELGKVNEEGE KNCKEENAAR SKQDTPDGES SIGKNSFNNP AYYILEGVPH
PSAAELLSSP TSPTAPPVKA PPPSAGARTK PPPAASGPAH SRRTVVAGHP ARGVSEESSS
EDDGGGATLA GAQGGGIGGT VGSTLNRPPP DFPPPPLPKG ALETAAAEAQ LGKPRSLYPD
LAEVRIPPAG PAGPLVMGDG FRRGAAGALD DQSCSVLQMA KTLSESEFPG QPPRAPSAPP
PVRAPTIGIL DACRTFPPRN PIPESIAEDM PEEALWGSSS SSLSVGESSV GEWLQRLGLE
RYEQGLLHNG WDDLEFLSDI TEEDLEEAGV LDPAHKQILL ESLRQQQQQQ K
//
