QCR7_HUMAN
ID QCR7_HUMAN Reviewed; 111 AA.
AC P14927; E5RJU0; Q6FGD1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Cytochrome b-c1 complex subunit 7;
DE AltName: Full=Complex III subunit 7;
DE AltName: Full=Complex III subunit VII;
DE AltName: Full=QP-C;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN Name=UQCRB; Synonyms=UQBP;
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 1).
RC TISSUE=Fibroblast;
RX PubMed=3056408; DOI=10.1016/s0006-291x(88)80941-0;
RA Suzuki H., Yoshitaka H., Toda H., Nishikimi M., Ozawa T.;
RT "Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-
RT binding protein of complex III.";
RL Biochem. Biophys. Res. Commun. 156:987-994(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=2543413; DOI=10.1016/0006-291x(89)91607-0;
RA Suzuki H., Hosokawa Y., Toda H., Nishikimi M., Ozawa T.;
RT "Isolation of a single nuclear gene encoding human ubiquinone-binding
RT protein in complex III of mitochondrial respiratory chain.";
RL Biochem. Biophys. Res. Commun. 161:371-378(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Urinary bladder;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=2159470; DOI=10.1016/s0021-9258(19)39051-9;
RA Suzuki H., Hosokawa Y., Toda H., Nishikimi M., Ozawa T.;
RT "Common protein-binding sites in the 5'-flanking regions of human genes for
RT cytochrome c1 and ubiquinone-binding protein.";
RL J. Biol. Chem. 265:8159-8163(1990).
RN [8]
RP INVOLVEMENT IN MC3DN3.
RX PubMed=12709789; DOI=10.1007/s00439-003-0946-0;
RA Haut S., Brivet M., Touati G., Rustin P., Lebon S., Garcia-Cazorla A.,
RA Saudubray J.-M., Boutron A., Legrand A., Slama A.;
RT "A deletion in the human QP-C gene causes a complex III deficiency
RT resulting in hypoglycaemia and lactic acidosis.";
RL Hum. Genet. 113:118-122(2003).
RN [9]
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 [10]
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).
RN [11]
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 [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 6-111.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. {ECO:0000250|UniProtKB:P00128}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:28844695). {ECO:0000250|UniProtKB:P00129,
CC ECO:0000269|PubMed:28844695}.
CC -!- INTERACTION:
CC P14927; Q15027: ACAP1; NbExp=3; IntAct=EBI-743128, EBI-751746;
CC P14927; Q96QU6: ACCS; NbExp=3; IntAct=EBI-743128, EBI-743387;
CC P14927; Q14457: BECN1; NbExp=3; IntAct=EBI-743128, EBI-949378;
CC P14927; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-743128, EBI-21529239;
CC P14927; P06241-3: FYN; NbExp=3; IntAct=EBI-743128, EBI-10691738;
CC P14927; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-743128, EBI-2857315;
CC P14927; P84074: HPCA; NbExp=3; IntAct=EBI-743128, EBI-12197079;
CC P14927; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-743128, EBI-712105;
CC P14927; A1A512: KIAA0355; NbExp=3; IntAct=EBI-743128, EBI-25844799;
CC P14927; Q15012: LAPTM4A; NbExp=3; IntAct=EBI-743128, EBI-723416;
CC P14927; Q92615: LARP4B; NbExp=3; IntAct=EBI-743128, EBI-1052558;
CC P14927; P43358: MAGEA4; NbExp=5; IntAct=EBI-743128, EBI-743122;
CC P14927; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-743128, EBI-10194128;
CC P14927; O15481: MAGEB4; NbExp=3; IntAct=EBI-743128, EBI-751857;
CC P14927; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-743128, EBI-17438286;
CC P14927; Q19AV6: ZSWIM7; NbExp=3; IntAct=EBI-743128, EBI-5281647;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00128}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00128}; Matrix side
CC {ECO:0000250|UniProtKB:P00128}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P14927-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14927-2; Sequence=VSP_045601;
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear 3 (MC3DN3)
CC [MIM:615158]: A disorder of the mitochondrial respiratory chain
CC resulting in a highly variable phenotype depending on which tissues are
CC affected. Clinical features include mitochondrial encephalopathy,
CC psychomotor retardation, ataxia, severe failure to thrive, liver
CC dysfunction, renal tubulopathy, muscle weakness and exercise
CC intolerance. {ECO:0000269|PubMed:12709789}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the ubiquinone-binding protein
CC (QP-C). {ECO:0000305}.
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DR EMBL; X13585; CAA31926.1; -; mRNA.
DR EMBL; M22348; AAA60238.1; -; mRNA.
DR EMBL; CR542176; CAG46973.1; -; mRNA.
DR EMBL; CR542196; CAG46993.1; -; mRNA.
DR EMBL; M26730; AAA60235.1; -; Genomic_DNA.
DR EMBL; M35761; AAA60235.1; JOINED; Genomic_DNA.
DR EMBL; M26706; AAA60235.1; JOINED; Genomic_DNA.
DR EMBL; M26707; AAA60235.1; JOINED; Genomic_DNA.
DR EMBL; M26700; AAA60236.1; -; mRNA.
DR EMBL; M26701; AAA60237.1; -; Genomic_DNA.
DR EMBL; AP003465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91749.1; -; Genomic_DNA.
DR EMBL; BC005230; AAH05230.1; -; mRNA.
DR EMBL; BU535281; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M37387; AAA60361.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS59107.1; -. [P14927-2]
DR CCDS; CCDS6269.1; -. [P14927-1]
DR PIR; A32450; A32450.
DR RefSeq; NP_001186904.1; NM_001199975.2.
DR RefSeq; NP_001241681.1; NM_001254752.1. [P14927-2]
DR RefSeq; NP_006285.1; NM_006294.4. [P14927-1]
DR PDB; 5XTE; EM; 3.40 A; F/S=6-111.
DR PDB; 5XTH; EM; 3.90 A; AF/AS=6-111.
DR PDB; 5XTI; EM; 17.40 A; AF/AS=6-111.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P14927; -.
DR SMR; P14927; -.
DR BioGRID; 113227; 125.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P14927; 49.
DR MINT; P14927; -.
DR STRING; 9606.ENSP00000430494; -.
DR BindingDB; P14927; -.
DR ChEMBL; CHEMBL1671612; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR CarbonylDB; P14927; -.
DR GlyGen; P14927; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P14927; -.
DR PhosphoSitePlus; P14927; -.
DR SwissPalm; P14927; -.
DR BioMuta; UQCRB; -.
DR DMDM; 136717; -.
DR UCD-2DPAGE; P14927; -.
DR EPD; P14927; -.
DR jPOST; P14927; -.
DR MassIVE; P14927; -.
DR MaxQB; P14927; -.
DR PaxDb; P14927; -.
DR PeptideAtlas; P14927; -.
DR PRIDE; P14927; -.
DR ProteomicsDB; 16706; -.
DR ProteomicsDB; 53099; -. [P14927-1]
DR TopDownProteomics; P14927-1; -. [P14927-1]
DR Antibodypedia; 42750; 172 antibodies from 27 providers.
DR DNASU; 7381; -.
DR Ensembl; ENST00000287022.10; ENSP00000287022.5; ENSG00000156467.10. [P14927-1]
DR Ensembl; ENST00000518406.5; ENSP00000430494.1; ENSG00000156467.10. [P14927-2]
DR GeneID; 7381; -.
DR KEGG; hsa:7381; -.
DR MANE-Select; ENST00000287022.10; ENSP00000287022.5; NM_006294.5; NP_006285.1.
DR UCSC; uc003yhq.5; human. [P14927-1]
DR CTD; 7381; -.
DR DisGeNET; 7381; -.
DR GeneCards; UQCRB; -.
DR HGNC; HGNC:12582; UQCRB.
DR HPA; ENSG00000156467; Tissue enhanced (skeletal).
DR MalaCards; UQCRB; -.
DR MIM; 191330; gene.
DR MIM; 615158; phenotype.
DR neXtProt; NX_P14927; -.
DR OpenTargets; ENSG00000156467; -.
DR Orphanet; 1460; Isolated complex III deficiency.
DR PharmGKB; PA37213; -.
DR VEuPathDB; HostDB:ENSG00000156467; -.
DR eggNOG; KOG3440; Eukaryota.
DR GeneTree; ENSGT00390000012916; -.
DR HOGENOM; CLU_115154_2_0_1; -.
DR InParanoid; P14927; -.
DR OMA; APYIMKR; -.
DR OrthoDB; 1298800at2759; -.
DR PhylomeDB; P14927; -.
DR TreeFam; TF105035; -.
DR BioCyc; MetaCyc:HS08128-MON; -.
DR BRENDA; 7.1.1.8; 2681.
DR PathwayCommons; P14927; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P14927; -.
DR SIGNOR; P14927; -.
DR BioGRID-ORCS; 7381; 295 hits in 1054 CRISPR screens.
DR ChiTaRS; UQCRB; human.
DR GeneWiki; UQCRB; -.
DR GenomeRNAi; 7381; -.
DR Pharos; P14927; Tbio.
DR PRO; PR:P14927; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P14927; protein.
DR Bgee; ENSG00000156467; Expressed in heart right ventricle and 213 other tissues.
DR ExpressionAtlas; P14927; baseline and differential.
DR Genevisible; P14927; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005746; C:mitochondrial respirasome; TAS:ProtInc.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal.
DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR Gene3D; 1.10.1090.10; -; 1.
DR InterPro; IPR003197; QCR7.
DR InterPro; IPR036544; QCR7_sf.
DR PANTHER; PTHR12022; PTHR12022; 1.
DR Pfam; PF02271; UCR_14kD; 1.
DR PIRSF; PIRSF000022; Bc1_14K; 1.
DR SUPFAM; SSF81524; SSF81524; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00129"
FT CHAIN 2..111
FT /note="Cytochrome b-c1 complex subunit 7"
FT /id="PRO_0000193524"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00129"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 12
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT VAR_SEQ 87..111
FT /note="ENFYLEPYLKEVIRERKEREEWAKK -> VFAVPALHSASYLDEKISPLSVP
FT PDPKKSFCEANSHPLNCIETRQRKISTLNRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045601"
FT VARIANT 30
FT /note="L -> P (in dbSNP:rs35895613)"
FT /id="VAR_052443"
FT CONFLICT 6
FT /note="A -> G (in Ref. 2; AAA60236)"
FT /evidence="ECO:0000305"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 53..72
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 111 AA; 13530 MW; E61629D06DFA55B7 CRC64;
MAGKQAVSAS GKWLDGIRKW YYNAAGFNKL GLMRDDTIYE DEDVKEAIRR LPENLYNDRM
FRIKRALDLN LKHQILPKEQ WTKYEEENFY LEPYLKEVIR ERKEREEWAK K
