FOXA2_HUMAN
ID FOXA2_HUMAN Reviewed; 457 AA.
AC Q9Y261; Q8WUW4; Q96DF7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Hepatocyte nuclear factor 3-beta;
DE Short=HNF-3-beta;
DE Short=HNF-3B;
DE AltName: Full=Forkhead box protein A2;
DE AltName: Full=Transcription factor 3B;
DE Short=TCF-3B;
GN Name=FOXA2; Synonyms=HNF3B, TCF3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT VAL-328.
RC TISSUE=Liver;
RX PubMed=10672453; DOI=10.1007/s001250050016;
RA Yamada S., Zhu Q., Aihara Y., Onda H., Zhang Z., Yu L., Jin L., Si Y.J.,
RA Nishigori H., Tomura H., Inoue I., Morikawa A., Yamagata K., Hanafusa T.,
RA Matsuzawa Y., Takeda J.;
RT "Cloning of cDNA and the gene encoding human hepatocyte nuclear factor
RT (HNF)-3 beta and mutation screening in Japanese subjects with maturity-
RT onset diabetes of the young.";
RL Diabetologia 43:121-124(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hinokio Y., Horikawa Y., Furuta H., Cox N.J., Iwasaki N., Honda M.,
RA Ogata M., Iwamoto Y., Bell G.I.;
RT "No evidence for diabetes-associated mutations in the hepatocyte nuclear
RT factor-3 beta gene in Japanese patients with MODY.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10899756; DOI=10.1159/000022943;
RA Navas M.A., Vaisse C., Boger S., Heimesaat M., Kollee L.A., Stoffel M.;
RT "The human HNF-3 genes: cloning, partial sequence and mutation screening in
RT patients with impaired glucose homeostasis.";
RL Hum. Hered. 50:370-381(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14500912; DOI=10.1073/pnas.1931483100;
RA Wolfrum C., Besser D., Luca E., Stoffel M.;
RT "Insulin regulates the activity of forkhead transcription factor Hnf-
RT 3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic
RT localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11624-11629(2003).
RN [7]
RP PROMOTER-BINDING.
RX PubMed=15737987; DOI=10.1074/jbc.m501973200;
RA Verschuur M., de Jong M., Felida L., de Maat M.P., Vos H.L.;
RT "A hepatocyte nuclear factor-3 site in the fibrinogen beta promoter is
RT important for interleukin 6-induced expression, and its activity is
RT influenced by the adjacent -148C/T polymorphism.";
RL J. Biol. Chem. 280:16763-16771(2005).
RN [8]
RP INTERACTION WITH FOXA1 AND FOXA3.
RX PubMed=19919681; DOI=10.1186/gb-2009-10-11-r129;
RA Motallebipour M., Ameur A., Reddy Bysani M.S., Patra K., Wallerman O.,
RA Mangion J., Barker M.A., McKernan K.J., Komorowski J., Wadelius C.;
RT "Differential binding and co-binding pattern of FOXA1 and FOXA3 and their
RT relation to H3K4me3 in HepG2 cells revealed by ChIP-seq.";
RL Genome Biol. 10:R129.0-R129.0(2009).
RN [9]
RP INTERACTION WITH PRKDC.
RX PubMed=19478084; DOI=10.1074/jbc.m109.016295;
RA Nock A., Ascano J.M., Jones T., Barrero M.J., Sugiyama N., Tomita M.,
RA Ishihama Y., Malik S.;
RT "Identification of DNA-dependent protein kinase as a cofactor for the
RT forkhead transcription factor FoxA2.";
RL J. Biol. Chem. 284:19915-19926(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-309, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Transcription factor that is involved in embryonic
CC development, establishment of tissue-specific gene expression and
CC regulation of gene expression in differentiated tissues. Is thought to
CC act as a 'pioneer' factor opening the compacted chromatin for other
CC proteins through interactions with nucleosomal core histones and
CC thereby replacing linker histones at target enhancer and/or promoter
CC sites. Binds DNA with the consensus sequence 5'-
CC [AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic
CC development is required for notochord formation. Involved in the
CC development of multiple endoderm-derived organ systems such as the
CC liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in
CC part redundant roles. Originally described as a transcription activator
CC for a number of liver genes such as AFP, albumin, tyrosine
CC aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory
CC regions of these genes. Involved in glucose homeostasis; regulates the
CC expression of genes important for glucose sensing in pancreatic beta-
CC cells and glucose homeostasis. Involved in regulation of fat
CC metabolism. Binds to fibrinogen beta promoter and is involved in IL6-
CC induced fibrinogen beta transcriptional activation. {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a monomer. Binds TLE1 (By similarity). Interacts
CC with FOXA1 and FOXA3. Interacts with PRKDC. {ECO:0000250,
CC ECO:0000269|PubMed:19478084, ECO:0000269|PubMed:19919681}.
CC -!- INTERACTION:
CC Q9Y261-2; P01023: A2M; NbExp=3; IntAct=EBI-25830360, EBI-640741;
CC Q9Y261-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-25830360, EBI-10968534;
CC Q9Y261-2; P14136: GFAP; NbExp=3; IntAct=EBI-25830360, EBI-744302;
CC Q9Y261-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-25830360, EBI-713665;
CC Q9Y261-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25830360, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:14500912}. Cytoplasm {ECO:0000269|PubMed:14500912}.
CC Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent
CC manner; in response to insulin signaling via AKT1 is exported from the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y261-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y261-2; Sequence=VSP_041212;
CC -!- PTM: Phosphorylation on Thr-156 abolishes binding to target promoters
CC and subsequent transcription activation upon insulin stimulation.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hepatocyte nuclear factors entry;
CC URL="https://en.wikipedia.org/wiki/Hepatocyte_nuclear_factors";
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DR EMBL; AB028021; BAA78106.1; -; mRNA.
DR EMBL; AF147787; AAD41081.1; -; Genomic_DNA.
DR EMBL; AF176110; AAD51978.1; -; Genomic_DNA.
DR EMBL; AL121722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006545; AAH06545.2; -; mRNA.
DR EMBL; BC011780; AAH11780.1; ALT_INIT; mRNA.
DR EMBL; BC019288; AAH19288.1; -; mRNA.
DR CCDS; CCDS13147.1; -. [Q9Y261-1]
DR CCDS; CCDS46585.1; -. [Q9Y261-2]
DR RefSeq; NP_068556.2; NM_021784.4. [Q9Y261-2]
DR RefSeq; NP_710141.1; NM_153675.2. [Q9Y261-1]
DR PDB; 5X07; X-ray; 2.80 A; C/F/I/L=157-258.
DR PDBsum; 5X07; -.
DR AlphaFoldDB; Q9Y261; -.
DR SMR; Q9Y261; -.
DR BioGRID; 109412; 22.
DR IntAct; Q9Y261; 16.
DR MINT; Q9Y261; -.
DR STRING; 9606.ENSP00000400341; -.
DR iPTMnet; Q9Y261; -.
DR PhosphoSitePlus; Q9Y261; -.
DR BioMuta; FOXA2; -.
DR DMDM; 8134491; -.
DR jPOST; Q9Y261; -.
DR MassIVE; Q9Y261; -.
DR MaxQB; Q9Y261; -.
DR PaxDb; Q9Y261; -.
DR PeptideAtlas; Q9Y261; -.
DR PRIDE; Q9Y261; -.
DR ProteomicsDB; 85664; -. [Q9Y261-1]
DR ProteomicsDB; 85665; -. [Q9Y261-2]
DR Antibodypedia; 3772; 871 antibodies from 47 providers.
DR DNASU; 3170; -.
DR Ensembl; ENST00000377115.4; ENSP00000366319.4; ENSG00000125798.15. [Q9Y261-1]
DR Ensembl; ENST00000419308.7; ENSP00000400341.3; ENSG00000125798.15. [Q9Y261-2]
DR GeneID; 3170; -.
DR KEGG; hsa:3170; -.
DR MANE-Select; ENST00000419308.7; ENSP00000400341.3; NM_021784.5; NP_068556.2. [Q9Y261-2]
DR UCSC; uc002wsm.4; human. [Q9Y261-1]
DR CTD; 3170; -.
DR DisGeNET; 3170; -.
DR GeneCards; FOXA2; -.
DR HGNC; HGNC:5022; FOXA2.
DR HPA; ENSG00000125798; Tissue enhanced (liver, pancreas, stomach).
DR MalaCards; FOXA2; -.
DR MIM; 600288; gene.
DR neXtProt; NX_Q9Y261; -.
DR OpenTargets; ENSG00000125798; -.
DR Orphanet; 95494; Combined pituitary hormone deficiencies, genetic forms.
DR PharmGKB; PA201091; -.
DR VEuPathDB; HostDB:ENSG00000125798; -.
DR eggNOG; KOG3563; Eukaryota.
DR GeneTree; ENSGT00940000155999; -.
DR HOGENOM; CLU_027910_4_1_1; -.
DR InParanoid; Q9Y261; -.
DR OMA; GMGASMT; -.
DR PhylomeDB; Q9Y261; -.
DR TreeFam; TF316127; -.
DR PathwayCommons; Q9Y261; -.
DR Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
DR SignaLink; Q9Y261; -.
DR SIGNOR; Q9Y261; -.
DR BioGRID-ORCS; 3170; 36 hits in 1090 CRISPR screens.
DR ChiTaRS; FOXA2; human.
DR GeneWiki; FOXA2; -.
DR GenomeRNAi; 3170; -.
DR Pharos; Q9Y261; Tbio.
DR PRO; PR:Q9Y261; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y261; protein.
DR Bgee; ENSG00000125798; Expressed in pancreatic ductal cell and 85 other tissues.
DR ExpressionAtlas; Q9Y261; baseline and differential.
DR Genevisible; Q9Y261; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; ISS:ParkinsonsUK-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0031018; P:endocrine pancreas development; IDA:BHF-UCL.
DR GO; GO:2000971; P:negative regulation of detection of glucose; ISS:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; ISS:BHF-UCL.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; ISS:BHF-UCL.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IC:BHF-UCL.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0090009; P:primitive streak formation; ISS:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; IDA:UniProtKB.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0070741; P:response to interleukin-6; TAS:UniProtKB.
DR CDD; cd00059; FH; 1.
DR DisProt; DP01124; -.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013638; Fork-head_N.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR018533; Forkhead_box_C.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF08430; Forkhead_N; 1.
DR Pfam; PF09354; HNF_C; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..457
FT /note="Hepatocyte nuclear factor 3-beta"
FT /id="PRO_0000091795"
FT DNA_BIND 159..252
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 14..93
FT /note="Transactivation domain 1"
FT /evidence="ECO:0000250"
FT REGION 280..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..457
FT /note="Transactivation domain 2"
FT /evidence="ECO:0000250"
FT MOTIF 106..113
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35583"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT VAR_SEQ 1
FT /note="M -> MHSASSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041212"
FT VARIANT 328
FT /note="A -> V (in Japanese subjects with maturity-onset
FT diabetes of the young; unknown pathological significance;
FT dbSNP:rs199796119)"
FT /evidence="ECO:0000269|PubMed:10672453"
FT /id="VAR_008858"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:5X07"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5X07"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:5X07"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5X07"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:5X07"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:5X07"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5X07"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5X07"
SQ SEQUENCE 457 AA; 48306 MW; 61DDE4C75C70680A CRC64;
MLGAVKMEGH EPSDWSSYYA EPEGYSSVSN MNAGLGMNGM NTYMSMSAAA MGSGSGNMSA
GSMNMSSYVG AGMSPSLAGM SPGAGAMAGM GGSAGAAGVA GMGPHLSPSL SPLGGQAAGA
MGGLAPYANM NSMSPMYGQA GLSRARDPKT YRRSYTHAKP PYSYISLITM AIQQSPNKML
TLSEIYQWIM DLFPFYRQNQ QRWQNSIRHS LSFNDCFLKV PRSPDKPGKG SFWTLHPDSG
NMFENGCYLR RQKRFKCEKQ LALKEAAGAA GSGKKAAAGA QASQAQLGEA AGPASETPAG
TESPHSSASP CQEHKRGGLG ELKGTPAAAL SPPEPAPSPG QQQQAAAHLL GPPHHPGLPP
EAHLKPEHHY AFNHPFSINN LMSSEQQHHH SHHHHQPHKM DLKAYEQVMH YPGYGSPMPG
SLAMGPVTNK TGLDASPLAA DTSYYQGVYS RPIMNSS
