GPX4_RAT
ID GPX4_RAT Reviewed; 197 AA.
AC P36970; Q6PZ55; Q76LU9; Q91XR8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Phospholipid hydroperoxide glutathione peroxidase {ECO:0000303|PubMed:7592947};
DE Short=PHGPx {ECO:0000303|PubMed:7592947};
DE EC=1.11.1.12 {ECO:0000269|PubMed:1556123};
DE AltName: Full=Glutathione peroxidase 4 {ECO:0000250|UniProtKB:O70325};
DE Short=GPx-4 {ECO:0000250|UniProtKB:O70325};
DE Short=GSHPx-4 {ECO:0000250|UniProtKB:O70325};
DE Flags: Precursor;
GN Name=Gpx4 {ECO:0000250|UniProtKB:O70325};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL).
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=7592947; DOI=10.1074/jbc.270.45.26993;
RA Pushpa-Rekha T.R., Burdsall A.L., Oleksa L.M., Chisolm G.M., Driscoll D.M.;
RT "Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and
RT identification of multiple transcription and translation start sites.";
RL J. Biol. Chem. 270:26993-26999(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NUCLEAR), SUBCELLULAR LOCATION (ISOFORM
RP NUCLEAR), AND TISSUE SPECIFICITY (ISOFORM NUCLEAR).
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=14575705; DOI=10.1016/j.bbrc.2003.09.183;
RA Nakamura T., Imai H., Tsunashima N., Nakagawa Y.;
RT "Molecular cloning and functional expression of nucleolar phospholipid
RT hydroperoxide glutathione peroxidase in mammalian cells.";
RL Biochem. Biophys. Res. Commun. 311:139-148(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Wistar;
RX PubMed=12819198; DOI=10.1074/jbc.m305327200;
RA Maiorino M., Scapin M., Ursini F., Biasolo M., Bosello V., Flohe L.;
RT "Distinct promoters determine alternative transcription of gpx-4 into
RT phospholipid-hydroperoxide glutathione peroxidase variants.";
RL J. Biol. Chem. 278:34286-34290(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NUCLEAR).
RC STRAIN=Wistar;
RA Tramer F., Vetere A., Martinelli M., Paroni F., Marsich E., Sandri G.,
RA Panfili E.;
RT "Cloning of cDNA of rat phospholipid hydroperoxide/sperm nucleus
RT glutathione peroxidase.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NUCLEAR), AND SUBCELLULAR LOCATION
RP (ISOFORM NUCLEAR).
RC TISSUE=Testis {ECO:0000312|EMBL:AAK74113.1};
RX PubMed=11344099; DOI=10.1096/fj.00-0655fje;
RA Pfeifer H., Conrad M., Roethlein D., Kyriakopoulos A., Brielmeier M.,
RA Bornkamm G.W., Behne D.;
RT "Identification of a specific sperm nuclei selenoenzyme necessary for
RT protamine thiol cross-linking during sperm maturation.";
RL FASEB J. 15:1236-1238(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-197 (ISOFORM MITOCHONDRIAL).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8749327; DOI=10.1093/jb/118.5.1061;
RA Imai H., Sumi D., Hanamoto A., Arai M., Sugiyama A., Chiba N., Kuchino Y.,
RA Nakagawa Y.;
RT "Molecular cloning and functional expression of a cDNA for rat phospholipid
RT hydroperoxide glutathione peroxidase: 3'-untranslated region of the gene is
RT necessary for functional expression.";
RL J. Biochem. 118:1061-1067(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-197 (ISOFORM MITOCHONDRIAL).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Sunde R.A., Dyer J.A., Moran T.V., Evenson J.K.;
RT "Rat liver phospholipid hydroperoxide glutathione peroxidase.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1556123; DOI=10.1016/s0021-9258(18)42673-7;
RA Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F.;
RT "Phospholipid hydroperoxide glutathione peroxidase of rat testis.
RT Gonadotropin dependence and immunocytochemical identification.";
RL J. Biol. Chem. 267:6142-6146(1992).
RN [9]
RP FUNCTION (ISOFORM CYTOPLASMIC).
RX PubMed=9442035; DOI=10.1074/jbc.273.4.1990;
RA Imai H., Narashima K., Arai M., Sakamoto H., Chiba N., Nakagawa Y.;
RT "Suppression of leukotriene formation in RBL-2H3 cells that overexpressed
RT phospholipid hydroperoxide glutathione peroxidase.";
RL J. Biol. Chem. 273:1990-1997(1998).
RN [10]
RP FUNCTION (ISOFORM MITOCHONDRIAL).
RX PubMed=9988735; DOI=10.1074/jbc.274.8.4924;
RA Arai M., Imai H., Koumura T., Yoshida M., Emoto K., Umeda M., Chiba N.,
RA Nakagawa Y.;
RT "Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a
RT major role in preventing oxidative injury to cells.";
RL J. Biol. Chem. 274:4924-4933(1999).
RN [11]
RP FUNCTION (ISOFORM MITOCHONDRIAL).
RX PubMed=10506188; DOI=10.1074/jbc.274.41.29294;
RA Nomura K., Imai H., Koumura T., Arai M., Nakagawa Y.;
RT "Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses
RT apoptosis mediated by a mitochondrial death pathway.";
RL J. Biol. Chem. 274:29294-29302(1999).
RN [12]
RP FUNCTION (ISOFORM MITOCHONDRIAL).
RX PubMed=10998361; DOI=10.1042/0264-6021:3510183;
RA Nomura K., Imai H., Koumura T., Kobayashi T., Nakagawa Y.;
RT "Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits
RT the release of cytochrome c from mitochondria by suppressing the
RT peroxidation of cardiolipin in hypoglycaemia-induced apoptosis.";
RL Biochem. J. 351:183-193(2000).
RN [13]
RP FUNCTION (ISOFORM CYTOPLASMIC).
RX PubMed=11010961; DOI=10.1074/jbc.m003191200;
RA Sakamoto H., Imai H., Nakagawa Y.;
RT "Involvement of phospholipid hydroperoxide glutathione peroxidase in the
RT modulation of prostaglandin D2 synthesis.";
RL J. Biol. Chem. 275:40028-40035(2000).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-78 (ISOFORM NUCLEAR), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Essential antioxidant peroxidase that directly reduces
CC phospholipid hydroperoxide even if they are incorporated in membranes
CC and lipoproteins (By similarity). Can also reduce fatty acid
CC hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By
CC similarity). Plays a key role in protecting cells from oxidative damage
CC by preventing membrane lipid peroxidation (PubMed:1556123,
CC PubMed:9988735). Required to prevent cells from ferroptosis, a non-
CC apoptotic cell death resulting from an iron-dependent accumulation of
CC lipid reactive oxygen species (By similarity). The presence of
CC selenocysteine (Sec) versus Cys at the active site is essential for
CC life: it provides resistance to overoxidation and prevents cells
CC against ferroptosis (By similarity). The presence of Sec at the active
CC site is also essential for the survival of a specific type of
CC parvalbumin-positive interneurons, thereby preventing against fatal
CC epileptic seizures (By similarity). May be required to protect cells
CC from the toxicity of ingested lipid hydroperoxides (By similarity).
CC Required for normal sperm development and male fertility (By
CC similarity). Essential for maturation and survival of photoreceptor
CC cells (By similarity). Plays a role in a primary T-cell response to
CC viral and parasitic infection by protecting T-cells from ferroptosis
CC and by supporting T-cell expansion (By similarity). Plays a role of
CC glutathione peroxidase in platelets in the arachidonic acid metabolism
CC (By similarity). Reduces hydroperoxy ester lipids formed by a 15-
CC lipoxygenase that may play a role as down-regulator of the cellular 15-
CC lipoxygenase pathway (By similarity). {ECO:0000250|UniProtKB:O70325,
CC ECO:0000250|UniProtKB:P36968, ECO:0000250|UniProtKB:P36969,
CC ECO:0000269|PubMed:1556123, ECO:0000269|PubMed:9988735}.
CC -!- FUNCTION: [Isoform Cytoplasmic]: Specifically able to suppress the
CC production of leukotriene and prostaglandin in response to several
CC stimuli by reducing fatty acid hydroperoxide (PubMed:9442035,
CC PubMed:11010961). {ECO:0000269|PubMed:11010961,
CC ECO:0000269|PubMed:9442035}.
CC -!- FUNCTION: [Isoform Mitochondrial]: Specifically required to prevent
CC mitochondrial cell death by mediating reduction of cardiolipin
CC hydroperoxide (PubMed:9988735, PubMed:10506188, PubMed:10998361). Also
CC required for normal sperm development and male fertility (By
CC similarity). {ECO:0000250|UniProtKB:O70325,
CC ECO:0000269|PubMed:10506188, ECO:0000269|PubMed:10998361,
CC ECO:0000269|PubMed:9988735}.
CC -!- FUNCTION: [Isoform Nuclear]: Required for male fertility by stabilizing
CC the condensed chromatin in sperm nuclei.
CC {ECO:0000250|UniProtKB:O70325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC EC=1.11.1.12; Evidence={ECO:0000269|PubMed:1556123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P36969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC Evidence={ECO:0000250|UniProtKB:P36969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC Evidence={ECO:0000250|UniProtKB:P36968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC Evidence={ECO:0000250|UniProtKB:P36968};
CC -!- SUBUNIT: Monomer. Has a tendency to form higher mass oligomers.
CC {ECO:0000250|UniProtKB:P36969}.
CC -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus
CC {ECO:0000269|PubMed:11344099}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:14575705}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000269|PubMed:1556123}. Cytoplasm {ECO:0000269|PubMed:1556123}.
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm
CC {ECO:0000269|PubMed:1556123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=Mitochondrial; Synonyms=L-form {ECO:0000303|PubMed:9988735};
CC IsoId=P36970-1; Sequence=Displayed;
CC Name=Cytoplasmic; Synonyms=S-form {ECO:0000303|PubMed:9988735};
CC IsoId=P36970-2; Sequence=VSP_018746;
CC Name=Nuclear;
CC IsoId=P36970-3; Sequence=VSP_059350;
CC -!- TISSUE SPECIFICITY: Present primarily in testis (PubMed:1556123).
CC Expressed in flagella of epididymal sperm (PubMed:19423663). Isoform
CC Cytoplasmic: Highly expressed in testis (PubMed:14575705). Present in
CC spermatogonia, spermatocyte and spermatid (at protein level)
CC (PubMed:14575705). {ECO:0000269|PubMed:14575705,
CC ECO:0000269|PubMed:1556123, ECO:0000269|PubMed:19423663}.
CC -!- MISCELLANEOUS: [Isoform Cytoplasmic]: Produced by alternative
CC initiation at Met-28 of isoform Mitochondrial. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; U37427; AAC52503.2; -; mRNA.
DR EMBL; AB072798; BAC87836.1; -; mRNA.
DR EMBL; AJ537598; CAD61276.1; -; Genomic_DNA.
DR EMBL; AJ537598; CAD61277.1; -; Genomic_DNA.
DR EMBL; AJ537598; CAD61278.1; -; Genomic_DNA.
DR EMBL; X82679; CAA57996.1; -; mRNA.
DR EMBL; AY570513; AAS76675.1; -; mRNA.
DR EMBL; AF274028; AAK74113.1; -; mRNA.
DR EMBL; L24896; AAA41842.2; -; mRNA.
DR PIR; JC4332; JC4332.
DR RefSeq; NP_001034938.1; NM_001039849.2. [P36970-3]
DR RefSeq; NP_058861.3; NM_017165.3. [P36970-1]
DR STRING; 10116.ENSRNOP00000018691; -.
DR PeroxiBase; 3733; RnoGPx04-A.
DR PeroxiBase; 3812; RnoGPx04-B.
DR PeroxiBase; 3813; RnoGPx04-C.
DR iPTMnet; P36970; -.
DR SwissPalm; P36970; -.
DR jPOST; P36970; -.
DR PRIDE; P36970; -.
DR Ensembl; ENSRNOT00000093376; ENSRNOP00000076198; ENSRNOG00000013604. [P36970-1]
DR Ensembl; ENSRNOT00000093426; ENSRNOP00000076309; ENSRNOG00000013604. [P36970-3]
DR GeneID; 29328; -.
DR KEGG; rno:29328; -.
DR CTD; 2879; -.
DR RGD; 69226; Gpx4.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000161913; -.
DR OrthoDB; 1483113at2759; -.
DR PhylomeDB; P36970; -.
DR BRENDA; 1.11.1.12; 5301.
DR Reactome; R-RNO-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR Reactome; R-RNO-9018676; Biosynthesis of D-series resolvins.
DR Reactome; R-RNO-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR Reactome; R-RNO-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
DR Reactome; R-RNO-9023661; Biosynthesis of E-series 18(R)-resolvins.
DR SABIO-RK; P36970; -.
DR PRO; PR:P36970; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000013604; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P36970; baseline and differential.
DR Genevisible; Q76LU9; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:RGD.
DR GO; GO:0008430; F:selenium binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:RGD.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0110076; P:negative regulation of ferroptosis; ISS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Cytoplasm;
KW Developmental protein; Lipid metabolism; Mitochondrion; Nucleus;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Selenocysteine; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..197
FT /note="Phospholipid hydroperoxide glutathione peroxidase"
FT /id="PRO_0000013073"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:O70325"
FT NON_STD 73
FT /note="Selenocysteine"
FT /evidence="ECO:0000305|PubMed:7592947"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..28
FT /note="MSWGRLSRLLKPALLCGALAVPGLAGTM -> MGRAAARKRGRCRQRGRSPG
FT GRRRREPGRQSPRKRPGPRRRRARARRRRRARPRRMEPIPEPFNPRPLLQDLPQTSNSH
FT EFLGL (in isoform Nuclear)"
FT /id="VSP_059350"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018746"
FT CONFLICT 45
FT /note="A -> S (in Ref. 1; AAC52503 and 3; CAD61276/
FT CAD61277/CAD61278)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="I -> V (in Ref. 2; BAC87836)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="N -> S (in Ref. 4; AAS76675)"
FT /evidence="ECO:0000305"
FT MOD_RES P36970-3:78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 197 AA; 22225 MW; 83FF001A5A42F814 CRC64;
MSWGRLSRLL KPALLCGALA VPGLAGTMCA SRDDWRCARS MHEFAAKDID GHMVCLDKYR
GCVCIVTNVA SQUGKTDVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSNQEIKEFA
AGYNVRFDMY SKICVNGDDA HPLWKWMKVQ PKGRGMLGNA IKWNFTKFLI DKNGCVVKRY
GPMEEPQVIE KDLPCYL
