TFB1M_HUMAN
ID TFB1M_HUMAN Reviewed; 346 AA.
AC Q8WVM0; Q05DR0; Q9Y384;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dimethyladenosine transferase 1, mitochondrial;
DE EC=2.1.1.-;
DE AltName: Full=Mitochondrial 12S rRNA dimethylase 1;
DE AltName: Full=Mitochondrial transcription factor B1;
DE Short=h-mtTFB;
DE Short=h-mtTFB1;
DE Short=hTFB1M;
DE Short=mtTFB1;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
DE Flags: Precursor;
GN Name=TFB1M; ORFNames=CGI-75;
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 [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND SAM-BINDING.
RX PubMed=11809803; DOI=10.1128/mcb.22.4.1116-1125.2002;
RA McCulloch V., Seidel-Rogol B.L., Shadel G.S.;
RT "A human mitochondrial transcription factor is related to RNA adenine
RT methyltransferases and binds S-adenosylmethionine.";
RL Mol. Cell. Biol. 22:1116-1125(2002).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH POLRMT.
RX PubMed=12068295; DOI=10.1038/ng909;
RA Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA Gustafsson C.M.;
RT "Mitochondrial transcription factors B1 and B2 activate transcription of
RT human mtDNA.";
RL Nat. Genet. 31:289-294(2002).
RN [6]
RP FUNCTION, INTERACTION WITH TFAM, AND MUTAGENESIS OF GLY-65; ASN-141 AND
RP LYS-220.
RX PubMed=12897151; DOI=10.1128/mcb.23.16.5816-5824.2003;
RA McCulloch V., Shadel G.S.;
RT "Human mitochondrial transcription factor B1 interacts with the C-terminal
RT activation region of h-mtTFA and stimulates transcription independently of
RT its RNA methyltransferase activity.";
RL Mol. Cell. Biol. 23:5816-5824(2003).
RN [7]
RP ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-65 AND LYS-220.
RX PubMed=12496758; DOI=10.1038/ng1064;
RA Seidel-Rogol B.L., McCulloch V., Shadel G.S.;
RT "Human mitochondrial transcription factor B1 methylates ribosomal RNA at a
RT conserved stem-loop.";
RL Nat. Genet. 33:23-24(2003).
RN [8]
RP POSSIBLE INVOLVEMENT IN AMINOGLYCOSIDE-INDUCED DEAFNESS.
RX PubMed=15110318; DOI=10.1016/j.ymgme.2004.01.020;
RA Bykhovskaya Y., Mengesha E., Wang D., Yang H., Estivill X., Shohat M.,
RA Fischel-Ghodsian N.;
RT "Human mitochondrial transcription factor B1 as a modifier gene for hearing
RT loss associated with the mitochondrial A1555G mutation.";
RL Mol. Genet. Metab. 82:27-32(2004).
RN [9]
RP INDUCTION.
RX PubMed=15684387; DOI=10.1128/mcb.25.4.1354-1366.2005;
RA Gleyzer N., Vercauteren K., Scarpulla R.C.;
RT "Control of mitochondrial transcription specificity factors (TFB1M and
RT TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family
RT coactivators.";
RL Mol. Cell. Biol. 25:1354-1366(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP VARIANTS PRO-120; ALA-211 AND GLN-256.
RX PubMed=19096125; DOI=10.1155/2008/575323;
RA Alonso-Montes C., Castro M.G., Reguero J.R., Perrot A., Ozcelik C.,
RA Geier C., Posch M.G., Moris C., Alvarez V., Ruiz-Ortega M., Coto E.;
RT "Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for DNA
RT variants/haplotypes and the risk of cardiac hypertrophy.";
RL Dis. Markers 25:131-139(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which
CC specifically dimethylates mitochondrial 12S rRNA at the conserved stem
CC loop. Also required for basal transcription of mitochondrial DNA,
CC probably via its interaction with POLRMT and TFAM. Stimulates
CC transcription independently of the methyltransferase activity.
CC {ECO:0000269|PubMed:11809803, ECO:0000269|PubMed:12068295,
CC ECO:0000269|PubMed:12897151}.
CC -!- SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT. Interacts
CC with TFAM. {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151}.
CC -!- INTERACTION:
CC Q8WVM0; Q00059: TFAM; NbExp=2; IntAct=EBI-2615570, EBI-1049924;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11809803}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12068295}.
CC -!- INDUCTION: By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and
CC PGC-1 coactivators. {ECO:0000269|PubMed:15684387}.
CC -!- DISEASE: Note=Variations in TFB1M may influence the clinical expression
CC of aminoglycoside-induced deafness caused by the A1555G mutation in the
CC mitochondrial 12S rRNA.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05183.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF151833; AAD34070.1; -; mRNA.
DR EMBL; AL139101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005183; AAH05183.1; ALT_SEQ; mRNA.
DR EMBL; BC017788; AAH17788.1; -; mRNA.
DR CCDS; CCDS5248.1; -.
DR RefSeq; NP_057104.2; NM_016020.3.
DR PDB; 6AAX; X-ray; 2.99 A; A/C=28-346.
DR PDB; 6AJK; X-ray; 3.00 A; A=27-346.
DR PDBsum; 6AAX; -.
DR PDBsum; 6AJK; -.
DR AlphaFoldDB; Q8WVM0; -.
DR SMR; Q8WVM0; -.
DR BioGRID; 119295; 108.
DR IntAct; Q8WVM0; 22.
DR MINT; Q8WVM0; -.
DR STRING; 9606.ENSP00000356134; -.
DR GlyGen; Q8WVM0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WVM0; -.
DR PhosphoSitePlus; Q8WVM0; -.
DR BioMuta; TFB1M; -.
DR DMDM; 74751555; -.
DR EPD; Q8WVM0; -.
DR jPOST; Q8WVM0; -.
DR MassIVE; Q8WVM0; -.
DR MaxQB; Q8WVM0; -.
DR PaxDb; Q8WVM0; -.
DR PeptideAtlas; Q8WVM0; -.
DR PRIDE; Q8WVM0; -.
DR ProteomicsDB; 74803; -.
DR Antibodypedia; 33417; 209 antibodies from 28 providers.
DR DNASU; 51106; -.
DR Ensembl; ENST00000367166.5; ENSP00000356134.4; ENSG00000029639.11.
DR GeneID; 51106; -.
DR KEGG; hsa:51106; -.
DR MANE-Select; ENST00000367166.5; ENSP00000356134.4; NM_016020.4; NP_057104.2.
DR UCSC; uc003qqj.5; human.
DR CTD; 51106; -.
DR DisGeNET; 51106; -.
DR GeneCards; TFB1M; -.
DR HGNC; HGNC:17037; TFB1M.
DR HPA; ENSG00000029639; Low tissue specificity.
DR MalaCards; TFB1M; -.
DR MIM; 607033; gene.
DR neXtProt; NX_Q8WVM0; -.
DR OpenTargets; ENSG00000029639; -.
DR Orphanet; 90641; Mitochondrial non-syndromic sensorineural deafness.
DR PharmGKB; PA38198; -.
DR VEuPathDB; HostDB:ENSG00000029639; -.
DR eggNOG; KOG0821; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_041220_7_0_1; -.
DR InParanoid; Q8WVM0; -.
DR OMA; RIEQPFK; -.
DR PhylomeDB; Q8WVM0; -.
DR TreeFam; TF300798; -.
DR PathwayCommons; Q8WVM0; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
DR SignaLink; Q8WVM0; -.
DR BioGRID-ORCS; 51106; 157 hits in 1079 CRISPR screens.
DR ChiTaRS; TFB1M; human.
DR GeneWiki; TFB1M; -.
DR GenomeRNAi; 51106; -.
DR Pharos; Q8WVM0; Tbio.
DR PRO; PR:Q8WVM0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8WVM0; protein.
DR Bgee; ENSG00000029639; Expressed in right adrenal gland and 180 other tissues.
DR ExpressionAtlas; Q8WVM0; baseline and differential.
DR Genevisible; Q8WVM0; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; EXP:Reactome.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0000154; P:rRNA modification; TAS:Reactome.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IBA:GO_Central.
DR Gene3D; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00755; ksgA; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Methyltransferase; Mitochondrion;
KW Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..346
FT /note="Dimethyladenosine transferase 1, mitochondrial"
FT /id="PRO_0000273171"
FT BINDING 35..38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT VARIANT 120
FT /note="A -> P (in dbSNP:rs144355958)"
FT /evidence="ECO:0000269|PubMed:19096125"
FT /id="VAR_071246"
FT VARIANT 211
FT /note="T -> A (in dbSNP:rs769497533)"
FT /evidence="ECO:0000269|PubMed:19096125"
FT /id="VAR_071247"
FT VARIANT 256
FT /note="R -> Q (in dbSNP:rs73579353)"
FT /evidence="ECO:0000269|PubMed:19096125"
FT /id="VAR_071248"
FT MUTAGEN 65
FT /note="G->A: Abolishes methyltransferase activity, DNA-
FT binding and SAM-binding. Does not abolish transcription
FT activator function."
FT /evidence="ECO:0000269|PubMed:12496758,
FT ECO:0000269|PubMed:12897151"
FT MUTAGEN 141
FT /note="N->A: Does not affect SAM-binding, DNA-binding nor
FT transcription activator function."
FT /evidence="ECO:0000269|PubMed:12897151"
FT MUTAGEN 220
FT /note="K->A: Abolishes methyltransferase activity. Does not
FT affect SAM-binding, DNA-binding nor transcription activator
FT function."
FT /evidence="ECO:0000269|PubMed:12496758,
FT ECO:0000269|PubMed:12897151"
FT CONFLICT 31..32
FT /note="KQ -> NE (in Ref. 1; AAD34070)"
FT /evidence="ECO:0000305"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6AAX"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6AJK"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:6AAX"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6AAX"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6AJK"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6AAX"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 297..312
FT /evidence="ECO:0007829|PDB:6AAX"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6AAX"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:6AJK"
SQ SEQUENCE 346 AA; 39543 MW; 4C34F4FD72B01286 CRC64;
MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK AGNLTNAYVY
EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTFKVEKA
FSESLKRPWE DDPPNVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV
AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ
PFKLVEKVVQ NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF
KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL
