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Database: UniProt
Entry: M3Y1Q0_MUSPF
LinkDB: M3Y1Q0_MUSPF
Original site: M3Y1Q0_MUSPF 
ID   M3Y1Q0_MUSPF            Unreviewed;      1188 AA.
AC   M3Y1Q0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase {ECO:0000256|ARBA:ARBA00012981};
DE            EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
GN   Name=INPP5D {ECO:0000313|Ensembl:ENSMPUP00000005251.1,
GN   ECO:0000313|RefSeq:XP_004773560.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005251.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000005251.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004773560.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004773560.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC       family. {ECO:0000256|ARBA:ARBA00008734}.
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DR   EMBL; AEYP01081415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01081416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01081417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01081418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01081419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01081420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004773560.1; XM_004773503.3.
DR   STRING; 9669.ENSMPUP00000005251; -.
DR   Ensembl; ENSMPUT00000005339.1; ENSMPUP00000005251.1; ENSMPUG00000005289.1.
DR   GeneID; 101689592; -.
DR   KEGG; mpuf:101689592; -.
DR   CTD; 3635; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   GeneTree; ENSGT00940000156202; -.
DR   HOGENOM; CLU_007493_0_0_1; -.
DR   OMA; DSWFQCK; -.
DR   OrthoDB; 21647at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR   GO; GO:0050777; P:negative regulation of immune response; IEA:Ensembl.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045659; P:negative regulation of neutrophil differentiation; IEA:Ensembl.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:Ensembl.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR   CDD; cd09100; INPP5c_SHIP1-INPP5D; 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   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR46051:SF3; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 5-PHOSPHATASE 1; 1.
DR   PANTHER; PTHR46051; SH2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
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:UP000000715};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT   DOMAIN          5..101
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          103..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  133031 MW;  0707C10F213E649B CRC64;
     MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED
     DKFTVQASEG VPMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEEAGD EPEEETEGVL
     SPPELPPRNI PLFAGPCETK DVPLSSENVR ATEVSKPSLS ETLFQRLQSM DTSGLPEEHL
     KAIQDYLSTQ LALDSDFVKT GSSSLPHLKK LTTLLCKELY GEVLRTLPSL ESLQRLFDQQ
     LSPGLRPRPQ VPGEANPVNM VAKLSQLTSL LSSIEDKVKA LLHEGAESPH RRSLIPPVTF
     EVKSESLGIP QKLQLKVDVE SGKLIMKKGK DGSEDKFYPH NKILQLIKSQ KFLNKLVILV
     ETEKEKTLRK EYVFADSKKR EGFCQLLQQM KNKHSEQPEP DMITIFIGTW NMGNAPPPKK
     ITSWFLSKGQ GKTRDDSADY IPHDIYVIGT QEDPLGEKEW LEILKHSLQE ITSMTFKTIA
     IHTLWNIRIV VLAKPEHENR ISHICTDNVK TGIANTLGNK GAVGVSFMFN GTSLGFVNSH
     LTSGSEKKLR RNQNYMSILR FLALGDKKLS PFNITHRFTH LFWLGDLNYR VELPTWEAET
     IVQKIKQQQY ADLLSHDQLL MERKEQKVFL HFEEEEITFA PTYRFERLTR DKYAYTKQKA
     TGMKYNLPSW CDRVLWKSYP LVHVVCQSYG STSDIMTSDH SPVFATFEAG VTSQFVSKNG
     PGTVDSQGQI EFLRCFATLK TKSQTKFYLE FHSSCLESFV KSQEGENEEG SEGELVVKFG
     ETLPKLKPII SDPEYLLDQH ILISIKSSDS DESYGEGCIA LRLEATETQL PIYTPLTHHG
     EMTGHFRGEI KLQTSQGKMR EKLYDFVKTE RDESSGPKSL KSLTSHDPMK QWEPANRVPS
     SGSSSITEII NPNYIGVVPF GHMKQSLSPD QQPTAWSYDQ PLKDSSLGPG RGDSPPTPPS
     QPPVSPKKFS SSTATRVPCP RTQESRSCDV GKNPAEPSPP EDAQLTKPEM FENPLYGSVS
     SFPKPLPRKE QESPKMLRKE ALPCPDPGIV SPSILLPKAQ EAEGNKGTGK PTPTPFLSPT
     PRLRSFTCSS SAEGRPAGGD KSQGKAKAPA SLHAQVPAKR PIKPSRSELS PQAPPPPPLA
     QRPPLPVKSP AVLHLQHSKG RDYRENAELP HHGKHRPEDA PLSRAAMQ
//
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