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Database: UniProt
Entry: A0A3B5PY47_XIPMA
LinkDB: A0A3B5PY47_XIPMA
Original site: A0A3B5PY47_XIPMA 
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
//
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