IRS2_MOUSE
ID IRS2_MOUSE Reviewed; 1321 AA.
AC P81122; B9EJW3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Insulin receptor substrate 2;
DE Short=IRS-2;
DE AltName: Full=4PS;
GN Name=Irs2;
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, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7675087; DOI=10.1038/377173a0;
RA Sun X.J., Wang L.-M., Zhang Y., Yenush L., Myers M.G. Jr., Glasheen E.,
RA Lane W.S., Pierce J.H., White M.F.;
RT "Role of IRS-2 in insulin and cytokine signalling.";
RL Nature 377:173-177(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP INTERACTION WITH PHIP.
RX PubMed=11018022; DOI=10.1074/jbc.c000611200;
RA Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT "Cloning and characterization of PHIP, a novel insulin receptor substrate-1
RT pleckstrin homology domain interacting protein.";
RL J. Biol. Chem. 275:40492-40497(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17636024; DOI=10.1128/mcb.02409-06;
RA Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
RA Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
RT "Identification of a WD40 repeat-containing isoform of PHIP as a novel
RT regulator of beta-cell growth and survival.";
RL Mol. Cell. Biol. 27:6484-6496(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-649, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; SER-388; THR-524;
RP SER-728; SER-907; SER-1151 AND SER-1165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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).
CC -!- FUNCTION: May mediate the control of various cellular processes by
CC insulin.
CC -!- SUBUNIT: Interacts with PHIP. {ECO:0000269|PubMed:11018022}.
CC -!- INTERACTION:
CC P81122; Q923E4: Sirt1; NbExp=2; IntAct=EBI-1369862, EBI-1802585;
CC P81122; P06213-1: INSR; Xeno; NbExp=8; IntAct=EBI-1369862, EBI-15558981;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17636024}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, lung, brain, liver, kidney, heart
CC and spleen.
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DR EMBL; BC147580; AAI47581.1; -; mRNA.
DR CCDS; CCDS52477.1; -.
DR RefSeq; NP_001074681.1; NM_001081212.1.
DR PDB; 3BU3; X-ray; 1.65 A; B=620-634.
DR PDB; 3BU5; X-ray; 2.10 A; B=620-634.
DR PDB; 3BU6; X-ray; 1.95 A; B=620-634.
DR PDBsum; 3BU3; -.
DR PDBsum; 3BU5; -.
DR PDBsum; 3BU6; -.
DR AlphaFoldDB; P81122; -.
DR SMR; P81122; -.
DR BioGRID; 239306; 3.
DR DIP; DIP-39500N; -.
DR IntAct; P81122; 7.
DR MINT; P81122; -.
DR STRING; 10090.ENSMUSP00000038514; -.
DR iPTMnet; P81122; -.
DR PhosphoSitePlus; P81122; -.
DR EPD; P81122; -.
DR jPOST; P81122; -.
DR MaxQB; P81122; -.
DR PaxDb; P81122; -.
DR PeptideAtlas; P81122; -.
DR PRIDE; P81122; -.
DR ProteomicsDB; 269334; -.
DR Antibodypedia; 25473; 376 antibodies from 37 providers.
DR DNASU; 384783; -.
DR Ensembl; ENSMUST00000040514; ENSMUSP00000038514; ENSMUSG00000038894.
DR GeneID; 384783; -.
DR KEGG; mmu:384783; -.
DR UCSC; uc009kuz.1; mouse.
DR CTD; 8660; -.
DR MGI; MGI:109334; Irs2.
DR VEuPathDB; HostDB:ENSMUSG00000038894; -.
DR eggNOG; ENOG502QUNU; Eukaryota.
DR GeneTree; ENSGT00940000161407; -.
DR HOGENOM; CLU_004902_1_0_1; -.
DR InParanoid; P81122; -.
DR OMA; LCYRPCP; -.
DR OrthoDB; 298675at2759; -.
DR PhylomeDB; P81122; -.
DR TreeFam; TF325994; -.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-112399; IRS-mediated signalling.
DR Reactome; R-MMU-112412; SOS-mediated signalling.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-198203; PI3K/AKT activation.
DR Reactome; R-MMU-2428928; IRS-related events triggered by IGF1R.
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-74713; IRS activation.
DR Reactome; R-MMU-74749; Signal attenuation.
DR Reactome; R-MMU-8853659; RET signaling.
DR Reactome; R-MMU-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR BioGRID-ORCS; 384783; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Irs2; mouse.
DR EvolutionaryTrace; P81122; -.
DR PRO; PR:P81122; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P81122; protein.
DR Bgee; ENSMUSG00000038894; Expressed in digit skin and 141 other tissues.
DR Genevisible; P81122; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IGI:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0033673; P:negative regulation of kinase activity; IMP:BHF-UCL.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:BHF-UCL.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IGI:MGI.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IGI:MGI.
DR GO; GO:0009749; P:response to glucose; IDA:BHF-UCL.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR CDD; cd01204; PTB_IRS; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039011; IRS.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10614; PTHR10614; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00628; INSULINRSI.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methylation;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1321
FT /note="Insulin receptor substrate 2"
FT /id="PRO_0000084240"
FT DOMAIN 16..144
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 191..295
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 536..539
FT /note="YXXM motif 1"
FT MOTIF 594..597
FT /note="YXXM motif 2"
FT MOTIF 649..652
FT /note="YXXM motif 3"
FT MOTIF 671..674
FT /note="YXXM motif 4"
FT MOTIF 734..737
FT /note="YXXM motif 5"
FT MOTIF 814..817
FT /note="YXXM motif 6"
FT MOTIF 1061..1064
FT /note="YXXM motif 7"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 524
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 536
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 576
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 649
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 671
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 771
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 911
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 970
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 1071
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4H2"
FT MOD_RES 1242
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 1303
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="A -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Q -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="M -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="M -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="M -> K (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="F -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="F -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="T -> S (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:3BU3"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:3BU3"
SQ SEQUENCE 1321 AA; 136763 MW; 823A5458DA21C9C7 CRC64;
MASAPLPGPP ASAGGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL RGPGTGGDEA
SAAGGSPPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN INKRADAKHK YLIALYTKDE
YFAVAAENEQ EQEGWYRALT DLVSEGRSGE GGSGTTGGSC SASLPGVLGG SAGAAGCDDN
YGLVTPATAV YREVWQVNLK PKGLGQSKNL TGVYRLCLSA RTIGFVKLNC EQPSVTLQLM
NIRRCGHSDS FFFIEVGRSA VTGPGELWMQ ADDSVVAQNI HETILEAMKA LKELFEFRPR
SKSQSSGSSA THPISVPGAR RHHHLVNLPP SQTGLVRRSR TDSLAATPPA AKCTSCRVRT
ASEGDGGAAG GAGTAGGRPM SVAGSPLSPG PVRAPLSRSH TLSAGCGGRP SKVTLAPAGG
ALQHSRSMSM PVAHSPPAAT SPGSLSSSSG HGSGSYPLPP GSHPHLPHPL HHPQGQRPSS
GSASASGSPS DPGFMSLDEY GSSPGDLRAF SSHRSNTPES IAETPPARDG SGGELYGYMS
MDRPLSHCGR PYRRVSGDGA QDLDRGLRKR TYSLTTPARQ RQVPQPSSAS LDEYTLMRAT
FSGSSGRLCP SFPASSPKVA YNPYPEDYGD IEIGSHKSSS SNLGADDGYM PMTPGAALRS
GGPNSCKSDD YMPMSPTSVS APKQILQPRL AAALPPSGAA VPAPPSGVGR TFPVNGGGYK
ASSPAESSPE DSGYMRMWCG SKLSMENPDP KLLPNGDYLN MSPSEAGTAG TPPDFSAALR
GGSEGLKGIP GHCYSSLPRS YKAPCSCSGD NDQYVLMSSP VGRILEEERL EPQATPGAGT
FGAAGGSHTQ PHHSAVPSSM RPSAIGGRPE GFLGQRCRAV RPTRLSLEGL QTLPSMQEYP
LPTEPKSPGE YINIDFGEAG TRLSPPAPPL LASAASSSSL LSASSPASSL GSGTPGTSSD
SRQRSPLSDY MNLDFSSPKS PKPSTRSGDT VGSMDGLLSP EASSPYPPLP PRPSTSPSSL
QQPLPPAPGD LYRLPPASAA TSQGPTAGSS MSSEPGDNGD YTEMAFGVAA TPPQPIVAPP
KPEGARVASP TSGLKRLSLM DQVSGVEAFL QVSQPPDPHR GAKVIRADPQ GGRRRHSSET
FSSTTTVTPV SPSFAHNSKR HNSASVENVS LRKSSEGSST LGGGDEPPTS PGQAQPLVAV
PPVPQARPWN PGQPGALIGC PGGSSSPMRR ETSVGFQNGL NYIAIDVRGE QGSLAQSQPQ
PGDKNSWSRT RSLGGLLGTV GGSGASGVCG GPGTGALPSA STYASIDFLS HHLKEATVVK
E
