PRDX1_MOUSE
ID PRDX1_MOUSE Reviewed; 199 AA.
AC P35700; Q3UBV4; Q9CWI2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Peroxiredoxin-1;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=Macrophage 23 kDa stress protein;
DE AltName: Full=Osteoblast-specific factor 3;
DE Short=OSF-3;
DE AltName: Full=Thioredoxin peroxidase 2;
DE AltName: Full=Thioredoxin-dependent peroxide reductase 2;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000305};
GN Name=Prdx1; Synonyms=Msp23, Paga, Tdpx2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peritoneal macrophage;
RX PubMed=8360158; DOI=10.1016/s0021-9258(17)46676-2;
RA Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K.,
RA Sugita Y., Bannai S.;
RT "Cloning and characterization of a 23-kDa stress-induced mouse peritoneal
RT macrophage protein.";
RL J. Biol. Chem. 268:18633-18636(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Osteoblast;
RX PubMed=8089076; DOI=10.1093/oxfordjournals.jbchem.a124388;
RA Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E.;
RT "Cloning and characterization of OSF-3, a new member of the MER5 family,
RT expressed in mouse osteoblastic cells.";
RL J. Biochem. 115:641-643(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=10548725; DOI=10.1016/s0378-1119(99)00413-8;
RA Lee T.-H., Yu S.-L., Kim S.-U., Lee K.-K., Rhee S.G., Yu D.-Y.;
RT "Characterization of mouse peroxiredoxin I genomic DNA and its
RT expression.";
RL Gene 239:243-250(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Hino K., Sato H., Bannai S.;
RT "Characterization of mouse type I peroxiredoxin gene and pseudogenes.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Hippocampus, Kidney, Liver, Mammary gland, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 17-27; 94-109; 111-120; 141-151; 159-168 AND 173-190,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19766572; DOI=10.1016/j.cell.2009.06.042;
RA Yan Y., Sabharwal P., Rao M., Sockanathan S.;
RT "The antioxidant enzyme Prdx1 controls neuronal differentiation by thiol-
RT redox-dependent activation of GDE2.";
RL Cell 138:1209-1221(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH FAM107A.
RX PubMed=21969592; DOI=10.1073/pnas.1103318108;
RA Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J.,
RA Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D.,
RA Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G.,
RA Bradke F., Eder M., Mueller M.B., Rein T.;
RT "Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a
RT stress-induced actin bundling factor that modulates synaptic efficacy and
RT cognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Might participate in the signaling cascades of growth
CC factors and tumor necrosis factor-alpha by regulating the intracellular
CC concentrations of H(2)O(2) (By similarity). Reduces an intramolecular
CC disulfide bond in GDPD5 that gates the ability to GDPD5 to drive
CC postmitotic motor neuron differentiation (PubMed:19766572).
CC {ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:19766572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q06830};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer (By similarity). Interacts with
CC GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts
CC with SESN1 and SESN2 (By similarity). Interacts with FAM107A
CC (PubMed:21969592). {ECO:0000250|UniProtKB:P0CB50,
CC ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:21969592}.
CC -!- INTERACTION:
CC P35700; P35700: Prdx1; NbExp=2; IntAct=EBI-444948, EBI-444948;
CC P35700; Q13043: STK4; Xeno; NbExp=3; IntAct=EBI-444948, EBI-367376;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
CC -!- TISSUE SPECIFICITY: Found in various tissues; high concentration in
CC liver.
CC -!- INDUCTION: By oxidative and sulfhydryl-reactive agents.
CC -!- PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a
CC decrease in enzymatic activity. {ECO:0000250|UniProtKB:Q06830}.
CC -!- DISRUPTION PHENOTYPE: Mice embryos loss approximately 50% of
CC Islet1/Islet2+ and HB9+ motor neurons, whereas dorsal-ventral
CC patterning events and the numbers of Olig2+ progenitors are normal.
CC Toward the end of the cell death phase they have equivalent numbers of
CC motor neurons as wild type embryos. {ECO:0000269|PubMed:19766572}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:Q06830}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; D16142; BAA03713.1; -; mRNA.
DR EMBL; D21252; BAA04796.1; -; mRNA.
DR EMBL; AF157331; AAD45323.1; -; Genomic_DNA.
DR EMBL; AF157329; AAD45323.1; JOINED; Genomic_DNA.
DR EMBL; AF157330; AAD45323.1; JOINED; Genomic_DNA.
DR EMBL; AB023564; BAA86992.1; -; Genomic_DNA.
DR EMBL; AK002287; BAB21990.1; -; mRNA.
DR EMBL; AK008711; BAB25847.1; -; mRNA.
DR EMBL; AK010688; BAB27120.1; -; mRNA.
DR EMBL; AK083243; BAC38827.1; -; mRNA.
DR EMBL; AK145138; BAE26255.1; -; mRNA.
DR EMBL; AK150797; BAE29860.1; -; mRNA.
DR EMBL; AK151459; BAE30417.1; -; mRNA.
DR EMBL; AK167624; BAE39676.1; -; mRNA.
DR EMBL; AK169154; BAE40933.1; -; mRNA.
DR EMBL; BC083348; AAH83348.1; -; mRNA.
DR EMBL; BC086648; AAH86648.1; -; mRNA.
DR CCDS; CCDS18515.1; -.
DR PIR; A48513; A48513.
DR RefSeq; NP_035164.1; NM_011034.4.
DR AlphaFoldDB; P35700; -.
DR SMR; P35700; -.
DR BioGRID; 202018; 33.
DR IntAct; P35700; 21.
DR MINT; P35700; -.
DR STRING; 10090.ENSMUSP00000114159; -.
DR PeroxiBase; 4555; Mm2CysPrx01-1.
DR iPTMnet; P35700; -.
DR PhosphoSitePlus; P35700; -.
DR SwissPalm; P35700; -.
DR REPRODUCTION-2DPAGE; P35700; -.
DR SWISS-2DPAGE; P35700; -.
DR CPTAC; non-CPTAC-3329; -.
DR CPTAC; non-CPTAC-3528; -.
DR EPD; P35700; -.
DR jPOST; P35700; -.
DR MaxQB; P35700; -.
DR PaxDb; P35700; -.
DR PeptideAtlas; P35700; -.
DR PRIDE; P35700; -.
DR ProteomicsDB; 291865; -.
DR TopDownProteomics; P35700; -.
DR Antibodypedia; 1574; 705 antibodies from 45 providers.
DR DNASU; 18477; -.
DR Ensembl; ENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691.
DR Ensembl; ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
DR GeneID; 18477; -.
DR KEGG; mmu:18477; -.
DR UCSC; uc008uhd.1; mouse.
DR CTD; 5052; -.
DR MGI; MGI:99523; Prdx1.
DR VEuPathDB; HostDB:ENSMUSG00000028691; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000154277; -.
DR InParanoid; P35700; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; P35700; -.
DR TreeFam; TF105181; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 18477; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Prdx1; mouse.
DR PRO; PR:P35700; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P35700; protein.
DR Bgee; ENSMUSG00000028691; Expressed in vas deferens and 271 other tissues.
DR ExpressionAtlas; P35700; baseline and differential.
DR Genevisible; P35700; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0051920; F:peroxiredoxin activity; ISO:MGI.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Redox-active center; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CHAIN 2..199
FT /note="Peroxiredoxin-1"
FT /id="PRO_0000135077"
FT DOMAIN 6..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 52
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 7
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 52
FT /note="Interchain (with C-173); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 173
FT /note="Interchain (with C-52; in linked form)"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CONFLICT 196
FT /note="S -> F (in Ref. 5; BAB27120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22176 MW; BEF5C995A86124D1 CRC64;
MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF VCPTEIIAFS
DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLISDPKR TIAQDYGVLK
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG
SDTIKPDVNK SKEYFSKQK
