MLX_HUMAN
ID MLX_HUMAN Reviewed; 298 AA.
AC Q9UH92; A8K2J3; B2RAV8; B2RD73; Q53XM6; Q96FL2; Q9H2V0; Q9H2V1; Q9H2V2;
AC Q9NXN3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Max-like protein X;
DE AltName: Full=Class D basic helix-loop-helix protein 13;
DE Short=bHLHd13;
DE AltName: Full=Max-like bHLHZip protein;
DE AltName: Full=Protein BigMax;
DE AltName: Full=Transcription factor-like protein 4;
GN Name=MLX; Synonyms=BHLHD13, TCFL4;
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 [MRNA] (ISOFORM BETA), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Promyelocyte;
RX PubMed=10593926; DOI=10.1074/jbc.274.51.36344;
RA Billin A.N., Eilers A.L., Queva C., Ayer D.E.;
RT "Mlx, a novel Max-like bHLHZip protein that interacts with the Max network
RT of transcription factors.";
RL J. Biol. Chem. 274:36344-36350(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), AND
RP SUBCELLULAR LOCATION.
RX PubMed=10918583; DOI=10.1038/sj.onc.1203634;
RA Meroni G., Cairo S., Merla G., Messali S., Brent R., Ballabio A.,
RA Reymond A.;
RT "Mlx, a new Max-like bHLHZip family member: the center stage of a novel
RT transcription factors regulatory pathway?";
RL Oncogene 19:3266-3277(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RC TISSUE=Brain, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC 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 [6]
RP FUNCTION, AND INTERACTION WITH MLXIP.
RX PubMed=12446771; DOI=10.1128/mcb.22.24.8514-8526.2002;
RA Eilers A.L., Sundwall E., Lin M., Sullivan A.A., Ayer D.E.;
RT "A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular
RT localization of the MondoA-Mlx heterocomplex.";
RL Mol. Cell. Biol. 22:8514-8526(2002).
RN [7]
RP FUNCTION.
RX PubMed=16782875; DOI=10.1128/mcb.00657-05;
RA Sans C.L., Satterwhite D.J., Stoltzman C.A., Breen K.T., Ayer D.E.;
RT "MondoA-Mlx heterodimers are candidate sensors of cellular energy status:
RT mitochondrial localization and direct regulation of glycolysis.";
RL Mol. Cell. Biol. 26:4863-4871(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-77 AND SER-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP 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 regulator. Forms a sequence-specific DNA-
CC binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which
CC recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4,
CC TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in
CC transcriptional activation of glycolytic target genes. Involved in
CC glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926,
CC ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAD1, MAD4, MNT, WBSCR14 and
CC MLXIP. Can also bind DNA as a homodimer. {ECO:0000269|PubMed:10593926}.
CC -!- INTERACTION:
CC Q9UH92; P60520: GABARAPL2; NbExp=5; IntAct=EBI-741109, EBI-720116;
CC Q9UH92; Q14498-3: RBM39; NbExp=3; IntAct=EBI-741109, EBI-6654703;
CC Q9UH92; Q08117: TLE5; NbExp=4; IntAct=EBI-741109, EBI-717810;
CC Q9UH92; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-741109, EBI-10188476;
CC Q9UH92; Q2Q067: HBZ; Xeno; NbExp=3; IntAct=EBI-741109, EBI-9675545;
CC Q9UH92-3; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-8852072, EBI-1642333;
CC Q9UH92-3; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-8852072, EBI-10181188;
CC Q9UH92-3; O14936-4: CASK; NbExp=3; IntAct=EBI-8852072, EBI-12007726;
CC Q9UH92-3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-8852072, EBI-742054;
CC Q9UH92-3; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-8852072, EBI-746969;
CC Q9UH92-3; P60520: GABARAPL2; NbExp=3; IntAct=EBI-8852072, EBI-720116;
CC Q9UH92-3; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-8852072, EBI-10241252;
CC Q9UH92-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-8852072, EBI-739832;
CC Q9UH92-3; A8MW99: MEI4; NbExp=3; IntAct=EBI-8852072, EBI-19944212;
CC Q9UH92-3; P50221: MEOX1; NbExp=3; IntAct=EBI-8852072, EBI-2864512;
CC Q9UH92-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8852072, EBI-16439278;
CC Q9UH92-3; O75928-2: PIAS2; NbExp=3; IntAct=EBI-8852072, EBI-348567;
CC Q9UH92-3; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-8852072, EBI-17589229;
CC Q9UH92-3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-8852072, EBI-11139477;
CC Q9UH92-3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-8852072, EBI-11741437;
CC Q9UH92-3; P45379-11: TNNT2; NbExp=3; IntAct=EBI-8852072, EBI-17559309;
CC Q9UH92-3; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-8852072, EBI-10180829;
CC Q9UH92-3; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-8852072, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm
CC {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the
CC cytoplasm (PubMed:10918583). {ECO:0000269|PubMed:10918583}.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm
CC {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the
CC cytoplasm (PubMed:10918583). {ECO:0000269|PubMed:10918583}.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus
CC {ECO:0000269|PubMed:10918583}. Note=Found predominantly in the nucleus
CC (PubMed:10918583). {ECO:0000269|PubMed:10918583}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Gamma;
CC IsoId=Q9UH92-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q9UH92-2; Sequence=VSP_002137, VSP_002138;
CC Name=Beta;
CC IsoId=Q9UH92-3; Sequence=VSP_002137;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including spleen,
CC thymus, prostate, ovary, intestine, colon, peripheral blood leukocyte,
CC heart, liver, skeletal muscle and kidney. Lower levels of expression in
CC testis, brain, placenta and lung. {ECO:0000269|PubMed:10593926}.
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DR EMBL; AF203978; AAF14638.1; -; mRNA.
DR EMBL; AF213666; AAG40145.1; -; mRNA.
DR EMBL; AF213667; AAG40146.1; -; mRNA.
DR EMBL; AF213668; AAG40147.1; -; mRNA.
DR EMBL; AK000150; BAA90977.1; -; mRNA.
DR EMBL; AK290258; BAF82947.1; -; mRNA.
DR EMBL; AK314378; BAG37005.1; -; mRNA.
DR EMBL; AK315432; BAG37820.1; -; mRNA.
DR EMBL; BT009812; AAP88814.1; -; mRNA.
DR EMBL; BC010689; AAH10689.1; -; mRNA.
DR CCDS; CCDS11430.1; -. [Q9UH92-1]
DR CCDS; CCDS42341.1; -. [Q9UH92-2]
DR CCDS; CCDS45687.1; -. [Q9UH92-3]
DR PIR; JC5333; JC5333.
DR RefSeq; NP_733752.1; NM_170607.2. [Q9UH92-1]
DR RefSeq; NP_937847.1; NM_198204.1. [Q9UH92-3]
DR RefSeq; NP_937848.1; NM_198205.1. [Q9UH92-2]
DR AlphaFoldDB; Q9UH92; -.
DR BioGRID; 112805; 60.
DR IntAct; Q9UH92; 39.
DR MINT; Q9UH92; -.
DR STRING; 9606.ENSP00000246912; -.
DR BindingDB; Q9UH92; -.
DR ChEMBL; CHEMBL2062357; -.
DR iPTMnet; Q9UH92; -.
DR PhosphoSitePlus; Q9UH92; -.
DR BioMuta; MLX; -.
DR DMDM; 20138856; -.
DR EPD; Q9UH92; -.
DR jPOST; Q9UH92; -.
DR MassIVE; Q9UH92; -.
DR MaxQB; Q9UH92; -.
DR PaxDb; Q9UH92; -.
DR PeptideAtlas; Q9UH92; -.
DR PRIDE; Q9UH92; -.
DR ProteomicsDB; 84286; -. [Q9UH92-1]
DR ProteomicsDB; 84287; -. [Q9UH92-2]
DR ProteomicsDB; 84288; -. [Q9UH92-3]
DR Antibodypedia; 29285; 360 antibodies from 37 providers.
DR DNASU; 6945; -.
DR Ensembl; ENST00000246912.8; ENSP00000246912.3; ENSG00000108788.12. [Q9UH92-1]
DR Ensembl; ENST00000346833.8; ENSP00000320913.3; ENSG00000108788.12. [Q9UH92-2]
DR Ensembl; ENST00000435881.7; ENSP00000416627.1; ENSG00000108788.12. [Q9UH92-3]
DR GeneID; 6945; -.
DR KEGG; hsa:6945; -.
DR MANE-Select; ENST00000435881.7; ENSP00000416627.1; NM_198204.2; NP_937847.1. [Q9UH92-3]
DR UCSC; uc002iaf.4; human. [Q9UH92-1]
DR CTD; 6945; -.
DR DisGeNET; 6945; -.
DR GeneCards; MLX; -.
DR HGNC; HGNC:11645; MLX.
DR HPA; ENSG00000108788; Low tissue specificity.
DR MalaCards; MLX; -.
DR MIM; 602976; gene.
DR neXtProt; NX_Q9UH92; -.
DR OpenTargets; ENSG00000108788; -.
DR Orphanet; 3287; Takayasu arteritis.
DR PharmGKB; PA36397; -.
DR VEuPathDB; HostDB:ENSG00000108788; -.
DR eggNOG; KOG1319; Eukaryota.
DR GeneTree; ENSGT00940000157377; -.
DR HOGENOM; CLU_083204_0_0_1; -.
DR InParanoid; Q9UH92; -.
DR OMA; AHNTEDE; -.
DR OrthoDB; 1234389at2759; -.
DR PhylomeDB; Q9UH92; -.
DR TreeFam; TF318841; -.
DR PathwayCommons; Q9UH92; -.
DR Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR SignaLink; Q9UH92; -.
DR BioGRID-ORCS; 6945; 94 hits in 1108 CRISPR screens.
DR ChiTaRS; MLX; human.
DR GeneWiki; MLX_(gene); -.
DR GenomeRNAi; 6945; -.
DR Pharos; Q9UH92; Tchem.
DR PRO; PR:Q9UH92; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UH92; protein.
DR Bgee; ENSG00000108788; Expressed in oocyte and 208 other tissues.
DR ExpressionAtlas; Q9UH92; baseline and differential.
DR Genevisible; Q9UH92; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR032647; Mlx.
DR PANTHER; PTHR15741:SF25; PTHR15741:SF25; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..298
FT /note="Max-like protein X"
FT /id="PRO_0000127279"
FT DOMAIN 129..187
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..160
FT /note="Leucine-zipper"
FT COMPBIAS 91..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08609"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08609"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 15..68
FT /note="Missing (in isoform Alpha and isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10593926,
FT ECO:0000303|PubMed:10918583, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_002137"
FT VAR_SEQ 81..110
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:10918583,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_002138"
FT VARIANT 223
FT /note="Q -> R (in dbSNP:rs665268)"
FT /id="VAR_049547"
FT CONFLICT 247
FT /note="D -> V (in Ref. 1; AAF14638)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="Y -> C (in Ref. 3; BAA90977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33300 MW; D1981730051473C5 CRC64;
MTEPGASPED PWVKASPVGA HAGEGRAGRA RARRGAGRRG ASLLSPKSPT LSVPRGCRED
SSHPACAKVE YAYSDNSLDP GLFVESTRKG SVVSRANSIG STSASSVPNT DDEDSDYHQE
AYKESYKDRR RRAHTQAEQK RRDAIKRGYD DLQTIVPTCQ QQDFSIGSQK LSKAIVLQKT
IDYIQFLHKE KKKQEEEVST LRKDVTALKI MKVNYEQIVK AHQDNPHEGE DQVSDQVKFN
VFQGIMDSLF QSFNASISVA SFQELSACVF SWIEEHCKPQ TLREIVIGVL HQLKNQLY
