ID A0A3B5PY47_XIPMA Unreviewed; 1198 AA.
AC A0A3B5PY47;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000022944.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000022944.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000022944.1};
RG Ensembl;
RL Submitted (JUL-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; A0A3B5PY47; -.
DR Ensembl; ENSXMAT00000038230.1; ENSXMAP00000022944.1; ENSXMAG00000011097.2.
DR GeneTree; ENSGT00940000156576; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 22..118
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1136..1198
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 125..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 132751 MW; 7BFE579D4706427B CRC64;
MAGGGGGGGG GVSPLGPAPP MWYHRDLSRA AAEELLARAG RDGSFLVRDS ESVNGAYALC
VLFQKHVHTY RILPDEEGFL AVQTSQGVQP KRFKTLPELV SLYLQPNQGL VTTLLYAVDR
EETAVTDDRD YSDGEDEKPP LPPRSASTST PPGPETPTES TLAANGLSTI SHEYLKGSYA
LDLEAVKQGA SSLPHLNKTL VASCKRLNGE VDKVLSGLEI LSKVFDQQSA FMVTKMIQQS
VNQGGDQELE NLVTKLAILR DLLSSIEKKA LKALQDMSLS SPCSPPPFSM RHSKAIPVQA
FEVKLDVYLA ELTKIGKSQK YTLSVDVEGG RLVVMKKVKD NQEDWTTFTH DKIRQLIKSQ
RVQNKLGIVF EKEKDKSQRK DFIFASAKKR EAFCQLLQLM KNKHSNQDEP DMISIFIGTW
NMGSVPSPKS VASWVLCRGL GKTLDEMTVT IPHDLYVFGS QENSVCDREW VESLRAVLKE
QTELDYKPIA VQTLWSIKLA VLVKPEHENR ISHVGMSSVK TGIANTLGIK LIFSSVFHNI
VCLIFCQGNE KIARRNQNYL DILRLLSLGD KQLSSFDISL RFTHLFWLGD LNYRLDMDIQ
EILNYINRKE FEPLLKVDQL NLEREKNKVF LRFAEEEISF PPTYRYERGS RDTYVWQKQK
ATGMRTNVPS WCDRILWKSY PETHIVCNSY GCTDDIVTSD HSPVFGTFEV GVTSQFVSKK
GLPKSSEQAY IEFESIEAIV KTASRTKFFI EFYSTCLEGE SEKSYENDSQ SSDNVNFLRV
GWSNKQLTTL KPLLSEIEYL QDQHLLLTVK SVDGYESYGE CVLALKSMIG STAQQFHTYL
SHRGEETGNI RGSMRVRVPA ERMGTRERLY EWISVDQDET SGPKGKSTMV SRVGHEYVKS
VQLNLPFPPA QHHCLLILKL TQDTPDGDSS IGKNSFNNPA YYILEGVPHP SAAELLSSPT
SPTALPVKAP PPSAGTRTKP PPAASGPAHS RTVGSTLNRP PPDFPPPPLP KGALETAAEA
QLSKPRSLYP DLAEVRIPPA GPAGPLVMGD GFRRGAAGAL DDQSCSVLQM AKTLSESEFP
GQPPRAPSAP PPVRVPTIGI LDACRTFPPR NPIPESIAED MPEEALWGSS SSSLSVGESS
VGEWLQRLGL ERYEPGLLHN GWDDLEFLSD ITEEDLEEAG VLDPAHKQIL LESLSKYG
//