SHIP1_HUMAN
ID SHIP1_HUMAN Reviewed; 1189 AA.
AC Q92835; O00145; Q13544; Q13545; Q6P5A4; Q92656; Q9UE80;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;
DE EC=3.1.3.86 {ECO:0000269|PubMed:10764818, ECO:0000269|PubMed:8723348, ECO:0000269|PubMed:8769125};
DE AltName: Full=Inositol polyphosphate-5-phosphatase D;
DE EC=3.1.3.56 {ECO:0000269|PubMed:8769125, ECO:0000269|PubMed:9108392};
DE AltName: Full=Inositol polyphosphate-5-phosphatase of 145 kDa {ECO:0000303|PubMed:8874179};
DE Short=SIP-145 {ECO:0000303|PubMed:8874179};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase;
DE EC=3.1.3.36 {ECO:0000269|PubMed:10764818};
DE AltName: Full=SH2 domain-containing inositol 5'-phosphatase 1 {ECO:0000303|PubMed:9108392};
DE Short=SH2 domain-containing inositol phosphatase 1;
DE Short=SHIP-1;
DE AltName: Full=p150Ship;
DE Short=hp51CN {ECO:0000303|PubMed:8769125};
GN Name=INPP5D; Synonyms=SHIP {ECO:0000303|PubMed:10764818}, SHIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND VARIANT TYR-1169.
RX PubMed=8769125; DOI=10.1006/bbrc.1996.1161;
RA Drayer A.L., Pesesse X., De Smedt F., Woscholski R., Parker P., Erneux C.;
RT "Cloning and expression of a human placenta inositol 1,3,4,5-
RT tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-
RT phosphatase.";
RL Biochem. Biophys. Res. Commun. 225:243-249(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION
RP WITH SHC1.
RX PubMed=8874179;
RA Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.;
RT "Cloning and characterization of human SHIP, the 145-kD inositol 5-
RT phosphatase that associates with SHC after cytokine stimulation.";
RL Blood 88:2833-2840(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-1139 (ISOFORM 1), CATALYTIC ACTIVITY, AND INTERACTION WITH GRB2.
RC TISSUE=Lung;
RX PubMed=8723348; DOI=10.1016/s0960-9822(02)00511-0;
RA Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M., Jefferson A.B.,
RA Norris F.A., Masiarz F.R., Cousens L.S., Majerus P.W., Williams L.T.;
RT "Multiple forms of an inositol polyphosphate 5-phosphatase form signaling
RT complexes with Shc and Grb2.";
RL Curr. Biol. 6:438-445(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9058707;
RA Geier S.J., Algate P.A., Carlberg K., Flowers D., Friedman C., Trask B.,
RA Rohrschneider L.R.;
RT "The human SHIP gene is differentially expressed in cell lineages of the
RT bone marrow and blood.";
RL Blood 89:1876-1885(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, INTERACTION WITH GRB2, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9108392;
RA Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T.,
RA Mitani K., Yazaki Y., Hirai H.;
RT "Purification and molecular cloning of SH2- and SH3-containing inositol
RT polyphosphate-5-phosphatase, which is involved in the signaling pathway of
RT granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-
RT Abl.";
RL Blood 89:2745-2756(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TYR-1169.
RC TISSUE=B-cell, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH SLAMF1.
RX PubMed=10229804;
RA Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A.,
RA Sidorenko S.P.;
RT "CDw150 associates with src-homology 2-containing inositol phosphatase and
RT modulates CD95-mediated apoptosis.";
RL J. Immunol. 162:5719-5727(1999).
RN [8]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH DOK1.
RX PubMed=10822173; DOI=10.1016/s0898-6568(00)00073-5;
RA Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.;
RT "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with
RT the dok1 phosphoprotein in bcr-Abl transformed cells.";
RL Cell. Signal. 12:317-326(2000).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=10764818; DOI=10.1074/jbc.m910119199;
RA Kisseleva M.V., Wilson M.P., Majerus P.W.;
RT "The isolation and characterization of a cDNA encoding phospholipid-
RT specific inositol polyphosphate 5-phosphatase.";
RL J. Biol. Chem. 275:20110-20116(2000).
RN [10]
RP FUNCTION.
RX PubMed=12421919; DOI=10.4049/jimmunol.169.10.5441;
RA Freeburn R.W., Wright K.L., Burgess S.J., Astoul E., Cantrell D.A.,
RA Ward S.G.;
RT "Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-
RT trisphosphate metabolism in T lymphocytes and can regulate novel
RT phosphoinositide 3-kinase effectors.";
RL J. Immunol. 169:5441-5450(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP FUNCTION.
RX PubMed=16682172; DOI=10.1016/j.cellsig.2006.03.012;
RA Vaillancourt M., Levasseur S., Tremblay M.-L., Marois L.,
RA Rollet-Labelle E., Naccache P.H.;
RT "The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved
RT in CD32a signaling in human neutrophils.";
RL Cell. Signal. 18:2022-2032(2006).
RN [13]
RP INTERACTION WITH FCRL3.
RX PubMed=19843936; DOI=10.4049/jimmunol.0901982;
RA Kochi Y., Myouzen K., Yamada R., Suzuki A., Kurosaki T., Nakamura Y.,
RA Yamamoto K.;
RT "FCRL3, an autoimmune susceptibility gene, has inhibitory potential on B-
RT cell receptor-mediated signaling.";
RL J. Immunol. 183:5502-5510(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH FCRL6.
RX PubMed=20933011; DOI=10.1016/j.imlet.2010.09.023;
RA Kulemzin S.V., Zamoshnikova A.Y., Yurchenko M.Y., Vitak N.Y.,
RA Najakshin A.M., Fayngerts S.A., Chikaev N.A., Reshetnikova E.S.,
RA Kashirina N.M., Peclo M.M., Rutkevich P.N., Shevelev A.Y.,
RA Yanushevskaya E.V., Baranov K.O., Mamonkin M., Vlasik T.N., Sidorenko S.P.,
RA Taranin A.V., Mechetina L.V.;
RT "FCRL6 receptor: expression and associated proteins.";
RL Immunol. Lett. 134:174-182(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960; THR-963 AND SER-971, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP STRUCTURE BY NMR OF 1-112.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the human SHIP SH2 domain.";
RL Submitted (APR-2008) to the PDB data bank.
RN [18]
RP VARIANT GLU-685.
RX PubMed=12529653; DOI=10.1038/sj.leu.2402725;
RA Luo J.-M., Yoshida H., Komura S., Ohishi N., Pan L., Shigeno K.,
RA Hanamura I., Miura K., Iida S., Ueda R., Naoe T., Akao Y., Ohno R.,
RA Ohnishi K.;
RT "Possible dominant-negative mutation of the SHIP gene in acute myeloid
RT leukemia.";
RL Leukemia 17:1-8(2003).
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
CC (PubMed:8723348, PubMed:10764818, PubMed:8769125). Able also to
CC hydrolyzes the 5-phosphate of phosphatidylinositol-4,5-bisphosphate
CC (PtdIns(4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (PubMed:9108392,
CC PubMed:10764818, PubMed:8769125). Acts as a negative regulator of B-
CC cell antigen receptor signaling. Mediates signaling from the FC-gamma-
CC RIIB receptor (FCGR2B), playing a central role in terminating signal
CC transduction from activating immune/hematopoietic cell receptor
CC systems. Acts as a negative regulator of myeloid cell
CC proliferation/survival and chemotaxis, mast cell degranulation, immune
CC cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and
CC JNK signaling in B-cells. Regulates proliferation of osteoclast
CC precursors, macrophage programming, phagocytosis and activation and is
CC required for endotoxin tolerance. Involved in the control of cell-cell
CC junctions, CD32a signaling in neutrophils and modulation of EGF-induced
CC phospholipase C activity (PubMed:16682172). Key regulator of neutrophil
CC migration, by governing the formation of the leading edge and
CC polarization required for chemotaxis. Modulates FCGR3/CD16-mediated
CC cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced
CC apoptosis through its Smad-dependent expression.
CC {ECO:0000269|PubMed:10764818, ECO:0000269|PubMed:12421919,
CC ECO:0000269|PubMed:16682172, ECO:0000269|PubMed:8723348,
CC ECO:0000269|PubMed:8769125, ECO:0000269|PubMed:9108392}.
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:10764818, ECO:0000269|PubMed:8723348,
CC ECO:0000269|PubMed:8769125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000305|PubMed:10764818, ECO:0000305|PubMed:8723348,
CC ECO:0000305|PubMed:8769125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56; Evidence={ECO:0000269|PubMed:8769125,
CC ECO:0000269|PubMed:9108392};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393;
CC Evidence={ECO:0000305|PubMed:8769125, ECO:0000305|PubMed:9108392};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:10764818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC Evidence={ECO:0000305|PubMed:10764818};
CC -!- ACTIVITY REGULATION: Activated upon translocation to the sites of
CC synthesis of PtdIns(3,4,5)P3 in the membrane. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.95 uM for phosphatidylinositol-3,4,5-trisphosphate
CC {ECO:0000269|PubMed:10764818};
CC Vmax=0.458 umol/min/mg enzyme with phosphatidylinositol-3,4,5-
CC trisphosphate as substrate {ECO:0000269|PubMed:10764818};
CC -!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1
CC (PubMed:8874179). Interacts with tyrosine phosphorylated form of DOK1
CC (PubMed:10822173). Interacts with tyrosine phosphorylated form of DOK3
CC (By similarity). Interacts with tyrosine phosphorylated form of
CC SLAMF1/CD150 (PubMed:10229804). Interacts with PTPN11 in response to
CC IL-3 (By similarity). Interacts with receptor EPOR (By similarity).
CC Interacts with receptors MS4A2/FCER1B and FCER1G (By similarity).
CC Interacts with receptors FCGR2B and FCGR3 (By similarity). Interacts
CC with receptor FCGR2A, leading to regulate gene expression during the
CC phagocytic process (By similarity). Interacts with GRB2
CC (PubMed:8723348, PubMed:9108392). Interacts with PLCG1 (By similarity).
CC Interacts with tyrosine kinases SRC and TEC (By similarity). Interacts
CC with c-Met/MET (By similarity). Interacts with MILR1 (tyrosine-
CC phosphorylated) (By similarity). Can weakly interact (via NPXY motif 2)
CC with DAB2 (via PID domain); the interaction is impaired by tyrosine
CC phosphorylation of the NPXY motif (By similarity). Interacts with FCRL3
CC and FCRL6 (tyrosine phosphorylated form) (PubMed:20933011,
CC PubMed:19843936). Interacts (via SH2 domain) with tyrosine
CC phosphorylated KLRC1 (via ITIM). {ECO:0000250|UniProtKB:P97573,
CC ECO:0000250|UniProtKB:Q9ES52, ECO:0000269|PubMed:19843936,
CC ECO:0000269|PubMed:20933011}.
CC -!- INTERACTION:
CC Q92835; Q9BZW8: CD244; NbExp=6; IntAct=EBI-1380477, EBI-1580565;
CC Q92835; P31994: FCGR2B; NbExp=3; IntAct=EBI-1380477, EBI-724784;
CC Q92835; O75525: KHDRBS3; NbExp=3; IntAct=EBI-1380477, EBI-722504;
CC Q92835; Q15323: KRT31; NbExp=3; IntAct=EBI-1380477, EBI-948001;
CC Q92835; Q6A162: KRT40; NbExp=3; IntAct=EBI-1380477, EBI-10171697;
CC Q92835; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1380477, EBI-10172290;
CC Q92835; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1380477, EBI-10172052;
CC Q92835; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1380477, EBI-945833;
CC Q92835; Q96B97: SH3KBP1; NbExp=6; IntAct=EBI-1380477, EBI-346595;
CC Q92835-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9092209, EBI-3867333;
CC Q92835-2; O75525: KHDRBS3; NbExp=3; IntAct=EBI-9092209, EBI-722504;
CC Q92835-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-9092209, EBI-11749135;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10822173}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9ES52}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9ES52}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9ES52}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9ES52}. Membrane {ECO:0000269|PubMed:10822173};
CC Peripheral membrane protein {ECO:0000269|PubMed:10822173}.
CC Note=Translocates to the plasma membrane when activated, translocation
CC is probably due to different mechanisms depending on the stimulus and
CC cell type. Translocates from the cytoplasm to membrane ruffles in a
CC FCGR3/CD16-dependent manner. Colocalizes with FC-gamma-RIIB receptor
CC (FCGR2B) or FCGR3/CD16 at membrane ruffles. Tyrosine phosphorylation
CC may also participate in membrane localization.
CC {ECO:0000250|UniProtKB:Q9ES52}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92835-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92835-2; Sequence=VSP_027978;
CC Name=3; Synonyms=SIP-110;
CC IsoId=Q92835-3; Sequence=VSP_027977, VSP_027979;
CC -!- TISSUE SPECIFICITY: Specifically expressed in immune and hematopoietic
CC cells. Expressed in bone marrow and blood cells. Levels vary
CC considerably within this compartment. Present in at least 74% of
CC immature CD34+ cells, whereas within the more mature population of
CC CD33+ cells, it is present in only 10% of cells. Present in the
CC majority of T-cells, while it is present in a minority of B-cells (at
CC protein level). {ECO:0000269|PubMed:8769125,
CC ECO:0000269|PubMed:8874179, ECO:0000269|PubMed:9058707,
CC ECO:0000269|PubMed:9108392}.
CC -!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of
CC proteins such as SHC1 or PTPN11/SHP-2. It competes with that of GRB2
CC for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is
CC also required for tyrosine phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:Q9ES52}.
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|UniProtKB:Q9ES52}.
CC -!- PTM: Tyrosine phosphorylated by the members of the SRC family after
CC exposure to a diverse array of extracellular stimuli such as cytokines,
CC growth factors, antibodies, chemokines, integrin ligands and hypertonic
CC and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.
CC {ECO:0000269|PubMed:10822173, ECO:0000269|PubMed:9108392}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50454.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X98429; CAA67071.1; -; mRNA.
DR EMBL; U57650; AAB53573.1; -; mRNA.
DR EMBL; U50040; AAC50453.1; -; mRNA.
DR EMBL; U50041; AAC50454.1; ALT_INIT; mRNA.
DR EMBL; U84400; AAB49680.1; -; mRNA.
DR EMBL; U53470; AAD00081.1; -; mRNA.
DR EMBL; BC062985; AAH62985.1; -; mRNA.
DR EMBL; BC099920; AAH99920.1; -; mRNA.
DR EMBL; BC113580; AAI13581.1; -; mRNA.
DR EMBL; BC113582; AAI13583.1; -; mRNA.
DR CCDS; CCDS74672.1; -. [Q92835-1]
DR CCDS; CCDS77543.1; -. [Q92835-2]
DR PIR; JC4889; JC4889.
DR RefSeq; NP_001017915.1; NM_001017915.2. [Q92835-1]
DR RefSeq; NP_005532.2; NM_005541.4. [Q92835-2]
DR PDB; 2YSX; NMR; -; A=1-112.
DR PDB; 5RW2; X-ray; 1.22 A; A=397-857.
DR PDB; 5RW3; X-ray; 1.37 A; A=397-857.
DR PDB; 5RW4; X-ray; 1.31 A; A=397-857.
DR PDB; 5RW5; X-ray; 1.38 A; A=397-857.
DR PDB; 5RW6; X-ray; 1.32 A; A=397-857.
DR PDB; 5RW7; X-ray; 1.23 A; A=397-857.
DR PDB; 5RW8; X-ray; 1.27 A; A=397-857.
DR PDB; 5RW9; X-ray; 1.45 A; A=397-857.
DR PDB; 5RWA; X-ray; 1.29 A; A=397-857.
DR PDB; 5RWB; X-ray; 1.25 A; A=397-857.
DR PDB; 5RWC; X-ray; 1.40 A; A=397-857.
DR PDB; 5RWD; X-ray; 1.29 A; A=397-857.
DR PDB; 5RWE; X-ray; 1.34 A; A=397-857.
DR PDB; 5RWF; X-ray; 1.35 A; A=397-857.
DR PDB; 5RWG; X-ray; 1.46 A; A=397-857.
DR PDB; 5RWH; X-ray; 1.56 A; A=397-857.
DR PDB; 5RWI; X-ray; 1.29 A; A=397-857.
DR PDB; 5RWJ; X-ray; 1.26 A; A=397-857.
DR PDB; 5RWK; X-ray; 1.32 A; A=397-857.
DR PDB; 5RWL; X-ray; 1.37 A; A=397-857.
DR PDB; 5RWM; X-ray; 1.36 A; A=397-857.
DR PDB; 5RWN; X-ray; 1.38 A; A=397-857.
DR PDB; 5RWO; X-ray; 1.29 A; A=397-857.
DR PDB; 5RWP; X-ray; 1.48 A; A=397-857.
DR PDB; 5RWQ; X-ray; 1.32 A; A=397-857.
DR PDB; 5RWR; X-ray; 1.43 A; A=397-857.
DR PDB; 5RWS; X-ray; 1.28 A; A=397-857.
DR PDB; 5RWT; X-ray; 1.43 A; A=397-857.
DR PDB; 5RWU; X-ray; 1.37 A; A=397-857.
DR PDB; 5RWV; X-ray; 1.25 A; A=397-857.
DR PDB; 5RWW; X-ray; 1.16 A; A=397-857.
DR PDB; 5RWX; X-ray; 1.34 A; A=397-857.
DR PDB; 5RWY; X-ray; 1.35 A; A=397-857.
DR PDB; 5RWZ; X-ray; 1.42 A; A=397-857.
DR PDB; 5RX0; X-ray; 1.43 A; A=397-857.
DR PDB; 5RX1; X-ray; 1.31 A; A=397-857.
DR PDB; 5RX2; X-ray; 1.27 A; A=397-857.
DR PDB; 5RX3; X-ray; 1.45 A; A=397-857.
DR PDB; 5RX4; X-ray; 1.35 A; A=397-857.
DR PDB; 5RX5; X-ray; 1.28 A; A=397-857.
DR PDB; 5RX6; X-ray; 1.45 A; A=397-857.
DR PDB; 5RX7; X-ray; 1.36 A; A=397-857.
DR PDB; 5RX8; X-ray; 1.34 A; A=397-857.
DR PDB; 5RX9; X-ray; 1.29 A; A=397-857.
DR PDB; 5RXA; X-ray; 1.24 A; A=397-857.
DR PDB; 5RXB; X-ray; 1.58 A; A=397-857.
DR PDB; 5RXC; X-ray; 1.59 A; A=397-857.
DR PDB; 5RXD; X-ray; 1.33 A; A=397-857.
DR PDB; 5RXE; X-ray; 1.25 A; A=397-857.
DR PDB; 5RXF; X-ray; 1.26 A; A=397-857.
DR PDB; 5RXG; X-ray; 1.52 A; A=397-857.
DR PDB; 5RXH; X-ray; 1.42 A; A=397-857.
DR PDB; 5RXI; X-ray; 1.74 A; A=397-857.
DR PDB; 5RXJ; X-ray; 1.52 A; A=397-857.
DR PDB; 5RXK; X-ray; 1.46 A; A=397-857.
DR PDB; 5RXL; X-ray; 1.49 A; A=397-857.
DR PDB; 5RXM; X-ray; 1.46 A; A=397-857.
DR PDB; 5RXO; X-ray; 1.71 A; A=397-857.
DR PDB; 5RXP; X-ray; 1.53 A; A=397-857.
DR PDB; 5RXQ; X-ray; 1.65 A; A=397-857.
DR PDB; 5RXR; X-ray; 1.40 A; A=397-857.
DR PDB; 5RXS; X-ray; 1.37 A; A=397-857.
DR PDB; 5RXT; X-ray; 1.63 A; A=397-857.
DR PDB; 5RXU; X-ray; 1.64 A; A=397-857.
DR PDB; 5RXV; X-ray; 1.50 A; A=397-857.
DR PDB; 5RXW; X-ray; 1.34 A; A=397-857.
DR PDB; 5RXX; X-ray; 1.43 A; A=397-857.
DR PDB; 5RXY; X-ray; 1.40 A; A=397-857.
DR PDB; 5RXZ; X-ray; 1.56 A; A=397-857.
DR PDB; 5RY0; X-ray; 1.98 A; A=397-857.
DR PDB; 5RY1; X-ray; 1.52 A; A=397-857.
DR PDB; 5RY2; X-ray; 1.54 A; A=397-857.
DR PDB; 5RY3; X-ray; 1.50 A; A=397-857.
DR PDB; 5RY4; X-ray; 1.47 A; A=397-857.
DR PDB; 5RY5; X-ray; 1.54 A; A=397-857.
DR PDB; 5RY6; X-ray; 1.74 A; A=397-857.
DR PDB; 5RY7; X-ray; 1.60 A; A=397-857.
DR PDB; 5RY8; X-ray; 1.43 A; A=397-857.
DR PDB; 5RY9; X-ray; 1.52 A; A=397-857.
DR PDB; 5RYA; X-ray; 1.32 A; A=397-857.
DR PDB; 5RYB; X-ray; 1.55 A; A=397-857.
DR PDB; 5RYC; X-ray; 1.56 A; A=397-857.
DR PDB; 5RYD; X-ray; 1.60 A; A=397-857.
DR PDB; 5RYE; X-ray; 1.70 A; A=397-857.
DR PDB; 5RYF; X-ray; 1.49 A; A=397-857.
DR PDB; 5RYG; X-ray; 1.47 A; A=397-857.
DR PDB; 5RYH; X-ray; 1.72 A; A=397-857.
DR PDB; 5RYI; X-ray; 1.45 A; A=397-857.
DR PDB; 5RYJ; X-ray; 1.42 A; A=397-857.
DR PDB; 5RYK; X-ray; 1.55 A; A=397-857.
DR PDB; 5RYL; X-ray; 1.55 A; A=397-857.
DR PDB; 6IBD; X-ray; 1.48 A; A=397-857.
DR PDB; 6XY7; X-ray; 1.09 A; AAA=397-857.
DR PDBsum; 2YSX; -.
DR PDBsum; 5RW2; -.
DR PDBsum; 5RW3; -.
DR PDBsum; 5RW4; -.
DR PDBsum; 5RW5; -.
DR PDBsum; 5RW6; -.
DR PDBsum; 5RW7; -.
DR PDBsum; 5RW8; -.
DR PDBsum; 5RW9; -.
DR PDBsum; 5RWA; -.
DR PDBsum; 5RWB; -.
DR PDBsum; 5RWC; -.
DR PDBsum; 5RWD; -.
DR PDBsum; 5RWE; -.
DR PDBsum; 5RWF; -.
DR PDBsum; 5RWG; -.
DR PDBsum; 5RWH; -.
DR PDBsum; 5RWI; -.
DR PDBsum; 5RWJ; -.
DR PDBsum; 5RWK; -.
DR PDBsum; 5RWL; -.
DR PDBsum; 5RWM; -.
DR PDBsum; 5RWN; -.
DR PDBsum; 5RWO; -.
DR PDBsum; 5RWP; -.
DR PDBsum; 5RWQ; -.
DR PDBsum; 5RWR; -.
DR PDBsum; 5RWS; -.
DR PDBsum; 5RWT; -.
DR PDBsum; 5RWU; -.
DR PDBsum; 5RWV; -.
DR PDBsum; 5RWW; -.
DR PDBsum; 5RWX; -.
DR PDBsum; 5RWY; -.
DR PDBsum; 5RWZ; -.
DR PDBsum; 5RX0; -.
DR PDBsum; 5RX1; -.
DR PDBsum; 5RX2; -.
DR PDBsum; 5RX3; -.
DR PDBsum; 5RX4; -.
DR PDBsum; 5RX5; -.
DR PDBsum; 5RX6; -.
DR PDBsum; 5RX7; -.
DR PDBsum; 5RX8; -.
DR PDBsum; 5RX9; -.
DR PDBsum; 5RXA; -.
DR PDBsum; 5RXB; -.
DR PDBsum; 5RXC; -.
DR PDBsum; 5RXD; -.
DR PDBsum; 5RXE; -.
DR PDBsum; 5RXF; -.
DR PDBsum; 5RXG; -.
DR PDBsum; 5RXH; -.
DR PDBsum; 5RXI; -.
DR PDBsum; 5RXJ; -.
DR PDBsum; 5RXK; -.
DR PDBsum; 5RXL; -.
DR PDBsum; 5RXM; -.
DR PDBsum; 5RXO; -.
DR PDBsum; 5RXP; -.
DR PDBsum; 5RXQ; -.
DR PDBsum; 5RXR; -.
DR PDBsum; 5RXS; -.
DR PDBsum; 5RXT; -.
DR PDBsum; 5RXU; -.
DR PDBsum; 5RXV; -.
DR PDBsum; 5RXW; -.
DR PDBsum; 5RXX; -.
DR PDBsum; 5RXY; -.
DR PDBsum; 5RXZ; -.
DR PDBsum; 5RY0; -.
DR PDBsum; 5RY1; -.
DR PDBsum; 5RY2; -.
DR PDBsum; 5RY3; -.
DR PDBsum; 5RY4; -.
DR PDBsum; 5RY5; -.
DR PDBsum; 5RY6; -.
DR PDBsum; 5RY7; -.
DR PDBsum; 5RY8; -.
DR PDBsum; 5RY9; -.
DR PDBsum; 5RYA; -.
DR PDBsum; 5RYB; -.
DR PDBsum; 5RYC; -.
DR PDBsum; 5RYD; -.
DR PDBsum; 5RYE; -.
DR PDBsum; 5RYF; -.
DR PDBsum; 5RYG; -.
DR PDBsum; 5RYH; -.
DR PDBsum; 5RYI; -.
DR PDBsum; 5RYJ; -.
DR PDBsum; 5RYK; -.
DR PDBsum; 5RYL; -.
DR PDBsum; 6IBD; -.
DR PDBsum; 6XY7; -.
DR AlphaFoldDB; Q92835; -.
DR SMR; Q92835; -.
DR BioGRID; 109847; 52.
DR ELM; Q92835; -.
DR IntAct; Q92835; 75.
DR MINT; Q92835; -.
DR STRING; 9606.ENSP00000405338; -.
DR ChEMBL; CHEMBL1781870; -.
DR SwissLipids; SLP:000000951; -.
DR DEPOD; INPP5D; -.
DR GlyGen; Q92835; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q92835; -.
DR PhosphoSitePlus; Q92835; -.
DR BioMuta; INPP5D; -.
DR DMDM; 158564077; -.
DR EPD; Q92835; -.
DR jPOST; Q92835; -.
DR MassIVE; Q92835; -.
DR MaxQB; Q92835; -.
DR PaxDb; Q92835; -.
DR PeptideAtlas; Q92835; -.
DR PRIDE; Q92835; -.
DR ProteomicsDB; 75518; -. [Q92835-1]
DR ProteomicsDB; 75519; -. [Q92835-2]
DR ProteomicsDB; 75520; -. [Q92835-3]
DR Antibodypedia; 4272; 578 antibodies from 44 providers.
DR DNASU; 3635; -.
DR Ensembl; ENST00000359570.9; ENSP00000352575.7; ENSG00000168918.14. [Q92835-2]
DR Ensembl; ENST00000445964.6; ENSP00000405338.2; ENSG00000168918.14. [Q92835-1]
DR Ensembl; ENST00000629761.2; ENSP00000486669.1; ENSG00000281614.3. [Q92835-2]
DR Ensembl; ENST00000630854.3; ENSP00000487191.1; ENSG00000281614.3. [Q92835-1]
DR GeneID; 3635; -.
DR KEGG; hsa:3635; -.
DR MANE-Select; ENST00000445964.6; ENSP00000405338.2; NM_001017915.3; NP_001017915.1.
DR UCSC; uc032ovq.2; human. [Q92835-1]
DR CTD; 3635; -.
DR DisGeNET; 3635; -.
DR GeneCards; INPP5D; -.
DR HGNC; HGNC:6079; INPP5D.
DR HPA; ENSG00000168918; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 601582; gene.
DR neXtProt; NX_Q92835; -.
DR NIAGADS; ENSG00000168918; -.
DR OpenTargets; ENSG00000168918; -.
DR PharmGKB; PA29887; -.
DR VEuPathDB; HostDB:ENSG00000168918; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156202; -.
DR InParanoid; Q92835; -.
DR OMA; DSWFQCK; -.
DR OrthoDB; 311217at2759; -.
DR PhylomeDB; Q92835; -.
DR TreeFam; TF323475; -.
DR BioCyc; MetaCyc:HS09849-MON; -.
DR BRENDA; 3.1.3.86; 2681.
DR PathwayCommons; Q92835; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-210990; PECAM1 interactions.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR SignaLink; Q92835; -.
DR SIGNOR; Q92835; -.
DR BioGRID-ORCS; 3635; 13 hits in 266 CRISPR screens.
DR ChiTaRS; INPP5D; human.
DR EvolutionaryTrace; Q92835; -.
DR GeneWiki; INPP5D; -.
DR GenomeRNAi; 3635; -.
DR Pharos; Q92835; Tbio.
DR PRO; PR:Q92835; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q92835; protein.
DR Bgee; ENSG00000168918; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q92835; baseline and differential.
DR Genevisible; Q92835; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; TAS:Reactome.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
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:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
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; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane; Cytoplasm;
KW Cytoskeleton; Hydrolase; Immunity; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3-binding.
FT CHAIN 1..1189
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 5-
FT phosphatase 1"
FT /id="PRO_0000302866"
FT DOMAIN 5..101
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 103..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1030
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000250"
FT MOTIF 124..129
FT /note="SH3-binding 1"
FT MOTIF 912..915
FT /note="NPXY motif 1"
FT MOTIF 969..974
FT /note="SH3-binding 2"
FT MOTIF 1019..1022
FT /note="NPXY motif 2"
FT MOTIF 1040..1051
FT /note="SH3-binding 3"
FT COMPBIAS 104..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES52"
FT MOD_RES 915
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES52"
FT MOD_RES 944
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES52"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 963
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1022
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES52"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8723348"
FT /id="VSP_027977"
FT VAR_SEQ 117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8769125, ECO:0000303|PubMed:8874179"
FT /id="VSP_027978"
FT VAR_SEQ 213..222
FT /note="TTLLCKELYG -> MFTLSPAPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8723348"
FT /id="VSP_027979"
FT VARIANT 685
FT /note="V -> E (in one patient with acute myeloid leukemya;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:12529653"
FT /id="VAR_034979"
FT VARIANT 1169
FT /note="H -> Y (in dbSNP:rs9247)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8769125"
FT /id="VAR_059358"
FT CONFLICT 25..26
FT /note="DG -> GT (in Ref. 4; AAB49680)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="P -> H (in Ref. 4; AAB49680)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2YSX"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2YSX"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2YSX"
FT STRAND 402..412
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 458..473
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:5RWW"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 502..511
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5RWW"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:5RWK"
FT STRAND 522..530
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:5RWB"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:5RWW"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 580..587
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 599..607
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 619..625
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 673..679
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 685..692
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 704..711
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 730..740
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 748..753
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:5RWW"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 801..808
FT /evidence="ECO:0007829|PDB:5RWW"
FT TURN 809..811
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 814..821
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 831..839
FT /evidence="ECO:0007829|PDB:5RWW"
FT STRAND 842..854
FT /evidence="ECO:0007829|PDB:5RWW"
SQ SEQUENCE 1189 AA; 133292 MW; 7958E91A64A4B68B CRC64;
MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED
DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEDTGD DPEEDTVESV
VSPPELPPRN IPLTASSCEA KEVPFSNENP RATETSRPSL SETLFQRLQS MDTSGLPEEH
LKAIQDYLST QLAQDSEFVK TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ
QLSPGLRPRP QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT
FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS QKFLNKLVIL
VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE PDMITIFIGT WNMGNAPPPK
KITSWFLSKG QGKTRDDSAD YIPHDIYVIG TQEDPLSEKE WLEILKHSLQ EITSVTFKTV
AIHTLWNIRI VVLAKPEHEN RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS
HLTSGSEKKL RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE
TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT RDKYAYTKQK
ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD HSPVFATFEA GVTSQFVSKN
GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL EFHSSCLESF VKSQEGENEE GSEGELVVKF
GETLPKLKPI ISDPEYLLDQ HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH
GELTGHFQGE IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP
PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD SPLGPCRGES
PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA GDTLPQEDLP LTKPEMFENP
LYGSLSSFPK PAPRKDQESP KMPRKEPPPC PEPGILSPSI VLTKAQEADR GEGPGKQVPA
PRLRSFTCSS SAEGRAAGGD KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR
PPLPVKSPAV LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ
