CNPY3_HUMAN
ID CNPY3_HUMAN Reviewed; 278 AA.
AC Q9BT09; O15412; Q0P6I2; Q8NF54; Q8WTU8; Q9P0F2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein canopy homolog 3;
DE AltName: Full=CTG repeat protein 4a;
DE AltName: Full=Expanded repeat-domain protein CAG/CTG 5;
DE AltName: Full=Protein associated with TLR4;
DE AltName: Full=Trinucleotide repeat-containing gene 5 protein;
DE Flags: Precursor;
GN Name=CNPY3; Synonyms=CTG4A, ERDA5, PRAT4A, TNRC5;
GN ORFNames=HSPC084, UNQ1934/PRO4409;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Colon, 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-192 (ISOFORM 1).
RC TISSUE=Brain cortex;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-278 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-278 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-153.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP INTERACTION WITH HSP90B1.
RX PubMed=20865800; DOI=10.1038/ncomms1070;
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RT "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
RT substrate-specific cochaperone.";
RL Nat. Commun. 1:79-79(2010).
RN [9]
RP ERRATUM OF PUBMED:20865800.
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RL Nat. Commun. 3:653-653(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP INVOLVEMENT IN DEE60, AND VARIANT DEE60 ARG-125.
RX PubMed=29394991; DOI=10.1016/j.ajhg.2018.01.004;
RA Mutoh H., Kato M., Akita T., Shibata T., Wakamoto H., Ikeda H., Kitaura H.,
RA Aoto K., Nakashima M., Wang T., Ohba C., Miyatake S., Miyake N., Kakita A.,
RA Miyake K., Fukuda A., Matsumoto N., Saitsu H.;
RT "Biallelic Variants in CNPY3, Encoding an Endoplasmic Reticulum Chaperone,
RT Cause Early-Onset Epileptic Encephalopathy.";
RL Am. J. Hum. Genet. 102:321-329(2018).
CC -!- FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1.
CC Required for proper TLR folding, except that of TLR3, and hence
CC controls TLR exit from the endoplasmic reticulum. Consequently,
CC required for both innate and adaptive immune responses (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HSP90B1; this interaction is disrupted in the
CC presence of ATP. Interacts with TLR1, TLR2, TLR4 and TLR9 (By
CC similarity). Strongest interaction with TLR4 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BT09; Q86V38: ATN1; NbExp=3; IntAct=EBI-2835965, EBI-11954292;
CC Q9BT09; O00501: CLDN5; NbExp=3; IntAct=EBI-2835965, EBI-18400628;
CC Q9BT09; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2835965, EBI-10976677;
CC Q9BT09; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2835965, EBI-18304435;
CC Q9BT09; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-2835965, EBI-712073;
CC Q9BT09; P28799: GRN; NbExp=3; IntAct=EBI-2835965, EBI-747754;
CC Q9BT09; P48051: KCNJ6; NbExp=3; IntAct=EBI-2835965, EBI-12017638;
CC Q9BT09; Q92876: KLK6; NbExp=3; IntAct=EBI-2835965, EBI-2432309;
CC Q9BT09; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2835965, EBI-396669;
CC Q9BT09; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2835965, EBI-5235340;
CC Q9BT09; O76024: WFS1; NbExp=3; IntAct=EBI-2835965, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT09-2; Sequence=VSP_030132, VSP_030133;
CC -!- DISEASE: Developmental and epileptic encephalopathy 60 (DEE60)
CC [MIM:617929]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE60 is an autosomal recessive condition
CC characterized by onset of seizures in the first months of life.
CC {ECO:0000269|PubMed:29394991}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the canopy family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB91442.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF28907.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY358960; AAQ89319.1; -; mRNA.
DR EMBL; AL035587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004423; AAH04423.1; -; mRNA.
DR EMBL; BC008133; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC008898; AAH08898.1; -; mRNA.
DR EMBL; BC008961; AAH08961.1; -; mRNA.
DR EMBL; BC022093; AAH22093.3; -; mRNA.
DR EMBL; U80744; AAB91442.1; ALT_FRAME; mRNA.
DR EMBL; AF161347; AAF28907.1; ALT_FRAME; mRNA.
DR EMBL; AK090425; BAC03406.1; -; mRNA.
DR CCDS; CCDS4875.1; -. [Q9BT09-1]
DR RefSeq; NP_006577.2; NM_006586.4. [Q9BT09-1]
DR AlphaFoldDB; Q9BT09; -.
DR BioGRID; 115934; 119.
DR IntAct; Q9BT09; 41.
DR MINT; Q9BT09; -.
DR STRING; 9606.ENSP00000361926; -.
DR GlyConnect; 1651; 3 N-Linked glycans (1 site).
DR GlyGen; Q9BT09; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9BT09; -.
DR PhosphoSitePlus; Q9BT09; -.
DR BioMuta; CNPY3; -.
DR DMDM; 74752319; -.
DR EPD; Q9BT09; -.
DR jPOST; Q9BT09; -.
DR MassIVE; Q9BT09; -.
DR MaxQB; Q9BT09; -.
DR PaxDb; Q9BT09; -.
DR PeptideAtlas; Q9BT09; -.
DR PRIDE; Q9BT09; -.
DR ProteomicsDB; 78939; -. [Q9BT09-1]
DR ProteomicsDB; 78940; -. [Q9BT09-2]
DR Antibodypedia; 16108; 183 antibodies from 30 providers.
DR DNASU; 10695; -.
DR Ensembl; ENST00000372836.5; ENSP00000361926.4; ENSG00000137161.18. [Q9BT09-1]
DR GeneID; 10695; -.
DR KEGG; hsa:10695; -.
DR MANE-Select; ENST00000372836.5; ENSP00000361926.4; NM_006586.5; NP_006577.2.
DR UCSC; uc003ota.5; human. [Q9BT09-1]
DR CTD; 10695; -.
DR DisGeNET; 10695; -.
DR GeneCards; CNPY3; -.
DR HGNC; HGNC:11968; CNPY3.
DR HPA; ENSG00000137161; Low tissue specificity.
DR MalaCards; CNPY3; -.
DR MIM; 610774; gene.
DR MIM; 617929; phenotype.
DR neXtProt; NX_Q9BT09; -.
DR OpenTargets; ENSG00000137161; -.
DR Orphanet; 3451; Infantile spasms syndrome.
DR PharmGKB; PA162382601; -.
DR VEuPathDB; HostDB:ENSG00000137161; -.
DR eggNOG; KOG4052; Eukaryota.
DR GeneTree; ENSGT00390000014072; -.
DR HOGENOM; CLU_078068_0_0_1; -.
DR InParanoid; Q9BT09; -.
DR OMA; DKACLDE; -.
DR PhylomeDB; Q9BT09; -.
DR TreeFam; TF318951; -.
DR PathwayCommons; Q9BT09; -.
DR Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
DR SignaLink; Q9BT09; -.
DR BioGRID-ORCS; 10695; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; CNPY3; human.
DR GenomeRNAi; 10695; -.
DR Pharos; Q9BT09; Tbio.
DR PRO; PR:Q9BT09; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BT09; protein.
DR Bgee; ENSG00000137161; Expressed in monocyte and 197 other tissues.
DR ExpressionAtlas; Q9BT09; baseline and differential.
DR Genevisible; Q9BT09; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR021852; DUF3456.
DR Pfam; PF11938; DUF3456; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Coiled coil; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Epilepsy; Glycoprotein; Immunity;
KW Innate immunity; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..278
FT /note="Protein canopy homolog 3"
FT /id="PRO_0000313780"
FT DOMAIN 47..271
FT /note="Saposin B-type"
FT REGION 215..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..179
FT /evidence="ECO:0000255"
FT COMPBIAS 246..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 49..206
FT /evidence="ECO:0000250"
FT DISULFID 52..194
FT /evidence="ECO:0000250"
FT DISULFID 104..166
FT /evidence="ECO:0000250"
FT VAR_SEQ 51..54
FT /note="VCKY -> GTCG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030132"
FT VAR_SEQ 55..278
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030133"
FT VARIANT 125
FT /note="G -> R (in DEE60; unknown pathological significance;
FT dbSNP:rs1554292759)"
FT /evidence="ECO:0000269|PubMed:29394991"
FT /id="VAR_080491"
FT VARIANT 145
FT /note="M -> I (in dbSNP:rs1063252)"
FT /id="VAR_037731"
FT VARIANT 231
FT /note="S -> I (in dbSNP:rs9471969)"
FT /id="VAR_037732"
FT CONFLICT 272
FT /note="H -> P (in Ref. 5; BAC03406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 30748 MW; 07587320D316E0CE CRC64;
MDSMPEPASR CLLLLPLLLL LLLLLPAPEL GPSQAGAEEN DWVRLPSKCE VCKYVAVELK
SAFEETGKTK EVIGTGYGIL DQKASGVKYT KSDLRLIEVT ETICKRLLDY SLHKERTGSN
RFAKGMSETF ETLHNLVHKG VKVVMDIPYE LWNETSAEVA DLKKQCDVLV EEFEEVIEDW
YRNHQEEDLT EFLCANHVLK GKDTSCLAEQ WSGKKGDTAA LGGKKSKKKS SRAKAAGGRS
SSSKQRKELG GLEGDPSPEE DEGIQKASPL THSPPDEL
