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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1)

 SHIP1_RAT               Reviewed;        1190 AA.
P97573;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
23-MAY-2018, entry version 110.
RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;
EC=3.1.3.86;
AltName: Full=SH2 domain-containing inositol 5'-phosphatase 1;
Short=SH2 domain-containing inositol phosphatase 1;
Short=SHIP-1;
Name=Inpp5d; Synonyms=Ship, Ship1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, PHOSPHORYLATION, AND
INTERACTION WITH MS4A2; SHC1; GRB2 AND FCER1G.
PubMed=8910587; DOI=10.1074/jbc.271.46.29271;
Osborne M.A., Zenner G., Lubinus M., Zhang X., Songyang Z.,
Cantley L.C., Majerus P., Burn P., Kochan J.P.;
"The inositol 5'-phosphatase SHIP binds to immunoreceptor signaling
motifs and responds to high affinity IgE receptor aggregation.";
J. Biol. Chem. 271:29271-29278(1996).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; THR-963 AND
SER-971, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that
specifically hydrolyzes the 5-phosphate of phosphatidylinositol-
3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2,
thereby negatively regulating the PI3K (phosphoinositide 3-kinase)
pathways. Acts as a negative regulator of B-cell antigen receptor
signaling. Mediates signaling from the FC-gamma-RIIB receptor
(FCGR2B), playing a central role in terminating signal
transduction from activating immune/hematopoietic cell receptor
systems. Acts as a negative regulator of myeloid cell
proliferation/survival and chemotaxis, mast cell degranulation,
immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in
platelets and JNK signaling in B-cells. Regulates proliferation of
osteoclast precursors, macrophage programming, phagocytosis and
activation and is required for endotoxin tolerance. Involved in
the control of cell-cell junctions, CD32a signaling in neutrophils
and modulation of EGF-induced phospholipase C activity. Key
regulator of neutrophil migration, by governing the formation of
the leading edge and polarization required for chemotaxis.
Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates
the activin/TGF-beta-induced apoptosis through its Smad-dependent
expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus
affect the levels of the higher inositol polyphosphates like InsP6
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,4,5-
triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-
diphosphate + phosphate. {ECO:0000269|PubMed:8910587}.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane. {ECO:0000250}.
-!- SUBUNIT: Interacts with tyrosine phosphorylated forms of SHC1
(PubMed:8910587). Interacts with tyrosine phosphorylated form of
DOK1 (By similarity). Interacts with tyrosine phosphorylated form
of DOK3 (By similarity). Interacts with tyrosine phosphorylated
form of SLAMF1/CD150 (By similarity). Interacts with PTPN11/SHP-2
in response to IL-3 (By similarity). Interacts with receptor EPOR
(By similarity). Interacts with receptors MS4A2/FCER1B and FCER1G
(PubMed:8910587). Interacts with receptors FCGR2B and FCGR3 (By
similarity). Interacts with receptor FCGR2A, leading to regulate
gene expression during the phagocytic process (By similarity).
Interacts with GRB2 (PubMed:8910587). Interacts with PLCG1 (By
similarity). Interacts with tyrosine kinases SRC and TEC (By
similarity). Interacts with c-Met/MET (By similarity). Interacts
with MILR1 (tyrosine-phosphorylated) (By similarity). Can weakly
interact (via NPXY motif 2) with DAB2 (via PID domain); the
interaction is impaired by tyrosine phosphorylation of the NPXY
motif (By similarity). {ECO:0000250|UniProtKB:Q92835,
ECO:0000250|UniProtKB:Q9ES52, ECO:0000269|PubMed:8910587}.
-!- INTERACTION:
Q96RU3:FNBP1 (xeno); NbExp=2; IntAct=EBI-8008869, EBI-1111248;
Q15642-1:TRIP10 (xeno); NbExp=2; IntAct=EBI-8008869, EBI-16191375;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES52}.
Cell membrane {ECO:0000250|UniProtKB:Q9ES52}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q9ES52}. Membrane raft
{ECO:0000250|UniProtKB:Q9ES52}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9ES52}. Note=Translocates to the plasma
membrane when activated, translocation is probably due to
different mechanisms depending on the stimulus and cell type.
Translocates from the cytoplasm to membrane ruffles in a
FCGR3/CD16-dependent manner. Colocalizes with FC-gamma-RIIB
receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles. Tyrosine
phosphorylation may also participate in membrane localization.
{ECO:0000250|UniProtKB:Q9ES52}.
-!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with
that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras
pathway. It is also required for tyrosine phosphorylation (By
similarity). {ECO:0000250}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-
phosphorylated proteins is required for the specific binding of
the PID domain. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by the members of the SRC family
after exposure to a diverse array of extracellular stimuli such as
cytokines, growth factors, antibodies, chemokines, integrin
ligands and hypertonic and oxidative stress. Phosphorylated upon
IgG receptor FCGR2B-binding. {ECO:0000269|PubMed:8910587}.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
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EMBL; U55192; AAB40610.1; -; mRNA.
RefSeq; NP_062184.1; NM_019311.1.
UniGene; Rn.10659; -.
ProteinModelPortal; P97573; -.
SMR; P97573; -.
BioGrid; 248482; 6.
DIP; DIP-42709N; -.
IntAct; P97573; 4.
MINT; P97573; -.
STRING; 10116.ENSRNOP00000040111; -.
iPTMnet; P97573; -.
PhosphoSitePlus; P97573; -.
PaxDb; P97573; -.
PRIDE; P97573; -.
GeneID; 54259; -.
KEGG; rno:54259; -.
UCSC; RGD:2914; rat.
CTD; 3635; -.
RGD; 2914; Inpp5d.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
HOGENOM; HOG000004836; -.
HOVERGEN; HBG106726; -.
InParanoid; P97573; -.
KO; K03084; -.
PhylomeDB; P97573; -.
PRO; PR:P97573; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005884; C:actin filament; IDA:RGD.
GO; GO:0030863; C:cortical cytoskeleton; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030487; F:inositol-4,5-bisphosphate 5-phosphatase activity; IDA:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
Gene3D; 3.30.505.10; -; 1.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00128; IPPc; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Apoptosis; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Hydrolase; Immunity; Membrane; Phosphoprotein; Reference proteome;
Repeat; SH2 domain; SH3-binding.
CHAIN 1 1190 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 1.
/FTId=PRO_0000302868.
DOMAIN 8 104 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1014 1028 Interaction with DAB2. {ECO:0000250}.
MOTIF 126 131 SH3-binding 1.
MOTIF 914 917 NPXY motif 1.
MOTIF 969 974 SH3-binding 2.
MOTIF 1017 1020 NPXY motif 2.
MOTIF 1038 1049 SH3-binding 3.
COMPBIAS 961 1152 Pro-rich.
MOD_RES 245 245 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 917 917 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q92835}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 944 944 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 963 963 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES52}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1020 1020 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9ES52}.
SEQUENCE 1190 AA; 133593 MW; 85DD4F2190F98700 CRC64;
MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR NCVYTYRILP
NEDDKFTVQA SEGVPMRFFT KLDQLIEFYK KENMGLVTHL QFPVPLEEED AIDEPEEDTE
SVMSPPELPP RNIPVSGGPC EAKDLPLPTE NPRAPEVTRL SLSETLFQRL QSMDTSGLPE
EHLKAIQDYL STQLMLDSDF LKTGSSNLPH LKKLTSLLCK ELHGEVIRTL PSLESLQRLF
DQQLSPGLRP RPQVPGEANP ITMVAKLSQL TSLLSSIEDK VKALLHEGSE STNRRSLIPP
VTFEVKSESL GIPQKMHLKV DVESGKLIIK KSRDGSEDKF YSHKKILQLI KSQKFLNKLV
ILVETEKEKI LRKEYVFSDS KKREGFCQLL QQMKNKHSEQ SEPDMITIFI GTWNMGNAPP
PKKITSWFLS KGQGKTRDDS ADYIPHDIYV IGTQEDPLGE KEWLEILRHS LQEVTSMTFK
TVAIHTLWNI RIVVLAKPEH ENRISHICTD NVKTGIANTL GNKGAVGVSF MFNGTSLGFV
NSHLTSGSEK KLRRNQNYMN ILRFLALGDK KLSPFNITHR FTHLFWLGDL NYRVELPTWE
AEAIIQKIKQ QQYSDLLAHD QLLLERKEQE VFLHFEEEEI TFAPTYRFER LTRDKYAYTK
QKATGMKYNL PSWCDRVLWK SYPLVHVVCQ SYGSTSDIMT SDHSPVFATF EAGVTSQFVS
KNGPGAVDSQ GQIEFLACYA TLKTKSQTKF YLELHSSCLE SFVKSQEGEN EEGDEGELVV
RFGETLPKLK PIISDPEYLL DQHILISIKS SDSDESYGEG CIALRLETTE SQLPIYTPLT
HHGEMTGHFR GEIKLQTSEG KMREKLYDFV KTERDESSGM KCLKNLTSHD PMRQWEPAGR
VPACGISSLN EIINPNYIGM GPFGQPLHGK STLSPDQQLT AWSYDQLPKD SSLGPGRGEG
PPTPPSQPPL SPKKFSSSTA NRGSCPRVQE TRPGDLGKVE ALPQEDLPLT KPEMFENPLY
GSVSPFPKLV PRKEQESPKM MRKEPPPCPD PGVSSPSIML PKAQEVENVK GTSKQAPVPV
FGPTPRIRSF TCSSSAEGRM PSGDKSQGKP KAPASSQAPV PVKRPVKPSR SEMSQQTTPI
PAPRPPLPVK SPAVLQLQHS KGRDYRDNTE LPHHGKHRQE ESLLGRTAMQ


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