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Database: UniProt
Entry: INSR_MOUSE
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Original site: INSR_MOUSE 
ID   INSR_MOUSE              Reviewed;        1372 AA.
AC   P15208; F8VPU4;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   24-JAN-2024, entry version 236.
DE   RecName: Full=Insulin receptor;
DE            Short=IR;
DE            EC=2.7.10.1;
DE   AltName: CD_antigen=CD220;
DE   Contains:
DE     RecName: Full=Insulin receptor subunit alpha;
DE   Contains:
DE     RecName: Full=Insulin receptor subunit beta;
DE   Flags: Precursor;
GN   Name=Insr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2557333; DOI=10.1016/s0021-9258(20)88221-0;
RA   Flores-Riveros J.R., Sibley E., Kastelic T., Lane M.D.;
RT   "Substrate phosphorylation catalyzed by the insulin receptor tyrosine
RT   kinase. Kinetic correlation to autophosphorylation of specific sites in the
RT   beta subunit.";
RL   J. Biol. Chem. 264:21557-21572(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX   PubMed=2602374; DOI=10.1073/pnas.86.24.9732;
RA   Sibley E., Kastelic T., Kelly T.J., Lane M.D.;
RT   "Characterization of the mouse insulin receptor gene promoter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9732-9736(1989).
RN   [4]
RP   INTERACTION WITH IRS1 AND IRS2, AND MUTAGENESIS OF TYR-989.
RX   PubMed=8626379; DOI=10.1074/jbc.271.11.5980;
RA   Sawka-Verhelle D., Tartare-Deckert S., White M.F., Van Obberghen E.;
RT   "Insulin receptor substrate-2 binds to the insulin receptor through its
RT   phosphotyrosine-binding domain and through a newly identified domain
RT   comprising amino acids 591-786.";
RL   J. Biol. Chem. 271:5980-5983(1996).
RN   [5]
RP   INTERACTION WITH SORBS1.
RX   PubMed=9447983; DOI=10.1128/mcb.18.2.872;
RA   Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.;
RT   "A novel, multifunctional c-Cbl binding protein in insulin receptor
RT   signaling in 3T3-L1 adipocytes.";
RL   Mol. Cell. Biol. 18:872-879(1998).
RN   [6]
RP   MUTAGENESIS OF TYR-989.
RX   PubMed=10207032; DOI=10.1074/jbc.274.17.12075;
RA   Chaika O.V., Chaika N., Volle D.J., Hayashi H., Ebina Y., Wang L.M.,
RA   Pierce J.H., Lewis R.E.;
RT   "Mutation of tyrosine 960 within the insulin receptor juxtamembrane domain
RT   impairs glucose transport but does not inhibit ligand-mediated
RT   phosphorylation of insulin receptor substrate-2 in 3T3-L1 adipocytes.";
RL   J. Biol. Chem. 274:12075-12080(1999).
RN   [7]
RP   INTERACTION WITH SOCS3.
RX   PubMed=10821852; DOI=10.1074/jbc.275.21.15985;
RA   Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D.,
RA   Van Obberghen E.;
RT   "SOCS-3 is an insulin-induced negative regulator of insulin signaling.";
RL   J. Biol. Chem. 275:15985-15991(2000).
RN   [8]
RP   PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
RX   PubMed=12612081; DOI=10.1128/mcb.23.6.2096-2108.2003;
RA   Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A.,
RA   Meng T.C., Tonks N.K., Tiganis T.;
RT   "Regulation of insulin receptor signaling by the protein tyrosine
RT   phosphatase TCPTP.";
RL   Mol. Cell. Biol. 23:2096-2108(2003).
RN   [9]
RP   INTERACTION WITH SOCS1 AND SOCS3.
RX   PubMed=15169905; DOI=10.1128/mcb.24.12.5434-5446.2004;
RA   Ueki K., Kondo T., Kahn C.R.;
RT   "Suppressor of cytokine signaling 1 (SOCS-1) and SOCS-3 cause insulin
RT   resistance through inhibition of tyrosine phosphorylation of insulin
RT   receptor substrate proteins by discrete mechanisms.";
RL   Mol. Cell. Biol. 24:5434-5446(2004).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [12]
RP   INTERACTION WITH ARRB2.
RX   PubMed=19122674; DOI=10.1038/nature07617;
RA   Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J.,
RA   Pei G.;
RT   "Deficiency of a beta-arrestin-2 signal complex contributes to insulin
RT   resistance.";
RL   Nature 457:1146-1149(2009).
RN   [13]
RP   PHOSPHORYLATION AT TYR-1179 AND TYR-1180.
RX   PubMed=20655470; DOI=10.1016/j.cell.2010.06.003;
RA   Ferron M., Wei J., Yoshizawa T., Del Fattore A., DePinho R.A., Teti A.,
RA   Ducy P., Karsenty G.;
RT   "Insulin signaling in osteoblasts integrates bone remodeling and energy
RT   metabolism.";
RL   Cell 142:296-308(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC   Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [15]
RP   INTERACTION WITH LMBRD1.
RX   PubMed=24078630; DOI=10.1074/jbc.m113.479527;
RA   Tseng L.T., Lin C.L., Tzen K.Y., Chang S.C., Chang M.F.;
RT   "LMBD1 protein serves as a specific adaptor for insulin receptor
RT   internalization.";
RL   J. Biol. Chem. 288:32424-32432(2013).
RN   [16]
RP   FUNCTION, INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION.
RX   PubMed=27322061; DOI=10.1172/jci84708;
RA   Schmidt V., Schulz N., Yan X., Schuermann A., Kempa S., Kern M.,
RA   Blueher M., Poy M.N., Olivecrona G., Willnow T.E.;
RT   "SORLA facilitates insulin receptor signaling in adipocytes and exacerbates
RT   obesity.";
RL   J. Clin. Invest. 126:2706-2720(2016).
CC   -!- FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic
CC       actions of insulin. Binding of insulin leads to phosphorylation of
CC       several intracellular substrates, including, insulin receptor
CC       substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling
CC       intermediates. Each of these phosphorylated proteins serve as docking
CC       proteins for other signaling proteins that contain Src-homology-2
CC       domains (SH2 domain) that specifically recognize different
CC       phosphotyrosine residues, including the p85 regulatory subunit of PI3K
CC       and SHP2. Phosphorylation of IRSs proteins lead to the activation of
CC       two main signaling pathways: the PI3K-AKT/PKB pathway, which is
CC       responsible for most of the metabolic actions of insulin, and the Ras-
CC       MAPK pathway, which regulates expression of some genes and cooperates
CC       with the PI3K pathway to control cell growth and differentiation.
CC       Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to
CC       the activation of PI3K and the generation of phosphatidylinositol-(3,
CC       4, 5)-triphosphate (PIP3), a lipid second messenger, which activates
CC       several PIP3-dependent serine/threonine kinases, such as PDPK1 and
CC       subsequently AKT/PKB. The net effect of this pathway is to produce a
CC       translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic
CC       vesicles to the cell membrane to facilitate glucose transport.
CC       Moreover, upon insulin stimulation, activated AKT/PKB is responsible
CC       for: anti-apoptotic effect of insulin by inducing phosphorylation of
CC       BAD; regulates the expression of gluconeogenic and lipogenic enzymes by
CC       controlling the activity of the winged helix or forkhead (FOX) class of
CC       transcription factors. Another pathway regulated by PI3K-AKT/PKB
CC       activation is mTORC1 signaling pathway which regulates cell growth and
CC       metabolism and integrates signals from insulin. AKT mediates insulin-
CC       stimulated protein synthesis by phosphorylating TSC2 thereby activating
CC       mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in
CC       mediating cell growth, survival and cellular differentiation of
CC       insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers
CC       the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to
CC       binding insulin, the insulin receptor can bind insulin-like growth
CC       factors (IGFI and IGFII). When present in a hybrid receptor with IGF1R,
CC       binds IGF1 (By similarity). In adipocytes, inhibits lipolysis
CC       (PubMed:27322061). {ECO:0000250, ECO:0000269|PubMed:27322061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- ACTIVITY REGULATION: Activated in response to insulin.
CC       Autophosphorylation activates the kinase activity. PTPN1, PTPRE and
CC       PTPRF dephosphorylate important tyrosine residues, thereby reducing
CC       INSR activity. Inhibited by ENPP1. GRB10 and GRB14 inhibit the
CC       catalytic activity of the INSR, they block access of substrates to the
CC       activated receptor. SOCS1 and SOCS3 act as negative regulators of INSR
CC       activity, they bind to the activated INRS and interfere with the
CC       phosphorylation of INSR substrates (By similarity). Interacts with
CC       PTPRF (By similarity). Interacts with ATIC; ATIC together with
CC       PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling
CC       netwok regulating INSR autophosphorylation and endocytosis (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P15127}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
CC       bonds. The alpha chains carry the insulin-binding regions, while the
CC       beta chains carry the kinase domain. Forms a hybrid receptor with
CC       IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta
CC       chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts
CC       with SORBS1 but dissociates from it following insulin stimulation.
CC       Binds SH2B2 (By similarity). Activated form of INSR interacts (via Tyr-
CC       989) with the PTB/PID domains of IRS1 and SHC1. The sequences
CC       surrounding the phosphorylated NPXY motif contribute differentially to
CC       either IRS1 or SHC1 recognition. Interacts (via tyrosines in the C-
CC       terminus) with IRS2 (via PTB domain and 591-786 AA); the 591-786 would
CC       be the primary anchor of IRS2 to INSR while the PTB domain would have a
CC       stabilizing action on the interaction with INSR. Interacts with the SH2
CC       domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro,
CC       when autophosphorylated on tyrosine residues. Interacts with SOCS7 (By
CC       similarity). Interacts (via the phosphorylated Tyr-989), with SOCS3.
CC       Interacts (via the phosphorylated Tyr-1175, Tyr-1179, Tyr-1180) with
CC       SOCS1. Interacts with CAV2 (tyrosine-phosphorylated form); the
CC       interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By
CC       similarity). Interacts with ARRB2. Interacts with GRB10; this
CC       interaction blocks the association between IRS1/IRS2 and INSR,
CC       significantly reduces insulin-stimulated tyrosine phosphorylation of
CC       IRS1 and IRS2 and thus decreases insulin signaling (By similarity).
CC       Interacts with GRB7 (By similarity). Interacts with PDPK1 (By
CC       similarity). Interacts (via Tyr-1180) with GRB14 (via BPS domain); this
CC       interaction protects the tyrosines in the activation loop from
CC       dephosphorylation, but promotes dephosphorylation of Tyr-989, this
CC       results in decreased interaction with, and phosphorylation of, IRS1 (By
CC       similarity). Interacts (via subunit alpha) with ENPP1 (via 485-599 AA);
CC       this interaction blocks autophosphorylation (By similarity). Interacts
CC       with PTPRE; this interaction is dependent of Tyr-1175, Tyr-1179 and
CC       Tyr-1180 of the INSR (By similarity). Interacts with STAT5B (via SH2
CC       domain) (By similarity). Interacts with PTPRF (By similarity).
CC       Interacts with the insulin receptor SORL1; this interaction strongly
CC       increases its surface exposure, hence strengthens insulin signal
CC       reception (PubMed:27322061). Interacts (tyrosine phosphorylated) with
CC       CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation
CC       of the INSR C-terminal region (By similarity). Interacts with GNAI3;
CC       the interaction is probably mediated by CCDC88A/GIV (By similarity).
CC       Interacts with LMBRD1 (PubMed:24078630). Interacts (in response to
CC       insulin stimulation) with NCK1; this interaction may recruit PTPN1 to
CC       mediate INSR dephosphorylation (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P06213, ECO:0000269|PubMed:24078630,
CC       ECO:0000269|PubMed:27322061}.
CC   -!- INTERACTION:
CC       P15208; P49817: Cav1; NbExp=2; IntAct=EBI-6999015, EBI-1161338;
CC       P15208; Q60760: Grb10; NbExp=6; IntAct=EBI-6999015, EBI-861810;
CC       P15208; Q1XH17: Trim72; NbExp=2; IntAct=EBI-6999015, EBI-16034016;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27322061};
CC       Single-pass type I membrane protein {ECO:0000305}. Recycling endosome
CC       membrane {ECO:0000269|PubMed:27322061}. Late endosome
CC       {ECO:0000269|PubMed:27322061}. Lysosome {ECO:0000305|PubMed:27322061}.
CC       Note=Binding of insulin to INSR induces internalization and lysosomal
CC       degradation of the receptor, a means for down-regulating this signaling
CC       pathway after stimulation. In the presence of SORL1, internalized INSR
CC       molecules are redirected back to the cell surface, thereby preventing
CC       their lysosomal catabolism and strengthening insulin signal reception.
CC       {ECO:0000269|PubMed:27322061}.
CC   -!- DOMAIN: The tetrameric insulin receptor binds insulin via non-identical
CC       regions from two alpha chains, primarily via the C-terminal region of
CC       the first INSR alpha chain. Residues from the leucine-rich N-terminus
CC       of the other INSR alpha chain also contribute to this insulin binding
CC       site. A secondary insulin-binding site is formed by residues at the
CC       junction of fibronectin type-III domain 1 and 2 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on tyrosine residues in response to insulin (By
CC       similarity). Phosphorylation of Tyr-989 is required for IRS1-, SHC1-,
CC       and STAT5B-binding (By similarity). Dephosphorylated by PTPRE on Tyr-
CC       989, Tyr-1175, Tyr-1179 and Tyr-1180 residues (By similarity).
CC       Dephosphorylated by PTPRF and PTPN1 (By similarity). Dephosphorylated
CC       by PTPN2 and Ptprv; down-regulates insulin-induced signaling
CC       (PubMed:12612081, PubMed:20655470). {ECO:0000250,
CC       ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:20655470}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; J05149; AAA39318.1; -; mRNA.
DR   EMBL; AC168068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M28869; AAA39319.1; -; Genomic_DNA.
DR   CCDS; CCDS22059.1; -.
DR   PIR; A34157; A34157.
DR   RefSeq; NP_034698.2; NM_010568.3.
DR   PDB; 1LK2; X-ray; 1.35 A; P=423-430.
DR   PDB; 7SL1; EM; 3.40 A; A/B=1-1372.
DR   PDB; 7SL2; EM; 3.60 A; A/B=1-1372.
DR   PDB; 7SL3; EM; 3.40 A; A/B=1-1372.
DR   PDB; 7SL4; EM; 5.00 A; A/B=1-1372.
DR   PDB; 7SL6; EM; 3.70 A; A/B=1-1372.
DR   PDB; 7SL7; EM; 3.10 A; A/B=1-1372.
DR   PDB; 7STH; EM; 3.50 A; A/B=1-1372.
DR   PDB; 7STI; EM; 4.90 A; A/B=1-1372.
DR   PDB; 7STJ; EM; 4.40 A; A/B=1-1372.
DR   PDB; 7STK; EM; 4.00 A; A/B=1-1372.
DR   PDB; 8DTL; EM; 5.40 A; A/B=28-1372.
DR   PDB; 8DTM; EM; 3.50 A; A/B=28-1372.
DR   PDB; 8EYX; EM; 4.50 A; A/B=28-1372.
DR   PDB; 8EYY; EM; 4.90 A; A/B=28-1372.
DR   PDB; 8EZ0; EM; 3.70 A; A/B=28-1372.
DR   PDBsum; 1LK2; -.
DR   PDBsum; 7SL1; -.
DR   PDBsum; 7SL2; -.
DR   PDBsum; 7SL3; -.
DR   PDBsum; 7SL4; -.
DR   PDBsum; 7SL6; -.
DR   PDBsum; 7SL7; -.
DR   PDBsum; 7STH; -.
DR   PDBsum; 7STI; -.
DR   PDBsum; 7STJ; -.
DR   PDBsum; 7STK; -.
DR   PDBsum; 8DTL; -.
DR   PDBsum; 8DTM; -.
DR   PDBsum; 8EYX; -.
DR   PDBsum; 8EYY; -.
DR   PDBsum; 8EZ0; -.
DR   AlphaFoldDB; P15208; -.
DR   BMRB; P15208; -.
DR   EMDB; EMD-25188; -.
DR   EMDB; EMD-25189; -.
DR   EMDB; EMD-25190; -.
DR   EMDB; EMD-25191; -.
DR   EMDB; EMD-25192; -.
DR   EMDB; EMD-25193; -.
DR   EMDB; EMD-25428; -.
DR   EMDB; EMD-25429; -.
DR   EMDB; EMD-25430; -.
DR   EMDB; EMD-25431; -.
DR   EMDB; EMD-27704; -.
DR   EMDB; EMD-27705; -.
DR   EMDB; EMD-28723; -.
DR   EMDB; EMD-28724; -.
DR   EMDB; EMD-28725; -.
DR   SMR; P15208; -.
DR   BioGRID; 200774; 29.
DR   CORUM; P15208; -.
DR   DIP; DIP-41452N; -.
DR   IntAct; P15208; 21.
DR   MINT; P15208; -.
DR   STRING; 10090.ENSMUSP00000088837; -.
DR   BindingDB; P15208; -.
DR   ChEMBL; CHEMBL3187; -.
DR   CarbonylDB; P15208; -.
DR   GlyConnect; 2393; 7 N-Linked glycans (4 sites).
DR   GlyCosmos; P15208; 18 sites, 7 glycans.
DR   GlyGen; P15208; 19 sites, 7 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P15208; -.
DR   PhosphoSitePlus; P15208; -.
DR   jPOST; P15208; -.
DR   MaxQB; P15208; -.
DR   PaxDb; 10090-ENSMUSP00000088837; -.
DR   PeptideAtlas; P15208; -.
DR   ProteomicsDB; 267252; -.
DR   Pumba; P15208; -.
DR   Antibodypedia; 3403; 2540 antibodies from 53 providers.
DR   DNASU; 16337; -.
DR   Ensembl; ENSMUST00000091291.5; ENSMUSP00000088837.5; ENSMUSG00000005534.11.
DR   GeneID; 16337; -.
DR   KEGG; mmu:16337; -.
DR   UCSC; uc009krc.2; mouse.
DR   AGR; MGI:96575; -.
DR   CTD; 3643; -.
DR   MGI; MGI:96575; Insr.
DR   VEuPathDB; HostDB:ENSMUSG00000005534; -.
DR   eggNOG; KOG4258; Eukaryota.
DR   GeneTree; ENSGT00940000155404; -.
DR   HOGENOM; CLU_000288_166_0_1; -.
DR   InParanoid; P15208; -.
DR   OMA; WTEATHF; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; P15208; -.
DR   TreeFam; TF351636; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-MMU-74713; IRS activation.
DR   Reactome; R-MMU-74749; Signal attenuation.
DR   Reactome; R-MMU-74751; Insulin receptor signalling cascade.
DR   Reactome; R-MMU-74752; Signaling by Insulin receptor.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   BioGRID-ORCS; 16337; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Insr; mouse.
DR   EvolutionaryTrace; P15208; -.
DR   PRO; PR:P15208; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P15208; Protein.
DR   Bgee; ENSMUSG00000005534; Expressed in pigmented layer of retina and 217 other cell types or tissues.
DR   ExpressionAtlas; P15208; baseline and differential.
DR   Genevisible; P15208; MM.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005901; C:caveola; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0005899; C:insulin receptor complex; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR   GO; GO:0031981; C:nuclear lumen; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060417; C:yolk; ISO:MGI.
DR   GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; ISO:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0038024; F:cargo receptor activity; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0043559; F:insulin binding; ISS:UniProtKB.
DR   GO; GO:0005009; F:insulin receptor activity; IDA:MGI.
DR   GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
DR   GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR   GO; GO:0031405; F:lipoic acid binding; ISO:MGI.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0051425; F:PTB domain binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR   GO; GO:0030325; P:adrenal gland development; IGI:CACAO.
DR   GO; GO:0097242; P:amyloid-beta clearance; ISO:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR   GO; GO:0097062; P:dendritic spine maintenance; ISO:MGI.
DR   GO; GO:0008544; P:epidermis development; IMP:MGI.
DR   GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; ISO:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0008584; P:male gonad development; IGI:CACAO.
DR   GO; GO:0030238; P:male sex determination; IMP:MGI.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:1990535; P:neuron projection maintenance; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IGI:CACAO.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
DR   GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR   GO; GO:0051446; P:positive regulation of meiotic cell cycle; IGI:CACAO.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:BHF-UCL.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:MGI.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; ISO:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; IDA:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045995; P:regulation of embryonic development; ISO:MGI.
DR   GO; GO:2000194; P:regulation of female gonad development; IGI:CACAO.
DR   GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:MGI.
DR   GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05061; PTKc_InsR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040969; Insulin_TMD.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF17870; Insulin_TMD; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell membrane;
KW   Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein;
KW   Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..27
FT   CHAIN           28..748
FT                   /note="Insulin receptor subunit alpha"
FT                   /id="PRO_0000016693"
FT   CHAIN           753..1372
FT                   /note="Insulin receptor subunit beta"
FT                   /id="PRO_0000016695"
FT   TOPO_DOM        28..748
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        753..946
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        947..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        968..1372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          626..728
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          744..838
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          843..937
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1013..1288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          688..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..743
FT                   /note="Insulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          986..989
FT                   /note="Important for interaction with IRS1, SHC1 and
FT                   STAT5B"
FT                   /evidence="ECO:0000250"
FT   REGION          1349..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1351..1354
FT                   /note="PIK3R1 binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1149
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         1023
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1047
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         1094..1100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1153..1154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            66
FT                   /note="Insulin-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         401
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         989
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         1175
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         1179
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:20655470"
FT   MOD_RES         1180
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:20655470"
FT   MOD_RES         1345
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   MOD_RES         1351
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P06213"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        541
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        635
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        653
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        700
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        759
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        910
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        923
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        153..182
FT                   /evidence="ECO:0000250"
FT   DISULFID        186..209
FT                   /evidence="ECO:0000250"
FT   DISULFID        196..215
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..243
FT                   /evidence="ECO:0000250"
FT   DISULFID        239..252
FT                   /evidence="ECO:0000250"
FT   DISULFID        255..264
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..280
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..311
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..301
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..328
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        339..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        462..495
FT                   /evidence="ECO:0000250"
FT   DISULFID        551
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        676..889
FT                   /evidence="ECO:0000250"
FT   DISULFID        815..824
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         989
FT                   /note="Y->F: Abolishes interaction with IRS1 but not with
FT                   IRS2."
FT                   /evidence="ECO:0000269|PubMed:10207032,
FT                   ECO:0000269|PubMed:8626379"
FT   CONFLICT        1089
FT                   /note="T -> M (in Ref. 1; AAA39318)"
FT                   /evidence="ECO:0000305"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          88..93
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            187..192
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          198..207
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          209..213
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          223..226
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          252..260
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           283..294
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          308..314
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          319..321
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          327..330
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   HELIX           342..344
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           351..355
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            356..359
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          361..365
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           378..384
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          390..393
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          395..399
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            422..424
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          425..430
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            441..443
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          452..457
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           463..473
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           476..478
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          486..490
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          502..507
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           524..526
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          527..536
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          538..540
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          557..561
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          579..582
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          590..599
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          603..605
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          610..612
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          615..618
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          628..633
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          636..638
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          640..645
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          656..663
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           668..672
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          677..679
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   HELIX           718..742
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          788..793
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          795..799
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          807..816
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   TURN            819..821
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          828..833
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          838..842
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          848..851
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          853..855
FT                   /evidence="ECO:0007829|PDB:7SL1"
FT   STRAND          857..860
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          871..880
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          886..891
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   HELIX           892..898
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          900..903
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          908..921
FT                   /evidence="ECO:0007829|PDB:7SL7"
FT   STRAND          930..933
FT                   /evidence="ECO:0007829|PDB:7SL1"
SQ   SEQUENCE   1372 AA;  155610 MW;  B0FA7DBD2AD4646A CRC64;
     MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL
     QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
     VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE
     ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL
     GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG
     CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC
     TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL
     EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
     RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ
     NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT
     FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY
     WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ
     ILKELEESSF RKTFEDYLHN VVFVPRPSRK RRSLEEVGNV TATTLTLPDF PNVSSTIVPT
     SQEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA
     DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG
     CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG PLIFVFLFSV
     VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV YVPDEWEVPR EKITLLRELG
     QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL
     GVVSKGQPTL VVMELMAHGD LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL
     NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD
     GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN CPERLTDLMR
     MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK APESEELEME FEDMENVPLD
     RSSHCQREEA GGREGGSSLS IKRTYDEHIP YTHMNGGKKN GRVLTLPRSN PS
//
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