SHIP2_RAT
ID SHIP2_RAT Reviewed; 1257 AA.
AC Q9WVR3; Q9R1V2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2;
DE EC=3.1.3.86 {ECO:0000269|PubMed:11238900};
DE AltName: Full=Inositol polyphosphate phosphatase-like protein 1;
DE Short=INPPL-1;
DE AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2;
DE Short=SH2 domain-containing inositol phosphatase 2;
DE Short=SHIP-2;
GN Name=Inppl1; Synonyms=Ship2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND PHOSPHORYLATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=10381377; DOI=10.1006/bbrc.1999.0888;
RA Ishihara H., Sasaoka T., Hori H., Wada T., Hirai H., Haruta T.,
RA Kobayashi M.;
RT "Molecular cloning of rat SH2-containing inositol phosphatase 2 (SHIP2) and
RT its role in the regulation of insulin signaling.";
RL Biochem. Biophys. Res. Commun. 260:265-272(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10648902; DOI=10.1016/s0169-328x(99)00311-3;
RA Kudo M., Saito S., Owada Y., Suzaki H., Kondo H.;
RT "Localization of mRNA for SHIP2, SH2 domain-containing inositol
RT polyphosphate 5-phosphatase, in the brain of developing and mature rats.";
RL Brain Res. Mol. Brain Res. 75:172-177(2000).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11238900; DOI=10.1128/mcb.21.5.1633-1646.2001;
RA Wada T., Sasaoka T., Funaki M., Hori H., Murakami S., Ishiki M., Haruta T.,
RA Asano T., Ogawa W., Ishihara H., Kobayashi M.;
RT "Overexpression of SH2-containing inositol phosphatase 2 results in
RT negative regulation of insulin-induced metabolic actions in 3T3-L1
RT adipocytes via its 5'-phosphatase catalytic activity.";
RL Mol. Cell. Biol. 21:1633-1646(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-987.
RX PubMed=12351701; DOI=10.1210/me.2002-0083;
RA Ishihara H., Sasaoka T., Ishiki M., Wada T., Hori H., Kagawa S.,
RA Kobayashi M.;
RT "Membrane localization of Src homology 2-containing inositol 5'-phosphatase
RT 2 via Shc association is required for the negative regulation of insulin
RT signaling in Rat1 fibroblasts overexpressing insulin receptors.";
RL Mol. Endocrinol. 16:2371-2381(2002).
RN [5]
RP FUNCTION.
RX PubMed=17535963; DOI=10.1083/jcb.200609017;
RA Aoki K., Nakamura T., Inoue T., Meyer T., Matsuda M.;
RT "An essential role for the SHIP2-dependent negative feedback loop in
RT neuritogenesis of nerve growth factor-stimulated PC12 cells.";
RL J. Cell Biol. 177:817-827(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP VARIANT CYS-1142, AND POLYMORPHISM.
RX PubMed=12086927; DOI=10.2337/diabetes.51.7.2012;
RA Marion E., Kaisaki P.J., Pouillon V., Gueydan C., Levy J.C., Bodson A.,
RA Krzentowski G., Daubresse J.-C., Mockel J., Behrends J., Servais G.,
RA Szpirer C., Kruys V., Gauguier D., Schurmans S.;
RT "The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for
RT type 2 diabetes in rat and man.";
RL Diabetes 51:2012-2017(2002).
CC -!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically
CC hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively
CC regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a
CC central role in regulation of PI3K-dependent insulin signaling,
CC although the precise molecular mechanisms and signaling pathways remain
CC unclear. While overexpression reduces both insulin-stimulated MAP
CC kinase and Akt activation, its absence does not affect insulin
CC signaling or GLUT4 trafficking. Confers resistance to dietary obesity.
CC May act by regulating AKT2, but not AKT1, phosphorylation at the plasma
CC membrane. Part of a signaling pathway that regulates actin cytoskeleton
CC remodeling. Required for the maintenance and dynamic remodeling of
CC actin structures as well as in endocytosis, having a major impact on
CC ligand-induced EGFR internalization and degradation. Participates in
CC regulation of cortical and submembraneous actin by hydrolyzing
CC PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity).
CC Regulates cell adhesion and cell spreading. Required for HGF-mediated
CC lamellipodium formation, cell scattering and spreading. Acts as a
CC negative regulator of EPHA2 receptor endocytosis by inhibiting via
CC PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis
CC by regulating PtdIns(3,4,5)P3 level and is required to form an initial
CC protrusive pattern, and later, maintain proper neurite outgrowth. Acts
CC as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A).
CC Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a
CC central role in terminating signal transduction from activating
CC immune/hematopoietic cell receptor systems. Involved in EGF signaling
CC pathway. Upon stimulation by EGF, it is recruited by EGFR and
CC dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating
CC the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-
CC regulates Fc-gamma-R-mediated phagocytosis in macrophages independently
CC of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent
CC gene transcription by regulating macrophage colony-stimulating factor
CC (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and
CC could thus affect the levels of the higher inositol polyphosphates like
CC InsP6. Involved in endochondral ossification (By similarity).
CC {ECO:0000250|UniProtKB:O15357, ECO:0000269|PubMed:10381377,
CC ECO:0000269|PubMed:11238900, ECO:0000269|PubMed:12351701,
CC ECO:0000269|PubMed:17535963}.
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:0000269|PubMed:11238900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000305|PubMed:11238900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83417; Evidence={ECO:0000250|UniProtKB:O15357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43549;
CC Evidence={ECO:0000250|UniProtKB:O15357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-
CC (1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43556,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420,
CC ChEBI:CHEBI:83422; Evidence={ECO:0000250|UniProtKB:O15357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43557;
CC Evidence={ECO:0000250|UniProtKB:O15357};
CC -!- ACTIVITY REGULATION: Activated upon translocation to the sites of
CC synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity is
CC enhanced in the presence of phosphatidylserine (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1. Interacts
CC with EGFR. Upon stimulation by the EGF signaling pathway, it forms a
CC complex with SHC1 and EGFR. Interacts with cytoskeletal protein
CC SORBS3/vinexin, promoting its localization to the periphery of cells.
CC Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or
CC GP1BB) that regulates cortical and submembraneous actin. Interacts with
CC c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356'. Interacts
CC with p130Cas/BCAR1. Interacts with CENTD3/ARAP3 via its SAM domain.
CC Interacts with c-Cbl/CBL and CAP/SORBS1. Interacts with activated EPHA2
CC receptor. Interacts with receptors FCGR2A. Interacts with FCGR2B.
CC Interacts with tyrosine kinase ABL1. Interacts with tyrosine kinase
CC TEC. Interacts with CSF1R. Interacts (via N-terminus) with SH3YL1 (via
CC SH3 domain). Interacts (via SH2 domain) with tyrosine phosphorylated
CC KLRC1 (via ITIM). {ECO:0000250|UniProtKB:O15357,
CC ECO:0000250|UniProtKB:Q6P549}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12351701}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC {ECO:0000269|PubMed:12351701}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12351701}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O15357}. Nucleus {ECO:0000250|UniProtKB:D7PF45}.
CC Nucleus speckle {ECO:0000250|UniProtKB:D7PF45}. Note=Translocates to
CC membrane ruffles when activated, translocation is probably due to
CC different mechanisms depending on the stimulus and cell type. Partly
CC translocated via its SH2 domain which mediates interaction with
CC tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor
CC (FCGR2B). Tyrosine phosphorylation may also participate in membrane
CC localization. Insulin specifically stimulates its redistribution from
CC the cytosol to the plasma membrane. Recruited to the membrane following
CC M-CSF stimulation. In activated spreading platelets, localizes with
CC actin at filopodia, lamellipodia and the central actin ring.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVR3-2; Sequence=VSP_027986;
CC -!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of
CC proteins such as SHC1 or FCGR2A. It also mediates the interaction with
CC p130Cas/BCAR1 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated
CC proteins is required for the specific binding of the PID domain.
CC {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated by the members of the SRC family after
CC exposure to a diverse array of extracellular stimuli such as insulin,
CC growth factors such as EGF or PDGF, chemokines, integrin ligands and
CC hypertonic and oxidative stress. May be phosphorylated upon IgG
CC receptor FCGR2B-binding. Phosphorylated at Tyr-987 following cell
CC attachment and spreading. Phosphorylated at Tyr-1161 following EGF
CC signaling pathway stimulation (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Variant Cys-1142 found in diabetic GK strain may be a
CC cause of diabete in this strain. Genetic variations in Inppl1 may also
CC be a cause of susceptibility to hypertension.
CC {ECO:0000269|PubMed:12086927}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000305}.
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DR EMBL; AB011439; BAA81818.1; -; mRNA.
DR EMBL; AB025794; BAA82308.1; -; mRNA.
DR RefSeq; NP_001257772.1; NM_001270843.1. [Q9WVR3-2]
DR RefSeq; NP_075233.1; NM_022944.2. [Q9WVR3-1]
DR AlphaFoldDB; Q9WVR3; -.
DR BMRB; Q9WVR3; -.
DR SMR; Q9WVR3; -.
DR IntAct; Q9WVR3; 2.
DR STRING; 10116.ENSRNOP00000061371; -.
DR BindingDB; Q9WVR3; -.
DR ChEMBL; CHEMBL2331062; -.
DR iPTMnet; Q9WVR3; -.
DR PhosphoSitePlus; Q9WVR3; -.
DR jPOST; Q9WVR3; -.
DR PaxDb; Q9WVR3; -.
DR PRIDE; Q9WVR3; -.
DR Ensembl; ENSRNOT00000066915; ENSRNOP00000061371; ENSRNOG00000019730. [Q9WVR3-2]
DR GeneID; 65038; -.
DR KEGG; rno:65038; -.
DR UCSC; RGD:68396; rat. [Q9WVR3-1]
DR CTD; 3636; -.
DR RGD; 68396; Inppl1.
DR eggNOG; KOG0565; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR InParanoid; Q9WVR3; -.
DR OrthoDB; 311217at2759; -.
DR PhylomeDB; Q9WVR3; -.
DR TreeFam; TF323475; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR PRO; PR:Q9WVR3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:RGD.
DR GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0044255; P:cellular lipid metabolic process; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:RGD.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:RGD.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0097178; P:ruffle assembly; ISO:RGD.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
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 Pfam; PF03372; Exo_endo_phos; 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; SSF47769; SSF47769; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell adhesion; Cell projection;
KW Cytoplasm; Cytoskeleton; Hydrolase; Immunity; Lipid metabolism; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; SH2 domain; SH3-binding.
FT CHAIN 1..1257
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 5-
FT phosphatase 2"
FT /id="PRO_0000302872"
FT DOMAIN 21..117
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 1195..1257
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 119..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 945..950
FT /note="SH3-binding"
FT MOTIF 984..987
FT /note="NPXY motif"
FT COMPBIAS 120..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 887
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 987
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 1136
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 1161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15357"
FT VAR_SEQ 1184..1257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10381377"
FT /id="VSP_027986"
FT VARIANT 1142
FT /note="R -> C (in strain: GK)"
FT /evidence="ECO:0000269|PubMed:12086927"
FT MUTAGEN 987
FT /note="Y->F: Loss of phosphorylation following insulin
FT stimulation."
FT /evidence="ECO:0000269|PubMed:12351701"
FT CONFLICT 910
FT /note="S -> N (in Ref. 1; BAA81818)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="P -> L (in Ref. 1; BAA81818)"
FT /evidence="ECO:0000305"
SQ 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
