NOX4_MOUSE
ID NOX4_MOUSE Reviewed; 578 AA.
AC Q9JHI8; Q3TF39; Q8C3M1; Q8VCA3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NADPH oxidase 4;
DE EC=1.6.3.-;
DE AltName: Full=Kidney oxidase-1;
DE Short=KOX-1;
DE AltName: Full=Kidney superoxide-producing NADPH oxidase;
DE AltName: Full=Renal NAD(P)H-oxidase;
DE AltName: Full=Superoxide-generating NADPH oxidase 4;
GN Name=Nox4; Synonyms=Renox;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP ACTIVITY REGULATION.
RC TISSUE=Kidney;
RX PubMed=10869423; DOI=10.1073/pnas.130135897;
RA Geiszt M., Kopp J.B., Varnai P., Leto T.L.;
RT "Identification of renox, an NAD(P)H oxidase in kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11032835; DOI=10.1074/jbc.m007597200;
RA Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S.,
RA Hattori M., Sakaki Y., Sumimoto H.;
RT "A novel superoxide-producing NAD(P)H oxidase in kidney.";
RL J. Biol. Chem. 276:1417-1423(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11098048; DOI=10.1074/jbc.m001004200;
RA Yang S., Madyastha P., Bingel S., Ries W., Key L.;
RT "A new superoxide-generating oxidase in murine osteoclasts.";
RL J. Biol. Chem. 276:5452-5458(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Banfi B., Maturana A., Demaurex N., Krause K.-H.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Liver;
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] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 INDUCTION.
RX PubMed=15016652; DOI=10.1182/blood-2003-07-2240;
RA Suliman H.B., Ali M., Piantadosi C.A.;
RT "Superoxide dismutase-3 promotes full expression of the EPO response to
RT hypoxia.";
RL Blood 104:43-50(2004).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=15638999; DOI=10.1211/0022357055119;
RA Ding Y., Chen Z.-J., Liu S., Che D., Vetter M., Chang C.-H.;
RT "Inhibition of Nox-4 activity by plumbagin, a plant-derived bioactive
RT naphthoquinone.";
RL J. Pharm. Pharmacol. 57:111-116(2005).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15802177; DOI=10.1016/j.neuroscience.2004.12.038;
RA Vallet P., Charnay Y., Steger K., Ogier-Denis E., Kovari E., Herrmann F.,
RA Michel J.-P., Szanto I.;
RT "Neuronal expression of the NADPH oxidase NOX4, and its regulation in mouse
RT experimental brain ischemia.";
RL Neuroscience 132:233-238(2005).
CC -!- FUNCTION: Constitutive NADPH oxidase which generates superoxide
CC intracellularly upon formation of a complex with CYBA/p22phox.
CC Regulates signaling cascades probably through phosphatases inhibition.
CC May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium
CC channel and HIF1A activity. May regulate insulin signaling cascade. May
CC play a role in apoptosis, bone resorption and lipolysaccharide-mediated
CC activation of NFKB. {ECO:0000269|PubMed:10869423,
CC ECO:0000269|PubMed:11098048}.
CC -!- ACTIVITY REGULATION: Activated by insulin. Inhibited by diphenylene
CC iodonium (By similarity). Inhibited by plumbagin. Activated by phorbol
CC 12-myristate 13-acetate (PMA). {ECO:0000250,
CC ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:15638999}.
CC -!- SUBUNIT: Interacts with, relocalizes and stabilizes CYBA/p22phox.
CC Interacts with TLR4. Interacts with protein disulfide isomerase (By
CC similarity). Interacts with PPP1R15A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cell junction, focal
CC adhesion {ECO:0000250}. Cell membrane {ECO:0000250}. Note=May localize
CC to plasma membrane and focal adhesions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JHI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JHI8-2; Sequence=VSP_019060, VSP_019061;
CC Name=3;
CC IsoId=Q9JHI8-3; Sequence=VSP_019063, VSP_019064;
CC Name=4;
CC IsoId=Q9JHI8-4; Sequence=VSP_019062;
CC -!- TISSUE SPECIFICITY: EXpressed in brain, in all layers of the
CC cerebellum, in pyramidal cells of the Ammon horn and in Purkinje cells
CC (at protein level). Expressed in osteoclasts, leukocytes, kidney, liver
CC and lung. {ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:11098048,
CC ECO:0000269|PubMed:15802177}.
CC -!- INDUCTION: Upon brain ischemia it is up-regulated in ischemic tissues
CC and more specially in neocapillaries (at protein level). Up-regulated
CC upon hypoxia. {ECO:0000269|PubMed:15016652,
CC ECO:0000269|PubMed:15802177}.
CC -!- PTM: N-glycosylation is required for the function. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC021378; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF261944; AAF87573.1; -; mRNA.
DR EMBL; AB041034; BAA95682.1; -; mRNA.
DR EMBL; AB042745; BAB18134.1; -; mRNA.
DR EMBL; AF218723; AAF43142.1; -; mRNA.
DR EMBL; AF276957; AAK69443.1; -; mRNA.
DR EMBL; AK050371; BAC34215.1; -; mRNA.
DR EMBL; AK085509; BAC39460.1; -; mRNA.
DR EMBL; AK169304; BAE41059.1; -; mRNA.
DR EMBL; BC021378; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS21437.1; -. [Q9JHI8-1]
DR RefSeq; NP_056575.1; NM_015760.5. [Q9JHI8-1]
DR RefSeq; XP_006508075.1; XM_006508012.1. [Q9JHI8-4]
DR AlphaFoldDB; Q9JHI8; -.
DR SMR; Q9JHI8; -.
DR BioGRID; 206039; 8.
DR STRING; 10090.ENSMUSP00000032781; -.
DR PeroxiBase; 5966; MmNOx04.
DR GlyGen; Q9JHI8; 2 sites.
DR iPTMnet; Q9JHI8; -.
DR PhosphoSitePlus; Q9JHI8; -.
DR MaxQB; Q9JHI8; -.
DR PaxDb; Q9JHI8; -.
DR PRIDE; Q9JHI8; -.
DR ProteomicsDB; 252995; -. [Q9JHI8-1]
DR ProteomicsDB; 252996; -. [Q9JHI8-2]
DR ProteomicsDB; 252997; -. [Q9JHI8-3]
DR ProteomicsDB; 252998; -. [Q9JHI8-4]
DR ABCD; Q9JHI8; 1 sequenced antibody.
DR Antibodypedia; 17747; 640 antibodies from 38 providers.
DR DNASU; 50490; -.
DR Ensembl; ENSMUST00000032781; ENSMUSP00000032781; ENSMUSG00000030562. [Q9JHI8-1]
DR Ensembl; ENSMUST00000068829; ENSMUSP00000070039; ENSMUSG00000030562. [Q9JHI8-3]
DR GeneID; 50490; -.
DR KEGG; mmu:50490; -.
DR UCSC; uc009ifj.2; mouse. [Q9JHI8-2]
DR UCSC; uc009ifl.2; mouse. [Q9JHI8-1]
DR UCSC; uc009ifm.2; mouse. [Q9JHI8-4]
DR CTD; 50507; -.
DR MGI; MGI:1354184; Nox4.
DR VEuPathDB; HostDB:ENSMUSG00000030562; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000159621; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; Q9JHI8; -.
DR OMA; FIRGTHV; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9JHI8; -.
DR TreeFam; TF105354; -.
DR BRENDA; 1.6.3.1; 3474.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 50490; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Nox4; mouse.
DR PRO; PR:Q9JHI8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JHI8; protein.
DR Bgee; ENSMUSG00000030562; Expressed in adult mammalian kidney and 151 other tissues.
DR ExpressionAtlas; Q9JHI8; baseline and differential.
DR Genevisible; Q9JHI8; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0072341; F:modified amino acid binding; ISO:MGI.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISO:MGI.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IMP:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; ISO:MGI.
DR GO; GO:0003015; P:heart process; IGI:ARUK-UCL.
DR GO; GO:0050667; P:homocysteine metabolic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:ARUK-UCL.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB.
DR GO; GO:0006801; P:superoxide metabolic process; ISO:MGI.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="NADPH oxidase 4"
FT /id="PRO_0000238981"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..303
FT /note="Ferric oxidoreductase"
FT DOMAIN 304..419
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 248..575
FT /note="Mediates interaction with TLR4"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 150..164
FT /note="DPRKLLFTTIPGLTG -> VGGVCFSIFCSLVIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019060"
FT VAR_SEQ 165..578
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019061"
FT VAR_SEQ 358
FT /note="M -> MLCQKRWQPWHSRVWIYSFFVCSDAACHEDTSKMNHAFLL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019062"
FT VAR_SEQ 540
FT /note="K -> FEDQGQDFVPARKQHLHRGAPKALSFFSNGKGYLHFTIMTLKKCCFH
FT GSPLIF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019063"
FT VAR_SEQ 541..578
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019064"
FT CONFLICT 298
FT /note="R -> G (in Ref. 5; BAC39460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 66519 MW; 7887ADD40599A3D1 CRC64;
MAVSWRSWLA NEGVKHLCLL IWLSLNVLLF WKTFLLYNQG PEYYYIHQML GLGLCLSRAS
ASVLNLNCSL ILLPMCRTVL AYLRGSQKVP SRRTRRLLDK SKTLHITCGV TICIFSGVHV
AAHLVNALNF SVNYSEDFLE LNAARYQNED PRKLLFTTIP GLTGVCMVVV LFLMVTASTY
AIRVSNYDIF WYTHNLFFVF YMLLLLHVSG GLLKYQTNVD THPPGCISLN QTSSQNMSIP
DYVSEHFHGS LPRGFSKLED RYQKTLVKIC LEEPKFQAHF PQTWIWISGP LCLYCAERLY
RCIRSNKPVT IISVINHPSD VMELRMIKEN FKARPGQYII LHCPSVSALE NHPFTLTMCP
TETKATFGVH FKVVGDWTER FRDLLLPPSS QDSEILPFIH SRNYPKLYID GPFGSPFEES
LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFQ WFADLLCVLH
NKFWQENRPD FVNIQLYLSQ TDGIQKIIGE KYHTLNSRLF IGRPRWKLLF DEIAKCNRGK
TVGVFCCGPS SISKTLHSLS NRNNSYGTKF EYNKESFS
