TSC2_RAT
ID TSC2_RAT Reviewed; 1809 AA.
AC P49816;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tuberin;
DE AltName: Full=Tuberous sclerosis 2 protein homolog;
GN Name=Tsc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND DISEASE.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=8519695;
RA Xiao G.-H., Jin F., Yeung R.S.;
RT "Identification of tuberous sclerosis 2 messenger RNA splice variants that
RT are conserved and differentially expressed in rat and human tissues.";
RL Cell Growth Differ. 6:1185-1191(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Long Evans; TISSUE=Brain, and Kidney;
RX PubMed=7651821; DOI=10.1093/nar/23.14.2608;
RA Kobayashi T., Nishizawa M., Hirayama Y., Kobayashi E., Hino O.;
RT "cDNA structure, alternative splicing and exon-intron organization of the
RT predisposing tuberous sclerosis (Tsc2) gene of the Eker rat model.";
RL Nucleic Acids Res. 23:2608-2613(1995).
RN [3]
RP FUNCTION, AND INTERACTION WITH RABEP1.
RX PubMed=9045618; DOI=10.1074/jbc.272.10.6097;
RA Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S.;
RT "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase
RT activating protein (GAP) in modulating endocytosis.";
RL J. Biol. Chem. 272:6097-6100(1997).
RN [4]
RP MUTAGENESIS OF ASN-314 AND LEU-713.
RX PubMed=10029074;
RA Satake N., Kobayashi T., Kobayashi E., Izumi K., Hino O.;
RT "Isolation and characterization of a rat homologue of the human tuberous
RT sclerosis 1 gene (Tsc1) and analysis of its mutations in rat renal
RT carcinomas.";
RL Cancer Res. 59:849-855(1999).
RN [5]
RP FUNCTION.
RX PubMed=16707451; DOI=10.1158/0008-5472.can-05-4510;
RA Jiang X., Yeung R.S.;
RT "Regulation of microtubule-dependent protein transport by the
RT TSC2/mammalian target of rapamycin pathway.";
RL Cancer Res. 66:5258-5269(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1389 AND SER-1413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: In complex with TSC1, this tumor suppressor inhibits the
CC nutrient-mediated or growth factor-stimulated phosphorylation of S6K1
CC and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity).
CC Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a
CC direct activator of the protein kinase activity of mTORC1 (By
CC similarity). May also play a role in microtubule-mediated protein
CC transport (PubMed:16707451). Also stimulates the intrinsic GTPase
CC activity of the Ras-related proteins RAP1A and RAB5 (PubMed:9045618).
CC {ECO:0000250|UniProtKB:P49815, ECO:0000269|PubMed:16707451,
CC ECO:0000269|PubMed:9045618}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2 (By similarity). Probably forms a complex composed
CC of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and
CC client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not
CC contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a
CC complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit
CC TCS2 to the complex thereby stabilizing TSC2 (By similarity). Interacts
CC with TSC1 and HERC1; the interaction with TSC1 stabilizes TSC2 and
CC prevents the interaction with HERC1 (By similarity). May also interact
CC with the adapter molecule RABEP1 (PubMed:9045618). The final complex
CC may contain TSC2 and RABEP1 linked to RAB5 (PubMed:9045618). Interacts
CC with HSPA1 and HSPA8 (By similarity). Interacts with DAPK1 (By
CC similarity). Interacts with FBXW5 (By similarity). Interacts with NAA10
CC (via C-terminal domain) (By similarity). Interacts with RRAGA
CC (polyubiquitinated) (By similarity). Interacts with WDR45B (By
CC similarity). Interacts with RPAP3 and URI1 (By similarity). Interacts
CC with YWHAG (By similarity). {ECO:0000250|UniProtKB:P49815,
CC ECO:0000269|PubMed:9045618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P49816-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49816-2; Sequence=VSP_004481;
CC Name=3;
CC IsoId=P49816-3; Sequence=VSP_004482;
CC Name=4;
CC IsoId=P49816-4; Sequence=VSP_004481, VSP_004482;
CC -!- TISSUE SPECIFICITY: CNS, uterus, heart, skeletal muscle, kidney and
CC spleen.
CC -!- PTM: Phosphorylation at Ser-1388, Ser-1420 or Ser-1422 does not affect
CC interaction with TSC1. Phosphorylation at Ser-939 and Thr-1466 by
CC PKB/AKT1 is induced by growth factor stimulation. Phosphorylation by
CC AMPK activates it and leads to negative regulation of the mTORC1
CC complex. Phosphorylated at Ser-1800 by RPS6KA1; phosphorylation
CC inhibits TSC2 ability to suppress mTORC1 signaling. Phosphorylated by
CC DAPK1. {ECO:0000250|UniProtKB:P49815}.
CC -!- PTM: Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase
CC complex, leading to its subsequent degradation. Ubiquitinated by MYCBP2
CC independently of its phosphorylation status leading to subsequent
CC degradation; association with TSC1 protects from ubiquitination.
CC {ECO:0000250|UniProtKB:P49815}.
CC -!- DISEASE: Note=A germline insertion in Tsc2 is the cause of the Eker rat
CC model of inherited cancer susceptibility. Gives rise to a spectrum of
CC epithelial and nonepithelial neoplasms. {ECO:0000269|PubMed:8519695}.
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DR EMBL; U24150; AAC52289.1; -; mRNA.
DR EMBL; D50413; BAA08914.1; -; mRNA.
DR PIR; S57329; S57329.
DR RefSeq; NP_036812.2; NM_012680.3. [P49816-1]
DR RefSeq; XP_006245971.2; XM_006245909.3.
DR AlphaFoldDB; P49816; -.
DR SMR; P49816; -.
DR BioGRID; 246972; 9.
DR IntAct; P49816; 4.
DR MINT; P49816; -.
DR STRING; 10116.ENSRNOP00000016221; -.
DR iPTMnet; P49816; -.
DR PhosphoSitePlus; P49816; -.
DR PaxDb; P49816; -.
DR PRIDE; P49816; -.
DR GeneID; 24855; -.
DR KEGG; rno:24855; -.
DR UCSC; RGD:3908; rat. [P49816-1]
DR CTD; 7249; -.
DR RGD; 3908; Tsc2.
DR eggNOG; KOG3687; Eukaryota.
DR InParanoid; P49816; -.
DR OrthoDB; 341431at2759; -.
DR PhylomeDB; P49816; -.
DR TreeFam; TF324484; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-RNO-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR PRO; PR:P49816; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0033596; C:TSC1-TSC2 complex; ISO:RGD.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0043276; P:anoikis; ISO:RGD.
DR GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:RGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:RGD.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISO:RGD.
DR GO; GO:0046323; P:glucose import; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; ISO:RGD.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:RGD.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IMP:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IDA:RGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:RGD.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IMP:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:RGD.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0035176; P:social behavior; IMP:RGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR003913; Tuberin.
DR InterPro; IPR018515; Tuberin-type_domain.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR InterPro; IPR024584; Tuberin_N.
DR PANTHER; PTHR10063; PTHR10063; 3.
DR Pfam; PF11864; DUF3384; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF03542; Tuberin; 1.
DR PRINTS; PR01431; TUBERIN.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..1809
FT /note="Tuberin"
FT /id="PRO_0000065656"
FT DOMAIN 1533..1760
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 1078..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 927
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 939
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1466
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61037"
FT MOD_RES 1800
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT MOD_RES 1801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49815"
FT VAR_SEQ 947..989
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8519695"
FT /id="VSP_004481"
FT VAR_SEQ 1272..1294
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8519695"
FT /id="VSP_004482"
FT MUTAGEN 314
FT /note="N->S: In chemically induced renal carcinoma."
FT /evidence="ECO:0000269|PubMed:10029074"
FT MUTAGEN 713
FT /note="L->R: In chemically induced renal carcinoma."
FT /evidence="ECO:0000269|PubMed:10029074"
FT CONFLICT 932
FT /note="K -> S (in Ref. 2; BAA08914)"
FT /evidence="ECO:0000305"
FT CONFLICT 1514
FT /note="C -> F (in Ref. 2; BAA08914)"
FT /evidence="ECO:0000305"
FT CONFLICT 1730
FT /note="R -> S (in Ref. 2; BAA08914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1809 AA; 201278 MW; 6190BEFB45272664 CRC64;
MAKPTSKDSG LKEKFKILLG LGTSRPNPRC AEGKQTEFII TAEILRELSG ECGLNNRIRM
IGQICDVAKT KKLEEHAVEA LWKAVSDLLQ PERPPEARHA VLALLKAIVQ GQGDRLGVLR
ALFFKVIKDY PSNEDLHERL EVFKALTDNG RHITYLEEEL AEFVLQWMDV GLSSEFLLVL
VNLVKFNSCY LDEYIAPMVH MICLLCIRTV SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI
ITLCRTVNVK ELCEPCWKLM RNLLGTHLGH SAIYNMCRIM ENRSYMEDAP LLRGAVFFVG
MALWGAHRLY SLKNSPTSVL PSFYEAMTCP NEVVSYEIVL SITRLIKKYR KELQAVTWDI
LLDIIERLLQ QLQNLDSPEL RTIVHDLLTT VEELCDQNEF HGSQERYYEL VESYADQRPE
SSLLNLITYR AQSIHPAKDG WIQNLQLLME RFFRNECRSA VRIKVLDVLS FVLLINRQFY
EEELINSVVI SQLSHIPEDK DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS
PPLELEERDL AVYSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYETL ISHIQLHYKH
GYSLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCLCDCAE LDRASEKKAS
GPLSPPTGPP SPVPTGPAVR LGHLPYSLLF RVLLQCLKQE TDWKVLKLVL SKLPESLRYK
VLIFTSPCSV DQLSSALCSM LSAPKTLERL RGTPEGFSRT DLHLAVVPVL TALISYHNYL
DKTRQREMVY CLEQGLIYRC ASQCVVALAI CSVEMPDIII KALPVLVVKL THISATASMA
IPLLEFLSTL ARLPHLYRNF AAEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC
RLPFRKDFVP YITKGLRSNV LLSFDDTPEK DKFRARSTSL NERPKSLRIA RAPKQGLNNS
PPVKEFKESC AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSMAQ ADDNLKNLHL
ELTETCLDMM ARYVFSNFTA VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL
LGLDSGDLQG GSASSSDPGT HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG
VLDTSAPYTP GGPASLGAQA APAARPEKPC AGAQLPAAEK ANLAAYVPLL TQGWAEILVR
RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHRDTALY KSLSVPAAGT
AKPPTLPRSN TVASFSSLYQ PSCQGQLHRS VSWADSAVVL EEGSPGEAHV PVEPPELEDF
EAALGTDRHC QRPDAYSRSS SASSQEEKSH LEELAAGGIP IERAISSEGA RPTVDLSFQP
SQPLSKSSSS PELQTLQDIL GDLGDKTDIG RLSPEAKVRS QSGILDGEAA TWSAPGEESR
ITVPPEGPLP SSSPRSPSGL RPRGYTISDS APSRRGKRVE RDNFKSRTAA SSAEKVPGIN
PSFVFLQLYH SPFCGDESNK PILLPNESFE RSVQLLDQIP SYDTHKIAVL YVGEGQSSSE
LAILSNEHGS YRYTEFLTGL GRLIELKDCQ PDKVYLGGLD VCGEDGQFTY CWHDDIMQAV
FHIATLMPTK DVDKHRCDKK RHLGNDFVSI IYNDSGEDFK LGTIKGQFNF VHVIITPLDY
KCNLLTLQCR KDMEGLVDTS VAKIVSDRNL SFVARQMALH ANMASQVHHR RSNPTDIYPS
KWIARLRHIK RLRQRIREEV HYSNPSLPLM HPPAHTKVPA QAPTEATPTY ETGQRKRLIS
SVDDFTEFV
