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 27-MAR-2024, entry version 198. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9UH92; -. DR BioGRID; 112805; 62. DR ComplexPortal; CPX-2519; MXD1-MLX transcriptional repressor complex. DR ComplexPortal; CPX-2520; MXD4-MLX transcriptional repressor complex. DR ComplexPortal; CPX-2521; MNT-MLX transcriptional repressor complex. DR ComplexPortal; CPX-2525; MLXIP-MLX transcription factor complex. DR ComplexPortal; CPX-2530; MLXIPL-MLX transcription factor complex. DR IntAct; Q9UH92; 38. 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; 9606-ENSP00000246912; -. DR PeptideAtlas; Q9UH92; -. DR ProteomicsDB; 84286; -. [Q9UH92-1] DR ProteomicsDB; 84287; -. [Q9UH92-2] DR ProteomicsDB; 84288; -. [Q9UH92-3] DR Pumba; Q9UH92; -. DR Antibodypedia; 29285; 389 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 AGR; HGNC:11645; -. 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; GYETMLQ; -. DR OrthoDB; 2901982at2759; -. 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; 95 hits in 1186 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 210 other cell types or tissues. DR ExpressionAtlas; Q9UH92; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd19687; bHLHzip_Mlx; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR PANTHER; PTHR15741; BASIC HELIX-LOOP-HELIX ZIP TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR15741:SF25; MAX-LIKE PROTEIN X; 1. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR PROSITE; PS50888; BHLH; 1. DR Genevisible; Q9UH92; HS. 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 //