I17RA_MOUSE
ID I17RA_MOUSE Reviewed; 864 AA.
AC Q60943;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Interleukin-17 receptor A;
DE Short=IL-17 receptor A;
DE Short=IL-17RA;
DE AltName: CD_antigen=CD217;
DE Flags: Precursor;
GN Name=Il17ra; Synonyms=Il17r;
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], AND FUNCTION.
RC TISSUE=Thymic lymphoma;
RX PubMed=8777726; DOI=10.1016/1074-7613(95)90070-5;
RA Yao Z., Fanslow W.C., Seldin M.F., Rousseau A.-M., Painter S.L.,
RA Comeau M.R., Cohen J.I., Spriggs M.K.;
RT "Herpesvirus Saimiri encodes a new cytokine, IL-17, which binds to a novel
RT cytokine receptor.";
RL Immunity 3:811-821(1995).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17911633; DOI=10.4049/jimmunol.179.8.5462;
RA Kuestner R.E., Taft D.W., Haran A., Brandt C.S., Brender T., Lum K.,
RA Harder B., Okada S., Ostrander C.D., Kreindler J.L., Aujla S.J.,
RA Reardon B., Moore M., Shea P., Schreckhise R., Bukowski T.R., Presnell S.,
RA Guerra-Lewis P., Parrish-Novak J., Ellsworth J.L., Jaspers S., Lewis K.E.,
RA Appleby M., Kolls J.K., Rixon M., West J.W., Gao Z., Levin S.D.;
RT "Identification of the IL-17 receptor related molecule IL-17RC as the
RT receptor for IL-17F.";
RL J. Immunol. 179:5462-5473(2007).
RN [3]
RP FUNCTION.
RX PubMed=18157131; DOI=10.1038/ni1552;
RA Hsu H.C., Yang P., Wang J., Wu Q., Myers R., Chen J., Yi J., Guentert T.,
RA Tousson A., Stanus A.L., Le T.V., Lorenz R.G., Xu H., Kolls J.K.,
RA Carter R.H., Chaplin D.D., Williams R.W., Mountz J.D.;
RT "Interleukin 17-producing T helper cells and interleukin 17 orchestrate
RT autoreactive germinal center development in autoimmune BXD2 mice.";
RL Nat. Immunol. 9:166-175(2008).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19144317; DOI=10.1016/j.immuni.2008.11.009;
RA Ishigame H., Kakuta S., Nagai T., Kadoki M., Nambu A., Komiyama Y.,
RA Fujikado N., Tanahashi Y., Akitsu A., Kotaki H., Sudo K., Nakae S.,
RA Sasakawa C., Iwakura Y.;
RT "Differential roles of interleukin-17A and -17F in host defense against
RT mucoepithelial bacterial infection and allergic responses.";
RL Immunity 30:108-119(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20364087; DOI=10.1172/jci40891;
RA Cho J.S., Pietras E.M., Garcia N.C., Ramos R.I., Farzam D.M., Monroe H.R.,
RA Magorien J.E., Blauvelt A., Kolls J.K., Cheung A.L., Cheng G., Modlin R.L.,
RA Miller L.S.;
RT "IL-17 is essential for host defense against cutaneous Staphylococcus
RT aureus infection in mice.";
RL J. Clin. Invest. 120:1762-1773(2010).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20554964; DOI=10.4049/jimmunol.0903739;
RA Ho A.W., Shen F., Conti H.R., Patel N., Childs E.E., Peterson A.C.,
RA Hernandez-Santos N., Kolls J.K., Kane L.P., Ouyang W., Gaffen S.L.;
RT "IL-17RC is required for immune signaling via an extended SEF/IL-17R
RT signaling domain in the cytoplasmic tail.";
RL J. Immunol. 185:1063-1070(2010).
RN [8]
RP IDENTIFICATION AS IL17C CORECEPTOR, AND INTERACTION WITH IL17RE.
RX PubMed=21982598; DOI=10.1016/j.immuni.2011.09.010;
RA Chang S.H., Reynolds J.M., Pappu B.P., Chen G., Martinez G.J., Dong C.;
RT "Interleukin-17C promotes Th17 cell responses and autoimmune disease via
RT interleukin-17 receptor E.";
RL Immunity 35:611-621(2011).
RN [9]
RP FUNCTION, IDENTIFICATION AS IL17C CORECEPTOR, AND INTERACTION WITH IL17RE.
RX PubMed=21993849; DOI=10.1038/ni.2155;
RA Song X., Zhu S., Shi P., Liu Y., Shi Y., Levin S.D., Qian Y.;
RT "IL-17RE is the functional receptor for IL-17C and mediates mucosal
RT immunity to infection with intestinal pathogens.";
RL Nat. Immunol. 12:1151-1158(2011).
RN [10]
RP IDENTIFICATION AS IL17C CORECEPTOR, INTERACTION WITH IL17RE, AND TISSUE
RP SPECIFICITY.
RX PubMed=21993848; DOI=10.1038/ni.2156;
RA Ramirez-Carrozzi V., Sambandam A., Luis E., Lin Z., Jeet S., Lesch J.,
RA Hackney J., Kim J., Zhou M., Lai J., Modrusan Z., Sai T., Lee W., Xu M.,
RA Caplazi P., Diehl L., de Voss J., Balazs M., Gonzalez L. Jr., Singh H.,
RA Ouyang W., Pappu R.;
RT "IL-17C regulates the innate immune function of epithelial cells in an
RT autocrine manner.";
RL Nat. Immunol. 12:1159-1166(2011).
RN [11]
RP FUNCTION.
RX PubMed=27923703; DOI=10.1016/j.chom.2016.10.003;
RA Chen K., Eddens T., Trevejo-Nunez G., Way E.E., Elsegeiny W., Ricks D.M.,
RA Garg A.V., Erb C.J., Bo M., Wang T., Chen W., Lee J.S., Gaffen S.L.,
RA Kolls J.K.;
RT "IL-17 Receptor Signaling in the Lung Epithelium Is Required for Mucosal
RT Chemokine Gradients and Pulmonary Host Defense against K. pneumoniae.";
RL Cell Host Microbe 20:596-605(2016).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26735852; DOI=10.1371/journal.ppat.1005367;
RA Wang X., Ma K., Chen M., Ko K.H., Zheng B.J., Lu L.;
RT "IL-17A Promotes Pulmonary B-1a Cell Differentiation via Induction of
RT Blimp-1 Expression during Influenza Virus Infection.";
RL PLoS Pathog. 12:e1005367-e1005367(2016).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=28813677; DOI=10.1016/j.celrep.2017.07.063;
RA De Luca A., Pariano M., Cellini B., Costantini C., Villella V.R.,
RA Jose S.S., Palmieri M., Borghi M., Galosi C., Paolicelli G., Maiuri L.,
RA Fric J., Zelante T.;
RT "The IL-17F/IL-17RC Axis Promotes Respiratory Allergy in the Proximal
RT Airways.";
RL Cell Rep. 20:1667-1680(2017).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=27795421; DOI=10.1128/jvi.01529-16;
RA Acharya D., Wang P., Paul A.M., Dai J., Gate D., Lowery J.E., Stokic D.S.,
RA Leis A.A., Flavell R.A., Town T., Fikrig E., Bai F.;
RT "Interleukin-17A Promotes CD8+ T Cell Cytotoxicity To Facilitate West Nile
RT Virus Clearance.";
RL J. Virol. 91:0-0(2017).
RN [15]
RP INTERACTION WITH SARS-COV-2 VIRUS PROTEIN ORF8 (MICROBIAL INFECTION), AND
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=33723527; DOI=10.1016/j.isci.2021.102293;
RA Lin X., Fu B., Yin S., Li Z., Liu H., Zhang H., Xing N., Wang Y., Xue W.,
RA Xiong Y., Zhang S., Zhao Q., Xu S., Zhang J., Wang P., Nian W., Wang X.,
RA Wu H.;
RT "Title: ORF8 contributes to cytokine storm during SARS-CoV-2 infection by
RT activating IL-17 pathway.";
RL IScience 1:102293-102293(2021).
CC -!- FUNCTION: Receptor for IL17A and IL17F, major effector cytokines of
CC innate and adaptive immune system involved in antimicrobial host
CC defense and maintenance of tissue integrity. Receptor for IL17A
CC (PubMed:17911633, PubMed:20554964, PubMed:8777726, PubMed:27923703).
CC Receptor for IL17F (PubMed:17911633, PubMed:20554964). Binds to IL17A
CC with higher affinity than to IL17F (PubMed:17911633). Binds IL17A and
CC IL17F homodimers as part of a heterodimeric complex with IL17RC (By
CC similarity). Also binds heterodimers formed by IL17A and IL17F as part
CC of a heterodimeric complex with IL17RC (By similarity). Cytokine
CC binding triggers homotypic interaction of IL17RA and IL17RC chains with
CC TRAF3IP2 adapter, leading to TRAF6-mediated activation of NF-kappa-B
CC and MAPkinase pathways, ultimately resulting in transcriptional
CC activation of cytokines, chemokines, antimicrobial peptides and matrix
CC metalloproteinases, with potential strong immune inflammation (By
CC similarity). Involved in antimicrobial host defense primarily promoting
CC neutrophil activation and recruitment at infection sites to destroy
CC extracellular bacteria and fungi (PubMed:21993848, PubMed:20364087). In
CC secondary lymphoid organs, contributes to germinal center formation by
CC regulating the chemotactic response of B cells to CXCL12 and CXCL13,
CC enhancing retention of B cells within the germinal centers, B cell
CC somatic hypermutation rate and selection toward plasma cells
CC (PubMed:18157131). Plays a role in the maintenance of the integrity of
CC epithelial barriers during homeostasis and pathogen infection.
CC Stimulates the production of antimicrobial beta-defensins DEFB1,
CC DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry
CC of microbes through the epithelial barriers (PubMed:19144317). Involved
CC in antiviral host defense through various mechanisms. Enhances immunity
CC against West Nile virus by promoting T cell cytotoxicity
CC (PubMed:27795421). Contributes to influenza A virus (H1N1) clearance by
CC driving the differentiation of B-1a B cells, providing for production
CC of virus-specific IgM antibodies at first line of host defense
CC (PubMed:26735852). Receptor for IL17C as part of a heterodimeric
CC complex with IL17RE (PubMed:21993848, PubMed:21993849,
CC PubMed:21982598). {ECO:0000250|UniProtKB:Q96F46,
CC ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:18157131,
CC ECO:0000269|PubMed:19144317, ECO:0000269|PubMed:20364087,
CC ECO:0000269|PubMed:20554964, ECO:0000269|PubMed:21982598,
CC ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:21993849,
CC ECO:0000269|PubMed:26735852, ECO:0000269|PubMed:27795421,
CC ECO:0000269|PubMed:8777726}.
CC -!- FUNCTION: (Microbial infection) Receptor for SARS coronavirus-2/SARS-
CC CoV-2 virus protein ORF8, leading to IL17 pathway activation and an
CC increased secretion of pro-inflammatory factors through activating NF-
CC kappa-B signaling pathway. {ECO:0000269|PubMed:33723527}.
CC -!- SUBUNIT: Forms heterodimers with IL17RC; the heterodimer binds IL17A
CC and IL17F homodimers as well as the heterodimer formed by IL17A and
CC IL17F (PubMed:20554964). Forms complexes with 2:1 binding
CC stoichiometry: two receptor chains for one interleukin molecule (By
CC similarity). IL17A homodimer preferentially drives the formation of
CC IL17RA-IL17RC heterodimeric receptor complex, whereas IL17F homodimer
CC forms predominantly complexes with IL17RC homodimer (By similarity).
CC IL17A homodimer adopts an asymmetrical ternary structure with one
CC IL17RA molecule, allowing for high affinity interactions of one IL17A
CC monomer with one IL17RA molecule (via D1 and D2 domains), while
CC disfavoring binding of a second IL17RA molecule on the other IL17A
CC monomer (By similarity). IL17A-IL17F forms complexes with IL17RA-
CC IL17RC, but with lower affinity when compared to IL17A homodimer (By
CC similarity). IL17RA chain cannot distinguish between IL17A and IL17F
CC molecules, potentially enabling the formation of topologically distinct
CC complexes (By similarity). Interacts with TRAF3IP2 (By similarity).
CC Forms heterodimers with IL17RE; the heterodimer binds IL17C
CC (PubMed:21993848). {ECO:0000250|UniProtKB:Q96F46,
CC ECO:0000269|PubMed:20554964, ECO:0000269|PubMed:21993848}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 virus protein ORF8. {ECO:0000269|PubMed:33723527}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17911633};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:21993848). Highly
CC expressed in T cells and macrophages (PubMed:19144317). Highly
CC expressed in B-1a B cells and at a lower extent in B-1b and B-2 B cells
CC (at protein level) (PubMed:26735852). {ECO:0000269|PubMed:19144317,
CC ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:26735852}.
CC -!- INDUCTION: Up-regulated in brain upon West Nile virus infection.
CC {ECO:0000269|PubMed:27795421}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are susceptibile to S. aureus
CC cutaneous infection (PubMed:20364087). Mutant mice are susceptible to
CC A. fumigatus pulmonary infection characterized by excessive mucus
CC production, goblet cell hyperplasia and exacerbated T-helper 2 allergic
CC inflammation (PubMed:28813677). {ECO:0000269|PubMed:20364087,
CC ECO:0000269|PubMed:28813677}.
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DR EMBL; U31993; AAC52357.1; -; mRNA.
DR CCDS; CCDS20482.1; -.
DR RefSeq; NP_032385.1; NM_008359.2.
DR AlphaFoldDB; Q60943; -.
DR SMR; Q60943; -.
DR BioGRID; 200620; 6.
DR IntAct; Q60943; 4.
DR STRING; 10090.ENSMUSP00000002976; -.
DR GlyGen; Q60943; 7 sites.
DR iPTMnet; Q60943; -.
DR PhosphoSitePlus; Q60943; -.
DR EPD; Q60943; -.
DR MaxQB; Q60943; -.
DR PaxDb; Q60943; -.
DR PeptideAtlas; Q60943; -.
DR PRIDE; Q60943; -.
DR ProteomicsDB; 267075; -.
DR Antibodypedia; 22632; 742 antibodies from 43 providers.
DR DNASU; 16172; -.
DR Ensembl; ENSMUST00000002976; ENSMUSP00000002976; ENSMUSG00000002897.
DR GeneID; 16172; -.
DR KEGG; mmu:16172; -.
DR UCSC; uc009dnj.2; mouse.
DR CTD; 23765; -.
DR MGI; MGI:107399; Il17ra.
DR VEuPathDB; HostDB:ENSMUSG00000002897; -.
DR eggNOG; ENOG502QV5J; Eukaryota.
DR GeneTree; ENSGT00940000159018; -.
DR HOGENOM; CLU_018087_0_0_1; -.
DR InParanoid; Q60943; -.
DR OMA; KRWHFTF; -.
DR OrthoDB; 577180at2759; -.
DR PhylomeDB; Q60943; -.
DR TreeFam; TF329644; -.
DR BioGRID-ORCS; 16172; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Il17ra; mouse.
DR PRO; PR:Q60943; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q60943; protein.
DR Bgee; ENSMUSG00000002897; Expressed in granulocyte and 215 other tissues.
DR Genevisible; Q60943; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030368; F:interleukin-17 receptor activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0072537; P:fibroblast activation; ISO:MGI.
DR GO; GO:0071621; P:granulocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; ISO:MGI.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:MGI.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; ISO:MGI.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0072538; P:T-helper 17 type immune response; IDA:MGI.
DR Gene3D; 2.60.40.2150; -; 1.
DR Gene3D; 2.60.40.2160; -; 1.
DR InterPro; IPR039465; IL-17_rcpt-like.
DR InterPro; IPR032356; IL17R_fnIII_D1.
DR InterPro; IPR038683; IL17RA/B_FnIII-like_1_sf.
DR InterPro; IPR043046; IL17RA/B_FnIII-like_2_sf.
DR InterPro; IPR013568; SEFIR_dom.
DR PANTHER; PTHR15583; PTHR15583; 1.
DR Pfam; PF16556; IL17R_fnIII_D1; 1.
DR Pfam; PF08357; SEFIR; 1.
DR PROSITE; PS51534; SEFIR; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunity; Inflammatory response; Innate immunity;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..864
FT /note="Interleukin-17 receptor A"
FT /id="PRO_0000011031"
FT TOPO_DOM 32..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 379..537
FT /note="SEFIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT REGION 778..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..50
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
FT DISULFID 57..126
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
FT DISULFID 185..196
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
FT DISULFID 245..276
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
FT DISULFID 277..303
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
FT DISULFID 290..294
FT /evidence="ECO:0000250|UniProtKB:Q96F46"
SQ SEQUENCE 864 AA; 97808 MW; 343FD51AA687DA31 CRC64;
MAIRRCWPRV VPGPALGWLL LLLNVLAPGR ASPRLLDFPA PVCAQEGLSC RVKNSTCLDD
SWIHPKNLTP SSPKNIYINL SVSSTQHGEL VPVLHVEWTL QTDASILYLE GAELSVLQLN
TNERLCVKFQ FLSMLQHHRK RWRFSFSHFV VDPGQEYEVT VHHLPKPIPD GDPNHKSKII
FVPDCEDSKM KMTTSCVSSG SLWDPNITVE TLDTQHLRVD FTLWNESTPY QVLLESFSDS
ENHSCFDVVK QIFAPRQEEF HQRANVTFTL SKFHWCCHHH VQVQPFFSSC LNDCLRHAVT
VPCPVISNTT VPKPVADYIP LWVYGLITLI AILLVGSVIV LIICMTWRLS GADQEKHGDD
SKINGILPVA DLTPPPLRPR KVWIVYSADH PLYVEVVLKF AQFLITACGT EVALDLLEEQ
VISEVGVMTW VSRQKQEMVE SNSKIIILCS RGTQAKWKAI LGWAEPAVQL RCDHWKPAGD
LFTAAMNMIL PDFKRPACFG TYVVCYFSGI CSERDVPDLF NITSRYPLMD RFEEVYFRIQ
DLEMFEPGRM HHVRELTGDN YLQSPSGRQL KEAVLRFQEW QTQCPDWFER ENLCLADGQD
LPSLDEEVFE DPLLPPGGGI VKQQPLVREL PSDGCLVVDV CVSEEESRMA KLDPQLWPQR
ELVAHTLQSM VLPAEQVPAA HVVEPLHLPD GSGAAAQLPM TEDSEACPLL GVQRNSILCL
PVDSDDLPLC STPMMSPDHL QGDAREQLES LMLSVLQQSL SGQPLESWPR PEVVLEGCTP
SEEEQRQSVQ SDQGYISRSS PQPPEWLTEE EELELGEPVE SLSPEELRSL RKLQRQLFFW
ELEKNPGWNS LEPRRPTPEE QNPS
