ID PXDNL_HUMAN Reviewed; 1463 AA. AC A1KZ92; B5ME43; B6CGZ3; H0YBM9; Q6ZMR2; Q96LH9; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 13-FEB-2019, entry version 111. DE RecName: Full=Peroxidasin-like protein; DE EC=1.11.1.7; DE AltName: Full=Cardiac peroxidase; DE AltName: Full=Vascular peroxidase 2; DE AltName: Full=polysomal ribonuclease 1; DE Short=PRM1; DE Flags: Precursor; GN Name=PXDNL; Synonyms=VPO2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-981. RX PubMed=18929642; DOI=10.1016/j.freeradbiomed.2008.09.009; RA Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.; RT "Identification and characterization of VPO1, a new animal heme- RT containing peroxidase."; RL Free Radic. Biol. Med. 45:1682-1694(2008). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-981; LYS-1399 RP AND GLU-1452. RC TISSUE=Heart; RA Sum A., Peterfi Z., Geiszt M.; RT "Identification of a novel peroxidase in heart."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1463 (ISOFORM 2), RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1463 (ISOFORM 1), AND RP VARIANT VAL-981. RC TISSUE=Pericardium, and Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 752-1463, AND VARIANT RP VAL-981. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION (ISOFORM PMR1), AND SUBCELLULAR LOCATION. RX PubMed=12923263; DOI=10.1261/rna.5720303; RA Bremer K.A., Stevens A., Schoenberg D.R.; RT "An endonuclease activity similar to Xenopus PMR1 catalyzes the RT degradation of normal and nonsense-containing human beta-globin mRNA RT in erythroid cells."; RL RNA 9:1157-1167(2003). RN [7] RP ALTERNATIVE SPLICING (ISOFORM PMR1), FUNCTION, TISSUE SPECIFICITY, RP PHOSPHORYLATION, AND INTERACTION WITH SRC. RX PubMed=22543864; DOI=10.1261/rna.031369.111; RA Gu S.Q., Bakthavachalu B., Han J., Patil D.P., Otsuka Y., Guda C., RA Schoenberg D.R.; RT "Identification of the human PMR1 mRNA endonuclease as an RT alternatively processed product of the gene for peroxidasin-like RT protein."; RL RNA 18:1186-1196(2012). CC -!- FUNCTION: Isoform PMR1: Endonuclease selectively degrading some CC target mRNAs while they are engaged by translating ribosomes, CC among which albumin and beta-globin mRNAs. CC {ECO:0000269|PubMed:22543864}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + CC 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; CC EC=1.11.1.7; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently CC per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform PMR1: Cytoplasm. Note=Associates CC with polysomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=A1KZ92-1; Sequence=Displayed; CC Name=2; CC IsoId=A1KZ92-2; Sequence=VSP_033070, VSP_033071; CC Note=No experimental confirmation available.; CC Name=PMR1; CC IsoId=A1KZ92-3; Sequence=VSP_044240, VSP_044241; CC -!- TISSUE SPECIFICITY: the 57 kDa isoform PMR1 is the only form CC detected at protein levels in human cell lines. CC {ECO:0000269|PubMed:22543864}. CC -!- PTM: Phosphorylation by SRC on tyrosine residues is required for CC targeting to polysomes. {ECO:0000269|PubMed:22543864}. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00298}. CC -!- SEQUENCE CAUTION: CC Sequence=AAX70929.1; Type=Frameshift; Positions=127, 132; Evidence={ECO:0000305}; CC Sequence=BAB71713.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAD18663.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=EAW86707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; EU170240; ABX24517.1; -; mRNA. DR EMBL; AY877349; AAX70929.1; ALT_FRAME; mRNA. DR EMBL; AC090186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC103958; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107374; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011128; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC012413; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK058200; BAB71713.1; ALT_INIT; mRNA. DR EMBL; AK131524; BAD18663.1; ALT_INIT; mRNA. DR EMBL; CH471068; EAW86707.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS47855.1; -. [A1KZ92-1] DR RefSeq; NP_653252.3; NM_144651.4. DR UniGene; Hs.444882; -. DR ProteinModelPortal; A1KZ92; -. DR SMR; A1KZ92; -. DR BioGrid; 126492; 7. DR STRING; 9606.ENSP00000348645; -. DR PeroxiBase; 5398; HsPxd02. DR PeroxiBase; 5827; HsPxd03. DR iPTMnet; A1KZ92; -. DR PhosphoSitePlus; A1KZ92; -. DR BioMuta; PXDNL; -. DR EPD; A1KZ92; -. DR jPOST; A1KZ92; -. DR MaxQB; A1KZ92; -. DR PaxDb; A1KZ92; -. DR PRIDE; A1KZ92; -. DR ProteomicsDB; 126; -. DR ProteomicsDB; 127; -. [A1KZ92-2] DR Ensembl; ENST00000356297; ENSP00000348645; ENSG00000147485. [A1KZ92-1] DR GeneID; 137902; -. DR KEGG; hsa:137902; -. DR UCSC; uc003xqu.5; human. [A1KZ92-1] DR CTD; 137902; -. DR DisGeNET; 137902; -. DR EuPathDB; HostDB:ENSG00000147485.12; -. DR GeneCards; PXDNL; -. DR HGNC; HGNC:26359; PXDNL. DR HPA; HPA007919; -. DR neXtProt; NX_A1KZ92; -. DR OpenTargets; ENSG00000147485; -. DR PharmGKB; PA142671110; -. DR eggNOG; KOG2408; Eukaryota. DR eggNOG; ENOG410XPZ3; LUCA. DR GeneTree; ENSGT00940000163562; -. DR HOGENOM; HOG000016084; -. DR HOVERGEN; HBG108312; -. DR InParanoid; A1KZ92; -. DR KO; K19511; -. DR OMA; RVRNGRC; -. DR OrthoDB; 1324608at2759; -. DR PhylomeDB; A1KZ92; -. DR TreeFam; TF314316; -. DR BRENDA; 1.11.1.7; 2681. DR GenomeRNAi; 137902; -. DR PRO; PR:A1KZ92; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000147485; Expressed in 75 organ(s), highest expression level in right atrium auricular region. DR ExpressionAtlas; A1KZ92; baseline and differential. DR Genevisible; A1KZ92; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB. DR GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd09826; peroxidasin_like; 1. DR Gene3D; 1.10.640.10; -; 1. DR Gene3D; 2.60.40.10; -; 4. DR Gene3D; 3.80.10.10; -; 1. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR037120; Haem_peroxidase_sf_animal. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR034824; Peroxidasin_peroxidase. DR InterPro; IPR029610; PXDNL. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR11475:SF38; PTHR11475:SF38; 3. DR Pfam; PF03098; An_peroxidase; 1. DR Pfam; PF07679; I-set; 3. DR Pfam; PF13855; LRR_8; 2. DR Pfam; PF00093; VWC; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 4. DR SMART; SM00369; LRR_TYP; 6. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF48113; SSF48113; 1. DR SUPFAM; SSF48726; SSF48726; 4. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS51450; LRR; 6. DR PROSITE; PS50292; PEROXIDASE_3; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Complete proteome; Cytoplasm; KW Disulfide bond; Endonuclease; Glycoprotein; Heme; Hydrogen peroxide; KW Hydrolase; Immunoglobulin domain; Iron; Leucine-rich repeat; KW Metal-binding; Nuclease; Oxidoreductase; Peroxidase; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 1463 Peroxidasin-like protein. FT /FTId=PRO_0000330731. FT DOMAIN 24 50 LRRNT. FT REPEAT 51 72 LRR 1. FT REPEAT 75 96 LRR 2. FT REPEAT 99 120 LRR 3. FT REPEAT 123 144 LRR 4. FT REPEAT 147 168 LRR 5. FT DOMAIN 180 233 LRRCT. FT DOMAIN 234 322 Ig-like C2-type 1. FT DOMAIN 330 414 Ig-like C2-type 2. FT DOMAIN 419 504 Ig-like C2-type 3. FT DOMAIN 507 596 Ig-like C2-type 4. FT DOMAIN 1393 1451 VWFC. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT ACT_SITE 812 812 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 813 813 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 891 891 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 893 893 Calcium; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT METAL 895 895 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 897 897 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 1057 1057 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT SITE 960 960 Transition state stabilizer. FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT CARBOHYD 387 387 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 255 305 {ECO:0000250}. FT DISULFID 351 398 {ECO:0000250}. FT DISULFID 440 488 {ECO:0000250}. FT DISULFID 532 580 {ECO:0000250}. FT DISULFID 718 734 {ECO:0000250}. FT DISULFID 832 842 {ECO:0000250}. FT DISULFID 836 859 {ECO:0000250}. FT DISULFID 944 953 {ECO:0000250}. FT DISULFID 1160 1217 {ECO:0000250}. FT DISULFID 1258 1284 {ECO:0000250}. FT VAR_SEQ 1 801 Missing (in isoform PMR1). {ECO:0000305}. FT /FTId=VSP_044240. FT VAR_SEQ 1302 1463 CRSRGQFRAVTQESQKKRSAQYSYPVDKDMELSHLRSRQQD FT KIYVGEDARNVTVLAKTKFSQDFSTFAAEIQETITALREQI FT NKLEARLRQAGCTDVRGVPRKAEERWMKEDCTHCICESGQV FT TCVVEICPPAPCPSPELVKGTCCPVCRDRGMPSDSPEKR FT -> KQAGGTPEAGRVYRC (in isoform PMR1). FT {ECO:0000305}. FT /FTId=VSP_044241. FT VAR_SEQ 1302 1316 CRSRGQFRAVTQESQ -> KQAGGTPEAGRVYRC (in FT isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_033070. FT VAR_SEQ 1317 1463 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_033071. FT VARIANT 343 343 I -> T (in dbSNP:rs7833909). FT /FTId=VAR_050488. FT VARIANT 583 583 R -> Q (in dbSNP:rs16916235). FT /FTId=VAR_050489. FT VARIANT 616 616 D -> A (in dbSNP:rs16916207). FT /FTId=VAR_050490. FT VARIANT 981 981 M -> V (in dbSNP:rs2977020). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:18929642, FT ECO:0000269|Ref.2, ECO:0000269|Ref.5}. FT /FTId=VAR_050491. FT VARIANT 1327 1327 V -> D (in dbSNP:rs11774588). FT /FTId=VAR_050492. FT VARIANT 1399 1399 R -> K (in dbSNP:rs7827446). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_050493. FT VARIANT 1452 1452 D -> E (in dbSNP:rs1052704). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_050494. FT CONFLICT 781 781 R -> G (in Ref. 4; BAD18663). FT {ECO:0000305}. FT CONFLICT 833 833 S -> N (in Ref. 4; BAD18663). FT {ECO:0000305}. SQ SEQUENCE 1463 AA; 163686 MW; F6FE8200892CCCAE CRC64; MEPRLFCWTT LFLLAGWCLP GLPCPSRCLC FKSTVRCMHL MLDHIPQVPQ QTTVLDLRFN RIREIPGSAF KKLKNLNTLL LNNNHIRKIS RNAFEGLENL LYLYLYKNEI HALDKQTFKG LISLEHLYIH FNQLEMLQPE TFGDLLRLER LFLHNNKLSK IPAGSFSNLD SLKRLRLDSN ALVCDCDLMW LGELLQGFAQ HGHTQAAATC EYPRRLHGRA VASVTVEEFN CQSPRITFEP QDVEVPSGNT VYFTCRAEGN PKPEIIWIHN NHSLDLEDDT RLNVFDDGTL MIRNTRESDQ GVYQCMARNS AGEAKTQSAM LRYSSLPAKP SFVIQPQDTE VLIGTSTTLE CMATGHPHPL ITWTRDNGLE LDGSRHVATS SGLYLQNITQ RDHGRFTCHA NNSHGTVQAA ANIIVQAPPQ FTVTPKDQVV LEEHAVEWLC EADGNPPPVI VWTKTGGQLP VEGQHTVLSS GTLRIDRAAQ HDQGQYECQA VSSLGVKKVS VQLTVKPKAL AVFTQLPQDT SVEVGKNINI SCHAQGEPQP IITWNKEGVQ ITESGKFHVD DEGTLTIYDA GFPDQGRYEC VARNSFGLAV TNMFLTVTAI QGRQAGDDFV ESSILDAVQR VDSAINSTRR HLFSQKPHTS SDLLAQFHYP RDPLIVEMAR AGEIFEHTLQ LIRERVKQGL TVDLEGKEFR YNDLVSPRSL SLIANLSGCT ARRPLPNCSN RCFHAKYRAH DGTCNNLQQP TWGAALTAFA RLLQPAYRDG IRAPRGLGLP VGSRQPLPPP RLVATVWARA AAVTPDHSYT RMLMHWGWFL EHDLDHTVPA LSTARFSDGR PCSSVCTNDP PCFPMNTRHA DPRGTHAPCM LFARSSPACA SGRPSATVDS VYAREQINQQ TAYIDGSNVY GSSERESQAL RDPSVPRGLL KTGFPWPPSG KPLLPFSTGP PTECARQEQE SPCFLAGDHR ANEHLALAAM HTLWFREHNR MATELSALNP HWEGNTVYQE ARKIVGAELQ HITYSHWLPK VLGDPGTRML RGYRGYNPNV NAGIINSFAT AAFRFGHTLI NPILYRLNAT LGEISEGHLP FHKALFSPSR IIKEGGIDPV LRGLFGVAAK WRAPSYLLSP ELTQRLFSAA YSAAVDSAAT IIQRGRDHGI PPYVDFRVFC NLTSVKNFED LQNEIKDSEI RQKLRKLYGS PGDIDLWPAL MVEDLIPGTR VGPTLMCLFV TQFQRLRDGD RFWYENPGVF TPAQLTQLKQ ASLSRVLCDN GDSIQQVQAD VFVKAEYPQD YLNCSEIPKV DLRVWQDCCA DCRSRGQFRA VTQESQKKRS AQYSYPVDKD MELSHLRSRQ QDKIYVGEDA RNVTVLAKTK FSQDFSTFAA EIQETITALR EQINKLEARL RQAGCTDVRG VPRKAEERWM KEDCTHCICE SGQVTCVVEI CPPAPCPSPE LVKGTCCPVC RDRGMPSDSP EKR //