ID P85B_MOUSE Reviewed; 722 AA. AC O08908; Q5U3K7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 04-NOV-2026, entry version 205. DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit beta; DE Short=PI3-kinase regulatory subunit beta; DE Short=PI3K regulatory subunit beta; DE Short=PtdIns-3-kinase regulatory subunit beta; DE AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta; DE Short=PI3-kinase subunit p85-beta; DE Short=PtdIns-3-kinase regulatory subunit p85-beta; GN Name=Pik3r2; 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]. RC STRAIN=NIH Swiss; RX PubMed=9582025; DOI=10.1038/sj.onc.1201695; RA Janssen J.W.G., Schleithhoff L., Bartram C.R., Schulz A.S.; RT "An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta RT subunit and HUMORF8, a putative deubiquitinating enzyme."; RL Oncogene 16:1767-1772(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Spleen; 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 [9] RP FUNCTION, AND INTERACTION WITH PIK3R1 AND XBP1. RX PubMed=20348926; DOI=10.1038/nm.2099; RA Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U.; RT "The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 RT and increase its nuclear translocation."; RL Nat. Med. 16:429-437(2010). RN [10] RP INTERACTION WITH NYAP1; NYAP2 AND MYO16. RX PubMed=21946561; DOI=10.1038/emboj.2011.348; RA Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y., RA Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.; RT "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in RT neurons."; RL EMBO J. 30:4739-4754(2011). CC -!- FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a CC kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5- CC bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate CC (PIP3). PIP3 plays a key role by recruiting PH domain-containing CC proteins to the membrane, including AKT1 and PDPK1, activating CC signaling cascades involved in cell growth, survival, proliferation, CC motility and morphology. Binds to activated (phosphorylated) protein- CC tyrosine kinases, through its SH2 domain, and acts as an adapter, CC mediating the association of the p110 catalytic unit to the plasma CC membrane. Indirectly regulates autophagy (By similarity). Promotes CC nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin- CC dependent manner during metabolic overloading in the liver and hence CC plays a role in glucose tolerance improvement (PubMed:20348926). CC {ECO:0000250|UniProtKB:O00459, ECO:0000269|PubMed:20348926}. CC -!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R2 and a p110 CC catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. CC Interacts with FLT1 (tyrosine-phosphorylated) and FLT4 (tyrosine- CC phosphorylated) (By similarity). Interacts with FBXL2; PIK3R2 is a CC substrate of the SCF(FBXL2) complex. Interacts with PTPN13; CC dephosphorylates PIK3R2 (By similarity). Interacts with NYAP1, NYAP2 CC and MYO16 (PubMed:21946561). Interacts with XBP1 isoform 2; the CC interaction is direct and induces translocation of XBP1 isoform 2 into CC the nucleus in a ER stress- and/or insulin-dependent but PI3K- CC independent manner (PubMed:20348926). Interacts with PIK3R1; the CC interaction is dissociated in an insulin-dependent manner CC (PubMed:20348926). Interacts with SRC (By similarity). CC {ECO:0000250|UniProtKB:O00459, ECO:0000269|PubMed:20348926, CC ECO:0000269|PubMed:21946561}. CC -!- INTERACTION: CC O08908; O88665: Brd7; NbExp=4; IntAct=EBI-643570, EBI-643930; CC O08908; Q9JK42: Pdk2; NbExp=3; IntAct=EBI-643570, EBI-643530; CC -!- DOMAIN: The SH2 2 domain is required for interaction with FBXL2 and CC PTPN13. {ECO:0000250|UniProtKB:O00459}. CC -!- PTM: Phosphorylated in response to signaling from activated receptor- CC type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at CC Tyr-649 by PTPN13. Phosphorylation of Tyr-649 impairs while its CC dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)- CC mediated polyubiquitination. {ECO:0000250|UniProtKB:O00459}. CC -!- PTM: Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex CC probably promotes proteasomal degradation of PIK3R2. CC {ECO:0000250|UniProtKB:O00459}. CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y13569; CAA73903.1; -; mRNA. DR EMBL; CH466569; EDL28873.1; -; Genomic_DNA. DR EMBL; BC006796; AAH06796.1; -; mRNA. DR EMBL; BC085501; AAH85501.1; -; mRNA. DR CCDS; CCDS22381.1; -. DR RefSeq; NP_032867.2; NM_008841.3. DR PDB; 2Y3A; X-ray; 3.30 A; B=423-722. DR AlphaFoldDB; O08908; -. DR SMR; O08908; -. DR BioGRID; 202163; 36. DR CORUM; O08908; -. DR FunCoup; O08908; 2153. DR IntAct; O08908; 27. DR STRING; 10090.ENSMUSP00000034296; -. DR ChEMBL; CHEMBL4106167; -. DR iPTMnet; O08908; -. DR PhosphoSitePlus; O08908; -. DR jPOST; O08908; -. DR PaxDb; 10090-ENSMUSP00000034296; -. DR PeptideAtlas; O08908; -. DR ProteomicsDB; 294423; -. DR Pumba; O08908; -. DR DNASU; 18709; -. DR Ensembl; ENSMPUT00000015859; ENSMPUP00000015618; ENSMPUG00000015727. DR Ensembl; ENSMUST00000034296.15; ENSMUSP00000034296.9; ENSMUSG00000031834.16. DR GeneID; 18709; -. DR KEGG; mmu:18709; -. DR UCSC; uc009mbn.2; mouse. DR AGR; MGI:1098772; -. DR CTD; 5296; -. DR MGI; MGI:1098772; Pik3r2. DR VEuPathDB; HostDB:ENSMUSG00000031834; -. DR eggNOG; KOG4637; Eukaryota. DR GeneTree; ENSGT00940000157050; -. DR HOGENOM; CLU_007031_1_0_1; -. DR InParanoid; O08908; -. DR OMA; ACAHVWA; -. DR OrthoDB; 3175255at2759; -. DR PhylomeDB; O08908; -. DR Reactome; R-MMU-109704; PI3K Cascade. DR Reactome; R-MMU-112399; IRS-mediated signalling. DR Reactome; R-MMU-114604; GPVI-mediated activation cascade. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-1266695; Interleukin-7 signaling. DR Reactome; R-MMU-1433557; Signaling by SCF-KIT. DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-MMU-186763; Downstream signal transduction. DR Reactome; R-MMU-198203; PI3K/AKT activation. DR Reactome; R-MMU-201556; Signaling by ALK. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis. DR Reactome; R-MMU-210993; Tie2 Signaling. DR Reactome; R-MMU-2424491; DAP12 signaling. DR Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization. DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-8853659; RET signaling. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-MMU-9013026; RHOB GTPase cycle. DR Reactome; R-MMU-9013148; CDC42 GTPase cycle. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013404; RAC2 GTPase cycle. DR Reactome; R-MMU-9013409; RHOJ GTPase cycle. DR Reactome; R-MMU-9013420; RHOU GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-9035034; RHOF GTPase cycle. DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling. DR Reactome; R-MMU-912631; Regulation of signaling by CBL. DR Reactome; R-MMU-9696264; RND3 GTPase cycle. DR Reactome; R-MMU-9696270; RND2 GTPase cycle. DR Reactome; R-MMU-9696273; RND1 GTPase cycle. DR Reactome; R-MMU-9842663; Signaling by LTK. DR Reactome; R-MMU-9927354; Co-stimulation by ICOS. DR BioGRID-ORCS; 18709; 5 hits in 82 CRISPR screens. DR EvolutionaryTrace; O08908; -. DR PRO; PR:O08908; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; O08908; protein. DR Bgee; ENSMUSG00000031834; Expressed in embryonic brain and 65 other cell types or tissues. DR ExpressionAtlas; O08908; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISO:GO_Central. DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central. DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0019903; F:protein phosphatase binding; ISO:GO_Central. DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:GO_Central. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB. DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0001678; P:intracellular glucose homeostasis; IDA:UniProtKB. DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:GO_Central. DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:GO_Central. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:MGI. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI. DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:MGI. DR GO; GO:0051492; P:regulation of stress fiber assembly; IMP:MGI. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB. DR CDD; cd12926; iSH2_PIK3R2; 1. DR CDD; cd09930; SH2_cSH2_p85_like; 1. DR CDD; cd09942; SH2_nSH2_p85_like; 1. DR CDD; cd11909; SH3_PI3K_p85beta; 1. DR DisProt; DP02791; -. DR FunFam; 3.30.505.10:FF:000006; Phosphatidylinositol 3-kinase regulatory subunit alpha; 1. DR FunFam; 3.30.505.10:FF:000014; Phosphatidylinositol 3-kinase regulatory subunit alpha; 1. DR FunFam; 2.30.30.40:FF:000075; phosphatidylinositol 3-kinase regulatory subunit alpha; 1. DR FunFam; 1.10.555.10:FF:000037; Phosphatidylinositol 3-kinase regulatory subunit beta; 1. DR FunFam; 1.10.287.1490:FF:000001; Putative phosphatidylinositol 3-kinase regulatory subunit alpha; 1. DR Gene3D; 1.10.287.1490; -; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR Gene3D; 3.30.505.10; SH2 domain; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR032498; PI3K_P85_iSH2. DR InterPro; IPR035586; PI3K_p85beta_SH3. DR InterPro; IPR035020; PI3kinase_P85_cSH2. DR InterPro; IPR035022; PI3kinase_P85_nSH2. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1. DR PANTHER; PTHR10155:SF1; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT BETA; 1. DR Pfam; PF16454; PI3K_P85_iSH2; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00017; SH2; 2. DR PRINTS; PR00678; PI3KINASEP85. DR PRINTS; PR00401; SH2DOMAIN. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00252; SH2; 2. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF55550; SH2 domain; 2. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50001; SH2; 2. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Phosphoprotein; Protein transport; Reference proteome; KW Repeat; SH2 domain; SH3 domain; Stress response; Transport; KW Ubl conjugation. FT CHAIN 1..722 FT /note="Phosphatidylinositol 3-kinase regulatory subunit FT beta" FT /id="PRO_0000080764" FT DOMAIN 4..80 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 112..293 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT DOMAIN 324..419 FT /note="SH2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 616..710 FT /note="SH2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT REGION 84..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 287..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..98 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 147 FT /note="Arginine finger; crucial for GTP hydrolysis by FT stabilizing the transition state" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT MOD_RES 458 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455, FT ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:18034455" FT MOD_RES 599 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O00459" FT MOD_RES 649 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O00459" FT CONFLICT 433 FT /note="I -> V (in Ref. 1; CAA73903 and 3; AAH06796)" FT /evidence="ECO:0000305" FT HELIX 448..451 FT /evidence="ECO:0007829|PDB:2Y3A" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 455..496 FT /evidence="ECO:0007829|PDB:2Y3A" FT TURN 508..510 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 511..557 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 559..568 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 609..611 FT /evidence="ECO:0007829|PDB:2Y3A" FT TURN 614..616 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 623..630 FT /evidence="ECO:0007829|PDB:2Y3A" FT STRAND 637..640 FT /evidence="ECO:0007829|PDB:2Y3A" FT STRAND 649..654 FT /evidence="ECO:0007829|PDB:2Y3A" FT STRAND 656..667 FT /evidence="ECO:0007829|PDB:2Y3A" FT STRAND 670..674 FT /evidence="ECO:0007829|PDB:2Y3A" FT HELIX 683..688 FT /evidence="ECO:0007829|PDB:2Y3A" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:2Y3A" FT TURN 696..698 FT /evidence="ECO:0007829|PDB:2Y3A" SQ SEQUENCE 722 AA; 81266 MW; A999FAF9011455FE CRC64; MAGAEGFQYR AVYPFRRERP EDLELLPGDL LVVSRVALQA LGVADGGERC PHNVGWMPGF NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP LDGSSESGHI LPDLAEQFSP PDPAPPILVK LVEAIEQAEL DSECYSKPEL PATRTDWSLS DLEQWDRTAL YDAVKGFLLA LPAAVVTPEA AAEAYRALRE VAGPVGLVLE PPTLPLHQAL TLRFLLQHLG RVARRAPSPD TAVHALASAF GPLLLRIPPS GGEGDGSEPV PDFPVLLLER LVQEHVEEQD AAPPALPPKP SKAKPAPTAL ANGGSPPSLQ DAEWYWGDIS REEVNERLRD TPDGTFLVRD ASSKIQGEYT LTLRKGGNNK LIKVFHRDGH YGFSEPLTFC SVVELISHYR HESLAQYNAK LDTRLLYPVS KYQQDQVVKE DSIEAVGAQL KVYHQQYQDK SREYDQLYEE YTRTSQELQM KRTAIEAFNE TIKIFEEQGQ TQEKCSKEYL ERFRREGNEK EMQRILLNSE RLKSRIAEIH ESRTKLEQDL RAQASDNREI DKRMNSLKPD LMQLRKIRDQ YLVWLTQKGA RQRKINEWLG IKNETEDQYS LMEDEDALPH HEERTWYVGK INRTQAEEML SGKRDGTFLI RESSQRGCYA CSVVVDGDTK HCVIYRTATG FGFAEPYNLY GSLKELVLHY QHASLVQHND ALTVTLAHPV RAPGPGPPSA AR //