THB_MOUSE
ID THB_MOUSE Reviewed; 461 AA.
AC P37242; P37244; Q0VDR8; Q3TY80;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Thyroid hormone receptor beta;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2;
DE AltName: Full=c-erbA-2;
DE AltName: Full=c-erbA-beta;
GN Name=Thrb; Synonyms=Erba2, Nr1a2;
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] (ISOFORMS BETA-1 AND BETA-2).
RC TISSUE=Thyroid;
RX PubMed=1944303; DOI=10.1210/mend-5-8-1049;
RA Wood W.M., Ocran K.W., Gordon D.F., Ridgway E.C.;
RT "Isolation and characterization of mouse complementary DNAs encoding alpha
RT and beta thyroid hormone receptors from thyrotrope cells: the mouse
RT pituitary-specific beta 2 isoform differs at the amino terminus from the
RT corresponding species from rat pituitary tumor cells.";
RL Mol. Endocrinol. 5:1049-1061(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=7708051; DOI=10.1210/mend.8.12.7708051;
RA Wood W.M., Dowding J.M., Haugen B.R., Bright T.M., Gordon D.F.,
RA Ridgway E.C.;
RT "Structural and functional characterization of the genomic locus encoding
RT the murine beta 2 thyroid hormone receptor.";
RL Mol. Endocrinol. 8:1605-1617(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [5]
RP INTERACTION WITH C1D.
RX PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.;
RT "Cloning and characterization of a corepressor and potential component of
RT the nuclear hormone receptor repression complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
CC -!- FUNCTION: Nuclear hormone receptor that can act as a repressor or
CC activator of transcription. High affinity receptor for thyroid
CC hormones, including triiodothyronine and thyroxine.
CC -!- SUBUNIT: Binds DNA as a dimer; homodimer and heterodimer with RXRB.
CC Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and
CC MED1/TRAP220 in a ligand-inducible manner. Interacts with the
CC corepressor NCOR1 in absence of ligand (By similarity). Interacts with
CC C1D. Interacts with NR2F6; the interaction impairs the binding of the
CC THRB homodimer and THRB:RXRB heterodimer to T3 response elements.
CC Interacts with PRMT2 and THRSP (By similarity). Interacts with TACC1;
CC this interaction is decreased in the presence of thyroid hormone T3 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10828}.
CC -!- INTERACTION:
CC P37242; O08915: Aip; NbExp=2; IntAct=EBI-6935043, EBI-6935014;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-1;
CC IsoId=P37242-1; Sequence=Displayed;
CC Name=Beta-2;
CC IsoId=P37242-2, P37244-1;
CC Sequence=VSP_031078;
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; S62756; AAB20226.1; -; mRNA.
DR EMBL; S62758; AAB20227.1; -; mRNA.
DR EMBL; U15548; AAA86957.1; -; Genomic_DNA.
DR EMBL; U15542; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; U15543; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; U15544; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; U15545; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; U15546; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; U15547; AAA86957.1; JOINED; Genomic_DNA.
DR EMBL; AK158826; BAE34683.1; -; mRNA.
DR EMBL; BC089035; AAH89035.1; -; mRNA.
DR EMBL; BC119552; AAI19553.1; -; mRNA.
DR EMBL; BC119553; AAI19554.1; -; mRNA.
DR CCDS; CCDS26835.1; -. [P37242-2]
DR CCDS; CCDS49404.1; -. [P37242-1]
DR PIR; A40377; A40377.
DR PIR; A57035; A57035.
DR RefSeq; NP_001106888.1; NM_001113417.1. [P37242-1]
DR RefSeq; NP_033406.1; NM_009380.3. [P37242-2]
DR RefSeq; XP_006518029.1; XM_006517966.2. [P37242-1]
DR RefSeq; XP_006518030.1; XM_006517967.3. [P37242-1]
DR RefSeq; XP_006518031.1; XM_006517968.3. [P37242-1]
DR RefSeq; XP_006518033.1; XM_006517970.3. [P37242-1]
DR RefSeq; XP_006518034.1; XM_006517971.3. [P37242-1]
DR RefSeq; XP_006518035.1; XM_006517972.3. [P37242-1]
DR RefSeq; XP_011243039.1; XM_011244737.1. [P37242-1]
DR RefSeq; XP_011243040.1; XM_011244738.2. [P37242-1]
DR RefSeq; XP_011243041.1; XM_011244739.2. [P37242-1]
DR RefSeq; XP_011243042.1; XM_011244740.2. [P37242-1]
DR RefSeq; XP_011243043.1; XM_011244741.2. [P37242-1]
DR RefSeq; XP_011243044.1; XM_011244742.1. [P37242-1]
DR RefSeq; XP_011243045.1; XM_011244743.2. [P37242-1]
DR RefSeq; XP_017171435.1; XM_017315946.1.
DR RefSeq; XP_017171436.1; XM_017315947.1. [P37242-1]
DR AlphaFoldDB; P37242; -.
DR SMR; P37242; -.
DR BioGRID; 204184; 117.
DR ComplexPortal; CPX-710; RXRalpha-TRbeta nuclear hormone receptor complex.
DR DIP; DIP-43750N; -.
DR IntAct; P37242; 5.
DR MINT; P37242; -.
DR STRING; 10090.ENSMUSP00000022304; -.
DR PhosphoSitePlus; P37242; -.
DR MaxQB; P37242; -.
DR PaxDb; P37242; -.
DR PRIDE; P37242; -.
DR ProteomicsDB; 262913; -. [P37242-1]
DR ProteomicsDB; 262914; -. [P37242-2]
DR ABCD; P37242; 3 sequenced antibodies.
DR Antibodypedia; 4548; 505 antibodies from 42 providers.
DR DNASU; 21834; -.
DR Ensembl; ENSMUST00000022303; ENSMUSP00000022303; ENSMUSG00000021779. [P37242-1]
DR Ensembl; ENSMUST00000022304; ENSMUSP00000022304; ENSMUSG00000021779. [P37242-2]
DR Ensembl; ENSMUST00000091471; ENSMUSP00000089053; ENSMUSG00000021779. [P37242-1]
DR GeneID; 21834; -.
DR KEGG; mmu:21834; -.
DR UCSC; uc007shk.2; mouse. [P37242-1]
DR UCSC; uc007sho.2; mouse. [P37242-2]
DR CTD; 7068; -.
DR MGI; MGI:98743; Thrb.
DR VEuPathDB; HostDB:ENSMUSG00000021779; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156809; -.
DR HOGENOM; CLU_007368_18_2_1; -.
DR InParanoid; P37242; -.
DR OMA; YCMQELY; -.
DR OrthoDB; 1112927at2759; -.
DR PhylomeDB; P37242; -.
DR TreeFam; TF328382; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR BioGRID-ORCS; 21834; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Thrb; mouse.
DR PRO; PR:P37242; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P37242; protein.
DR Bgee; ENSMUSG00000021779; Expressed in auditory system and 84 other tissues.
DR ExpressionAtlas; P37242; baseline and differential.
DR Genevisible; P37242; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IMP:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
DR GO; GO:0008050; P:female courtship behavior; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007621; P:negative regulation of female receptivity; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; ISO:MGI.
DR GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:MGI.
DR GO; GO:0097474; P:retinal cone cell apoptotic process; IMP:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IGI:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00546; THYROIDHORMR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..461
FT /note="Thyroid hormone receptor beta"
FT /id="PRO_0000053448"
FT DOMAIN 217..461
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 107..181
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 107..127
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 145..169
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..106
FT /note="Modulating"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..461
FT /note="Interaction with NR2F6"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 282
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 282
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 331
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 331
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 435
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 435
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT VAR_SEQ 1..93
FT /note="MTPNSMTENGLPAWDKQKPRPDRGQDWKLVGMSEACLHRKSHVERRGALKNE
FT QTSPHLIQATWTSSIFHLDPDDVNDQSISSAQTFQTEEKKC -> MNYCMPEVHEVCPA
FT ASSNCYMQVTDYLAYLEDSPALSGRDVQAVPSSSIYMEQAWAVNQPYTCSYPGNLFKSK
FT DSDLDMALSQSSQPAHLPEEKPFPQVQSPPHSQK (in isoform Beta-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1944303"
FT /id="VSP_031078"
FT CONFLICT 445
FT /note="E -> G (in Ref. 3; BAE34683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52630 MW; 99089194FC3E6B33 CRC64;
MTPNSMTENG LPAWDKQKPR PDRGQDWKLV GMSEACLHRK SHVERRGALK NEQTSPHLIQ
ATWTSSIFHL DPDDVNDQSI SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR
CITCEGCKGF FRRTIQKSLH PSYSCKYEGK CIIDKVTRNQ CQECRFKKCI YVGMATDLVL
DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK
QKRKFLPEDI GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED
QIILLKGCCM EIMSLRAAVR YDPDSETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL
SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK
LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D
