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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)

 SHIP2_RAT               Reviewed;        1257 AA.
Q9WVR3; Q9R1V2;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-JUN-2018, entry version 115.
RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2;
EC=3.1.3.86;
AltName: Full=Inositol polyphosphate phosphatase-like protein 1;
Short=INPPL-1;
AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2;
Short=SH2 domain-containing inositol phosphatase 2;
Short=SHIP-2;
Name=Inppl1; Synonyms=Ship2;
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] (ISOFORM 2), FUNCTION, AND PHOSPHORYLATION.
STRAIN=Sprague-Dawley;
PubMed=10381377; DOI=10.1006/bbrc.1999.0888;
Ishihara H., Sasaoka T., Hori H., Wada T., Hirai H., Haruta T.,
Kobayashi M.;
"Molecular cloning of rat SH2-containing inositol phosphatase 2
(SHIP2) and its role in the regulation of insulin signaling.";
Biochem. Biophys. Res. Commun. 260:265-272(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10648902; DOI=10.1016/S0169-328X(99)00311-3;
Kudo M., Saito S., Owada Y., Suzaki H., Kondo H.;
"Localization of mRNA for SHIP2, SH2 domain-containing inositol
polyphosphate 5-phosphatase, in the brain of developing and mature
rats.";
Brain Res. Mol. Brain Res. 75:172-177(2000).
[3]
FUNCTION.
PubMed=11238900; DOI=10.1128/MCB.21.5.1633-1646.2001;
Wada T., Sasaoka T., Funaki M., Hori H., Murakami S., Ishiki M.,
Haruta T., Asano T., Ogawa W., Ishihara H., Kobayashi M.;
"Overexpression of SH2-containing inositol phosphatase 2 results in
negative regulation of insulin-induced metabolic actions in 3T3-L1
adipocytes via its 5'-phosphatase catalytic activity.";
Mol. Cell. Biol. 21:1633-1646(2001).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-987.
PubMed=12351701; DOI=10.1210/me.2002-0083;
Ishihara H., Sasaoka T., Ishiki M., Wada T., Hori H., Kagawa S.,
Kobayashi M.;
"Membrane localization of Src homology 2-containing inositol 5'-
phosphatase 2 via Shc association is required for the negative
regulation of insulin signaling in Rat1 fibroblasts overexpressing
insulin receptors.";
Mol. Endocrinol. 16:2371-2381(2002).
[5]
FUNCTION.
PubMed=17535963; DOI=10.1083/jcb.200609017;
Aoki K., Nakamura T., Inoue T., Meyer T., Matsuda M.;
"An essential role for the SHIP2-dependent negative feedback loop in
neuritogenesis of nerve growth factor-stimulated PC12 cells.";
J. Cell Biol. 177:817-827(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, 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).
[7]
VARIANT CYS-1142, AND POLYMORPHISM.
PubMed=12086927; DOI=10.2337/diabetes.51.7.2012;
Marion E., Kaisaki P.J., Pouillon V., Gueydan C., Levy J.C.,
Bodson A., Krzentowski G., Daubresse J.-C., Mockel J., Behrends J.,
Servais G., Szpirer C., Kruys V., Gauguier D., Schurmans S.;
"The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate
for type 2 diabetes in rat and man.";
Diabetes 51:2012-2017(2002).
-!- 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. Plays a central role in regulation of PI3K-dependent
insulin signaling, although the precise molecular mechanisms and
signaling pathways remain unclear. While overexpression reduces
both insulin-stimulated MAP kinase and Akt activation, its absence
does not affect insulin signaling or GLUT4 trafficking. Confers
resistance to dietary obesity. May act by regulating AKT2, but not
AKT1, phosphorylation at the plasma membrane. Part of a signaling
pathway that regulates actin cytoskeleton remodeling. Required for
the maintenance and dynamic remodeling of actin structures as well
as in endocytosis, having a major impact on ligand-induced EGFR
internalization and degradation. Participates in regulation of
cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3
thereby regulating membrane ruffling (By similarity). Regulates
cell adhesion and cell spreading. Required for HGF-mediated
lamellipodium formation, cell scattering and spreading. Acts as a
negative regulator of EPHA2 receptor endocytosis by inhibiting via
PI3K-dependent Rac1 activation. Acts as a regulator of
neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required
to form an initial protrusive pattern, and later, maintain proper
neurite outgrowth. Acts as a negative regulator of the FC-gamma-
RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB
receptor (FCGR2B), playing a central role in terminating signal
transduction from activating immune/hematopoietic cell receptor
systems. Involved in EGF signaling pathway. Upon stimulation by
EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3.
Plays a negative role in regulating the PI3K-PKB pathway, possibly
by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated
phagocytosis in macrophages independently of INPP5D/SHIP1. In
macrophages, down-regulates NF-kappa-B-dependent gene
transcription by regulating macrophage colony-stimulating factor
(M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4,
and could thus affect the levels of the higher inositol
polyphosphates like InsP6. Involved in endochondral ossification
(By similarity). {ECO:0000250|UniProtKB:O15357,
ECO:0000269|PubMed:10381377, ECO:0000269|PubMed:11238900,
ECO:0000269|PubMed:12351701, ECO:0000269|PubMed:17535963}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,4,5-
triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-
diphosphate + phosphate.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity
is enhanced in the presence of phosphatidylserine (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1.
Interacts with EGFR. Upon stimulation by the EGF signaling
pathway, it forms a complex with SHC1 and EGFR. Interacts with
cytoskeletal protein SORBS3/vinexin, promoting its localization to
the periphery of cells. Forms a complex with filamin (FLNA or
FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and
submembraneous actin. Interacts with c-Met/MET, when c-Met/MET is
phosphorylated on 'Tyr-1356'. Interacts with p130Cas/BCAR1.
Interacts with CENTD3/ARAP3 via its SAM domain. Interacts with c-
Cbl/CBL and CAP/SORBS1. Interacts with activated EPHA2 receptor.
Interacts with receptors FCGR2A. Interacts with FCGR2B. Interacts
with tyrosine kinase ABL1. Interacts with tyrosine kinase TEC.
Interacts with CSF1R. Interacts (via N-terminus) with SH3YL1 (via
SH3 domain). {ECO:0000250|UniProtKB:O15357,
ECO:0000250|UniProtKB:Q6P549}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12351701}. Cytoplasm, cytoskeleton
{ECO:0000250}. Membrane {ECO:0000269|PubMed:12351701}; Peripheral
membrane protein {ECO:0000269|PubMed:12351701}. Cell projection,
filopodium {ECO:0000250}. Cell projection, lamellipodium
{ECO:0000250}. Note=Translocates to membrane ruffles when
activated, translocation is probably due to different mechanisms
depending on the stimulus and cell type. Partly translocated via
its SH2 domain which mediates interaction with tyrosine
phosphorylated receptors such as the FC-gamma-RIIB receptor
(FCGR2B). Tyrosine phosphorylation may also participate in
membrane localization. Insulin specifically stimulates its
redistribution from the cytosol to the plasma membrane. Recruited
to the membrane following M-CSF stimulation. In activated
spreading platelets, localizes with actin at filopodia,
lamellipodia and the central actin ring.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9WVR3-1; Sequence=Displayed;
Name=2;
IsoId=Q9WVR3-2; Sequence=VSP_027986;
-!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
forms of proteins such as SHC1 or FCGR2A. It also mediates the
interaction with p130Cas/BCAR1 (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
insulin, growth factors such as EGF or PDGF, chemokines, integrin
ligands and hypertonic and oxidative stress. May be phosphorylated
upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987
following cell attachment and spreading. Phosphorylated at Tyr-
1161 following EGF signaling pathway stimulation (By similarity).
{ECO:0000250}.
-!- POLYMORPHISM: Variant Cys-1142 found in diabetic GK strain may be
a cause of diabete in this strain. Genetic variations in Inppl1
may also be a cause of susceptibility to hypertension.
{ECO:0000269|PubMed:12086927}.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB011439; BAA81818.1; -; mRNA.
EMBL; AB025794; BAA82308.1; -; mRNA.
RefSeq; NP_001257772.1; NM_001270843.1. [Q9WVR3-2]
RefSeq; NP_075233.1; NM_022944.2. [Q9WVR3-1]
UniGene; Rn.42902; -.
ProteinModelPortal; Q9WVR3; -.
SMR; Q9WVR3; -.
IntAct; Q9WVR3; 1.
STRING; 10116.ENSRNOP00000061371; -.
BindingDB; Q9WVR3; -.
ChEMBL; CHEMBL2331062; -.
iPTMnet; Q9WVR3; -.
PhosphoSitePlus; Q9WVR3; -.
PaxDb; Q9WVR3; -.
PRIDE; Q9WVR3; -.
GeneID; 65038; -.
KEGG; rno:65038; -.
UCSC; RGD:68396; rat. [Q9WVR3-1]
CTD; 3636; -.
RGD; 68396; Inppl1.
eggNOG; KOG0565; Eukaryota.
eggNOG; KOG4384; Eukaryota.
eggNOG; COG5411; LUCA.
HOGENOM; HOG000004836; -.
HOVERGEN; HBG106726; -.
InParanoid; Q9WVR3; -.
KO; K15909; -.
PhylomeDB; Q9WVR3; -.
TreeFam; TF323475; -.
PRO; PR:Q9WVR3; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IDA:RGD.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:RGD.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
GO; GO:0008156; P:negative regulation of DNA replication; IMP:RGD.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:RGD.
GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:RGD.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IMP:RGD.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
GO; GO:0042493; P:response to drug; IEP:RGD.
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; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00128; IPPc; 1.
SMART; SM00454; SAM; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell adhesion; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Immunity;
Membrane; Phosphoprotein; Reference proteome; SH2 domain; SH3-binding.
CHAIN 1 1257 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 2.
/FTId=PRO_0000302872.
DOMAIN 21 117 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 1195 1257 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
MOTIF 945 950 SH3-binding.
MOTIF 984 987 NPXY motif.
COMPBIAS 936 1106 Pro-rich.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 165 165 Phosphothreonine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 887 887 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 987 987 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1132 1132 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1136 1136 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1161 1161 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1256 1256 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
VAR_SEQ 1184 1257 Missing (in isoform 2).
{ECO:0000303|PubMed:10381377}.
/FTId=VSP_027986.
VARIANT 1142 1142 R -> C (in strain: GK).
{ECO:0000269|PubMed:12086927}.
MUTAGEN 987 987 Y->F: Loss of phosphorylation following
insulin stimulation.
{ECO:0000269|PubMed:12351701}.
CONFLICT 910 910 S -> N (in Ref. 1; BAA81818).
{ECO:0000305}.
CONFLICT 1009 1009 P -> L (in Ref. 1; BAA81818).
{ECO:0000305}.
SEQUENCE 1257 AA; 139143 MW; 3A994C8E52940083 CRC64;
MASVCGAPSP GGALGSQAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE
REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SVPAGPSSPL PAPETPTTPA AESTPNGLST
VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS
SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF
THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNKHSKQD
EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR
EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG
NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP
TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS
PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK
SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV
ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
SKAPSVLRGS QEHRSGSRKP TSTEASCPLS KLFEEPEKPP PTGRPPAPPR AVPREESLNP
RLKSEGTPEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPTSFARAPI PPTTKNKVAI
TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG
RSVGEARGPP PPKAHPRPPL PPGTSPASTF LEEVASADDR SCSVLQMAKT LSEVDYSPGP
GRSALLPNPL ELQLPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK


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