ID   EIF1_HUMAN              Reviewed;         113 AA.
AC   P41567; Q9UNQ9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 201.
DE   RecName: Full=Eukaryotic translation initiation factor 1 {ECO:0000303|PubMed:9732867};
DE            Short=eIF1 {ECO:0000303|PubMed:9732867};
DE   AltName: Full=A121;
DE   AltName: Full=Protein translation factor SUI1 homolog;
DE   AltName: Full=Sui1iso1;
GN   Name=EIF1; Synonyms=SUI1;
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].
RX   PubMed=7904817; DOI=10.1006/bbrc.1994.1040;
RA   Fields C.A., Adams M.D.;
RT   "Expressed sequence tags identify a human isolog of the suil translation
RT   initiation factor.";
RL   Biochem. Biophys. Res. Commun. 198:288-291(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Singh S.K., Murray S.F., Chin L.S.;
RT   "Okadaic acid-responsive genes in malignant glioma cells identified by mRNA
RT   differential display.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10347211; DOI=10.1074/jbc.274.23.16487;
RA   Sheikh M.S., Fernandez-Salas E., Yu M., Hussain A., Dinman J.D.,
RA   Peltz S.W., Huang Y., Fornace A.J. Jr.;
RT   "Cloning and characterization of a human genotoxic and endoplasmic
RT   reticulum stress-inducible cDNA that encodes translation initiation factor
RT   1 (eIF1(A121/SUI1)).";
RL   J. Biol. Chem. 274:16487-16493(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, 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   [5]
RP   FUNCTION.
RX   PubMed=9732867; DOI=10.1038/29703;
RA   Pestova T.V., Borukhov S.I., Hellen C.U.;
RT   "Eukaryotic ribosomes require initiation factors 1 and 1A to locate
RT   initiation codons.";
RL   Nature 394:854-859(1998).
RN   [6]
RP   INTERACTION WITH RENT2.
RX   PubMed=11073994; DOI=10.1128/mcb.20.23.8944-8957.2000;
RA   Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
RT   "Novel Upf2p orthologues suggest a functional link between translation
RT   initiation and nonsense surveillance complexes.";
RL   Mol. Cell. Biol. 20:8944-8957(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=12435632; DOI=10.1101/gad.1020902;
RA   Pestova T.V., Kolupaeva V.G.;
RT   "The roles of individual eukaryotic translation initiation factors in
RT   ribosomal scanning and initiation codon selection.";
RL   Genes Dev. 16:2906-2922(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=14600024; DOI=10.1101/gad.1141803;
RA   Lomakin I.B., Kolupaeva V.G., Marintchev A., Wagner G., Pestova T.V.;
RT   "Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit
RT   determined by directed hydroxyl radical probing.";
RL   Genes Dev. 17:2786-2797(2003).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH EIF5.
RX   PubMed=22813744; DOI=10.1016/j.celrep.2012.04.007;
RA   Luna R.E., Arthanari H., Hiraishi H., Nanda J., Martin-Marcos P.,
RA   Markus M.A., Akabayov B., Milbradt A.G., Luna L.E., Seo H.C., Hyberts S.G.,
RA   Fahmy A., Reibarkh M., Miles D., Hagner P.R., O'Day E.M., Yi T.,
RA   Marintchev A., Hinnebusch A.G., Lorsch J.R., Asano K., Wagner G.;
RT   "The C-terminal domain of eukaryotic initiation factor 5 promotes start
RT   codon recognition by its dynamic interplay with eIF1 and eIF2beta.";
RL   Cell Rep. 1:689-702(2012).
RN   [13]
RP   FUNCTION.
RX   PubMed=24319994; DOI=10.1021/bi4009775;
RA   Luna R.E., Arthanari H., Hiraishi H., Akabayov B., Tang L., Cox C.,
RA   Markus M.A., Luna L.E., Ikeda Y., Watanabe R., Bedoya E., Yu C.,
RA   Alikhan S., Wagner G., Asano K.;
RT   "The interaction between eukaryotic initiation factor 1A and eIF5 retains
RT   eIF1 within scanning preinitiation complexes.";
RL   Biochemistry 52:9510-9518(2013).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, 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   [15]
RP   FUNCTION, INTERACTION WITH EIF4G1, AND MUTAGENESIS OF 57-LYS-LYS-58 AND
RP   109-LYS--HIS-111.
RX   PubMed=29987188; DOI=10.1128/mcb.00139-18;
RA   Haimov O., Sehrawat U., Tamarkin-Ben Harush A., Bahat A., Uzonyi A.,
RA   Will A., Hiraishi H., Asano K., Dikstein R.;
RT   "Dynamic interaction of eukaryotic initiation factor 4G1 (eIF4G1) with
RT   eIF4E and eIF1 underlies scanning-dependent and -independent translation.";
RL   Mol. Cell. Biol. 38:0-0(2018).
RN   [16] {ECO:0000312|PDB:2IF1}
RP   STRUCTURE BY NMR.
RX   PubMed=10228174; DOI=10.1093/emboj/18.9.2631;
RA   Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G.;
RT   "Structure and interactions of the translation initiation factor eIF1.";
RL   EMBO J. 18:2631-2637(1999).
CC   -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which
CC       binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated
CC       region, and locates the initiation codon (PubMed:12435632,
CC       PubMed:14600024, PubMed:9732867). Together with eIF1A (EIF1AX), EIF1
CC       facilitates scanning and is essential for start codon recognition on
CC       the basis of AUG nucleotide context and location relative to the 5'-cap
CC       (PubMed:12435632, PubMed:14600024, PubMed:9732867). Participates to
CC       initiation codon selection by influencing the conformation of the 40S
CC       ribosomal subunit and the positions of bound mRNA and initiator tRNA;
CC       this is possible after its binding to the interface surface of the
CC       platform of the 40S ribosomal subunit close to the P-site
CC       (PubMed:14600024). Together with eIF1A (EIF1AX), also regulates the
CC       opening and closing of the mRNA binding channel, which ensures mRNA
CC       recruitment, scanning and the fidelity of initiation codon selection
CC       (PubMed:9732867). Continuously monitors and protects against premature
CC       and partial base-pairing of codons in the 5'-UTR with the anticodon of
CC       initiator tRNA (PubMed:12435632, PubMed:9732867). Together with eIF1A
CC       (EIF1AX), acts for ribosomal scanning, promotion of the assembly of 48S
CC       complex at the initiation codon (43S PIC becomes 48S PIC after the
CC       start codon is reached), and dissociation of aberrant complexes
CC       (PubMed:9732867). Interacts with EIF4G1, which in a mutual exclusive
CC       interaction associates either with EIF1 or with EIF4E on a common
CC       binding site (PubMed:29987188). EIF4G1-EIF1 complex promotes ribosome
CC       scanning (on both short and long 5'UTR), leaky scanning (on short
CC       5'UTR) which is the bypass of the initial start codon, and
CC       discrimination against cap-proximal AUG (PubMed:29987188). Is probably
CC       maintained within the 43S PIC in open conformation thanks to eIF1A-EIF5
CC       interaction (PubMed:24319994). Once the correct start codon is reached,
CC       EIF1 is physically excluded from the decoding site, shifting the PIC
CC       into the closed conformation and arresting it at the start codon
CC       (PubMed:22813744). {ECO:0000269|PubMed:12435632,
CC       ECO:0000269|PubMed:14600024, ECO:0000269|PubMed:22813744,
CC       ECO:0000269|PubMed:29987188, ECO:0000269|PubMed:9732867}.
CC   -!- SUBUNIT: Component of the 43S pre-initiation complex (43S PIC), which
CC       is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3
CC       complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary
CC       complex). Interacts with EIF4G1; in specific 5'-UTR length and AUG
CC       context (PubMed:29987188). Interacts with EIF5; which in a mutual
CC       exclusive interaction associates either with EIF1 or with EIF2S2 on a
CC       common binding site (PubMed:22813744). Interacts with RENT2
CC       (PubMed:11073994). {ECO:0000269|PubMed:11073994,
CC       ECO:0000269|PubMed:29987188}.
CC   -!- INTERACTION:
CC       P41567; Q14152: EIF3A; NbExp=2; IntAct=EBI-726200, EBI-366617;
CC       P41567; Q99613: EIF3C; NbExp=2; IntAct=EBI-726200, EBI-353741;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000305}.
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DR   EMBL; L26247; AAA60602.1; -; mRNA.
DR   EMBL; AF083441; AAD52028.1; -; mRNA.
DR   EMBL; AF100737; AAD19900.1; -; mRNA.
DR   EMBL; BC005118; AAH05118.1; -; mRNA.
DR   EMBL; BC008710; AAH08710.1; -; mRNA.
DR   CCDS; CCDS11403.1; -.
DR   PIR; JC2042; JC2042.
DR   RefSeq; NP_005792.1; NM_005801.4.
DR   PDB; 2IF1; NMR; -; A=1-113.
DR   PDB; 4KZX; X-ray; 7.81 A; l=1-113.
DR   PDB; 4KZY; X-ray; 7.01 A; l=1-113.
DR   PDB; 6YBW; EM; 3.10 A; p=1-113.
DR   PDB; 6ZMW; EM; 3.70 A; p=1-113.
DR   PDB; 6ZP4; EM; 2.90 A; Z=1-113.
DR   PDB; 6ZVJ; EM; 3.80 A; N=23-113.
DR   PDB; 7A09; EM; 3.50 A; Z=1-113.
DR   PDB; 7QP6; EM; 4.70 A; p=1-113.
DR   PDB; 8PJ1; EM; 3.40 A; p=1-113.
DR   PDB; 8PPK; EM; 2.98 A; p=1-113.
DR   PDB; 8PPL; EM; 2.65 A; Ip=1-113.
DR   PDB; 8XXN; EM; 3.60 A; C1=1-113.
DR   PDB; 9BLN; EM; 3.90 A; W=1-113.
DR   PDB; 9NPX; EM; 2.10 A; k=1-113.
DR   AlphaFoldDB; P41567; -.
DR   BMRB; P41567; -.
DR   EMDB; EMD-10775; -.
DR   EMDB; EMD-11302; -.
DR   EMDB; EMD-11335; -.
DR   EMDB; EMD-11458; -.
DR   EMDB; EMD-11602; -.
DR   EMDB; EMD-14113; -.
DR   EMDB; EMD-17696; -.
DR   EMDB; EMD-17804; -.
DR   EMDB; EMD-17805; -.
DR   EMDB; EMD-38754; -.
DR   EMDB; EMD-44671; -.
DR   EMDB; EMD-49635; -.
DR   EMDB; EMD-49637; -.
DR   SMR; P41567; -.
DR   BioGRID; 115504; 45.
DR   DIP; DIP-50783N; -.
DR   FunCoup; P41567; 1968.
DR   IntAct; P41567; 17.
DR   NDEx; IQUERY-CP-EIF1; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000419449; -.
DR   GlyCosmos; P41567; 1 site, 1 glycan.
DR   GlyGen; P41567; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P41567; -.
DR   PhosphoSitePlus; P41567; -.
DR   BioMuta; EIF1; -.
DR   jPOST; P41567; -.
DR   MassIVE; P41567; -.
DR   PaxDb; 9606-ENSP00000419449; -.
DR   PeptideAtlas; P41567; -.
DR   ProteomicsDB; 55464; -.
DR   Pumba; P41567; -.
DR   TopDownProteomics; P41567; -.
DR   Antibodypedia; 28894; 242 antibodies from 31 providers.
DR   DNASU; 10209; -.
DR   Ensembl; ENST00000469257.2; ENSP00000419449.1; ENSG00000173812.12.
DR   GeneID; 10209; -.
DR   KEGG; hsa:10209; -.
DR   MANE-Select; ENST00000469257.2; ENSP00000419449.1; NM_005801.4; NP_005792.1.
DR   AGR; HGNC:3249; -.
DR   ClinPGx; PA27683; -.
DR   CTD; 10209; -.
DR   DisGeNET; 10209; -.
DR   GeneCards; EIF1; -.
DR   HGNC; HGNC:3249; EIF1.
DR   HPA; ENSG00000173812; Low tissue specificity.
DR   MIM; 619901; gene.
DR   OpenTargets; ENSG00000173812; -.
DR   VEuPathDB; HostDB:ENSG00000173812; -.
DR   eggNOG; KOG1770; Eukaryota.
DR   GeneTree; ENSGT00390000015789; -.
DR   HOGENOM; CLU_082805_3_0_1; -.
DR   InParanoid; P41567; -.
DR   OMA; ACKMEFA; -.
DR   OrthoDB; 10248435at2759; -.
DR   PAN-GO; P41567; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P41567; -.
DR   PathwayCommons; P41567; -.
DR   SignaLink; P41567; -.
DR   SIGNOR; P41567; -.
DR   Agora; ENSG00000173812; -.
DR   BioGRID-ORCS; 10209; 723 hits in 1162 CRISPR screens.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; EIF1; human.
DR   EvolutionaryTrace; P41567; -.
DR   GeneWiki; EIF1; -.
DR   GenomeRNAi; 10209; -.
DR   Pharos; P41567; Tbio.
DR   PRO; PR:P41567; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P41567; protein.
DR   Bgee; ENSG00000173812; Expressed in sperm and 207 other cell types or tissues.
DR   ExpressionAtlas; P41567; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:UniProtKB.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:UniProtKB.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; IDA:CACAO.
DR   GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR   CDD; cd11566; eIF1_SUI1; 1.
DR   DisProt; DP00910; -.
DR   FunFam; 3.30.780.10:FF:000003; Eukaryotic translation initiation factor 1b; 1.
DR   Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR005874; SUI1_euk.
DR   NCBIfam; TIGR01160; SUI1_MOF2; 1.
DR   PANTHER; PTHR10388; EUKARYOTIC TRANSLATION INITIATION FACTOR SUI1; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   PIRSF; PIRSF004499; SUI1_euk; 1.
DR   SUPFAM; SSF55159; eIF1-like; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Proteomics identification; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   CHAIN           2..113
FT                   /note="Eukaryotic translation initiation factor 1"
FT                   /id="PRO_0000130554"
FT   SITE            41
FT                   /note="Binds 40S ribosomal subunit"
FT                   /evidence="ECO:0000305|PubMed:29987188"
FT   SITE            65
FT                   /note="Binds 40S ribosomal subunit"
FT                   /evidence="ECO:0000305|PubMed:29987188"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         59
FT                   /note="L -> P (in dbSNP:rs3390)"
FT                   /id="VAR_052505"
FT   VARIANT         90
FT                   /note="R -> G (in dbSNP:rs3387)"
FT                   /id="VAR_052506"
FT   MUTAGEN         57..58
FT                   /note="KK->AA: Decrease in interaction with EIF4G1."
FT                   /evidence="ECO:0000269|PubMed:29987188"
FT   MUTAGEN         109..111
FT                   /note="KVH->AVA: Decrease in interaction with EIF4G1."
FT                   /evidence="ECO:0000269|PubMed:29987188"
FT   CONFLICT        31
FT                   /note="I -> V (in Ref. 3; AAD19900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="A -> P (in Ref. 3; AAD19900)"
FT                   /evidence="ECO:0000305"
FT   TURN            6..9
FT                   /evidence="ECO:0007829|PDB:8PJ1"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:8PPL"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:6ZP4"
FT   HELIX           24..28
FT                   /evidence="ECO:0007829|PDB:8PJ1"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:2IF1"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:6YBW"
FT   HELIX           58..67
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:8PPL"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   HELIX           90..97
FT                   /evidence="ECO:0007829|PDB:9NPX"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:6ZP4"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:8PPL"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:8PPL"
SQ   SEQUENCE   113 AA;  12732 MW;  A7BC7F9B53FFEB2C CRC64;
     MSAIQNLHSF DPFADASKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI ADDYDKKKLV
     KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLVEI GLAKDDQLKV HGF
//