ID A0A3B5B2D0_9TELE Unreviewed; 1205 AA.
AC A0A3B5B2D0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000026911.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000026911.1}
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 AlphaFoldDB; A0A3B5B2D0; -.
DR Ensembl; ENSSPAT00000027352.1; ENSSPAP00000026911.1; ENSSPAG00000020205.1.
DR GeneTree; ENSGT00940000156576; -.
DR Proteomes; UP000261400; 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 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 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 20..116
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1137..1201
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 120..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 133925 MW; E249A0CAFEA00E42 CRC64;
MAGGGGGGGV SPLGPAPPMW YHRDLSRAAA EELLARAGRD GSFLVRDSES VNGAYALCVL
FQKHVHTYRI LPDDEGFLAV QTSQGVQPKR FKTLPELVSL YLQPSQGLVT TLLYPVDREE
TAISDDRDYS DGEDEKPPLP PRSASTSTPP GPDTPTDSPP AANGLSTISH EYLKGSYALD
LEAVKQGACA LPHLNKTLVA SCKRLNGEVD KVLSGLEILS KVFDQQSAFM VSKMIQQSVN
QGGDQELENL VTKLAILKDL LSSIEKKVRT YSTQICVQIC VKSFSRGPFQ VKLDVYLAEL
TKIGKSQKYT LSVDVEGGRL VVMKKVKDNQ EDWTTFTHDK IRQLIKSQRV QNKLGIVFEK
EKDKSQRKDF IFASAKKREA FCQLLQLMKN KHSNQDEPDM ISIFIGTWNM GSVPSPKSVA
SWVLCRGLGK TLDEMTVTIP HDLYVFGTQE NSVCDREWVE SLRAMLKEQT ELDYKPIAVQ
TLWNIKIAVL VKPEHENRIS HVGMSSVKTG IANTLGNKGA VGVSFMFNGT SFGFVNCHLT
SGNEKIARRN QNYLDILRLL SLGDKQLSSF DISLRFTHLF WLGDLNYRLD MDIQEILNYI
NRKEFEPLLK VDQLNLEREK NKVFLRFAEE EISFPPTYRY ERGSRDTYVW QKQKATGMRT
NVPSWCDRIL WKSYPETHIV CNSYGCTDDI VTSDHSPVFA TFEVGVTSQF VSKKGLPKSS
EQAYIEFESI EAIVKTASRT KFFIEFYSTC LEEFKKSYEN DSQSSDNVNF LRVGWSNKQL
TTLKPLLSEI EYLQDQHLLL TVKSLDGYES YGECVLALKS MIGSTAQQFH TYLSHRGEET
GNIRGSMRVR VPSERMGTRE RLYEWISVDK DETGGPKGKS TMVSRVGHEY VKSVHFSLFS
FCKCKKLNVF KYLILPKQDT ADGDPSICKN SYNNPAYYIL EGVPNQSAAA LSPELLPSPT
SANPQAAKAP PPSAGARTKP PCVGGITVGS TLNRPPPDFP PPPLPKGALE MVAEAPFTKP
RPLYPDLAEV RIPAAGPSAP LPLGEGFRRG GVGGVGAGAL DDQSCSVLQM AKTLSESEFP
GQPPRAPSAP PPLRGQPMGL GLDACRTFPP RNPITESIAE DMPEEALWGS SSSSLSVGES
SVGEWLQRLG LERYEQGLLH NGWDDLEFLS DITEEDLEEA GVLDPAHKRI LLESLRQQQQ
QQQQK
//
