LONP2_HUMAN
ID LONP2_HUMAN Reviewed; 852 AA.
AC Q86WA8; B7ZKL7; Q0D2H6; Q8N3B9; Q8NCE9; Q96K43;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
DE AltName: Full=Lon protease-like protein 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE Short=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE AltName: Full=Peroxisomal Lon protease {ECO:0000255|HAMAP-Rule:MF_03121};
DE Short=pLon {ECO:0000303|PubMed:18281296};
GN Name=LONP2 {ECO:0000255|HAMAP-Rule:MF_03121}; Synonyms=LONP;
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 [MRNA] (ISOFORM 1).
RA De Walque S., Van Veldhoven P.P.;
RT "A mammalian peroxisomal lon protease: cloning and characterization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-852 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14561759; DOI=10.1074/jbc.m305623200;
RA Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H.;
RT "Proteomic analysis of rat liver peroxisome: presence of peroxisome-
RT specific isozyme of Lon protease.";
RL J. Biol. Chem. 279:421-428(2004).
RN [7]
RP INTERACTION WITH ABCD3; ACOX1 AND ACAA1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF SER-743 AND 850-SER--LEU-852.
RX PubMed=18281296; DOI=10.1093/jb/mvn020;
RA Omi S., Nakata R., Okamura-Ikeda K., Konishi H., Taniguchi H.;
RT "Contribution of peroxisome-specific isoform of Lon protease in sorting
RT PTS1 proteins to peroxisomes.";
RL J. Biochem. 143:649-660(2008).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5 AND TYSND1, AND
RP MUTAGENESIS OF SER-743.
RX PubMed=22002062; DOI=10.1074/jbc.m111.285197;
RA Okumoto K., Kametani Y., Fujiki Y.;
RT "Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon
RT protease (PsLon), cooperatively regulate fatty acid beta-oxidation in
RT peroxisomal matrix.";
RL J. Biol. Chem. 286:44367-44379(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import (By similarity). May indirectly regulate peroxisomal
CC fatty acid beta-oxidation through degradation of the self-processed
CC forms of TYSND1. {ECO:0000255|HAMAP-Rule:MF_03121,
CC ECO:0000269|PubMed:22002062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC -!- SUBUNIT: Interacts with PEX5 (By similarity) (PubMed:22002062).
CC Interacts with TYSND1 (By similarity) (PubMed:22002062). May interact
CC with enzymes involved in beta-oxidation of fatty acids, including
CC ACOX1/AOX (PubMed:18281296). {ECO:0000255|HAMAP-Rule:MF_03121,
CC ECO:0000269|PubMed:18281296, ECO:0000269|PubMed:22002062}.
CC -!- INTERACTION:
CC Q86WA8; Q9H1X1: RSPH9; NbExp=2; IntAct=EBI-2513996, EBI-10305303;
CC Q86WA8; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-2513996, EBI-6872807;
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC Rule:MF_03121, ECO:0000269|PubMed:14561759,
CC ECO:0000269|PubMed:18281296, ECO:0000269|PubMed:22002062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86WA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WA8-2; Sequence=VSP_056190;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in the liver,
CC kidney and pancreas. {ECO:0000269|PubMed:18281296}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55278.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ548761; CAD68987.1; -; mRNA.
DR EMBL; AK027666; BAB55278.1; ALT_INIT; mRNA.
DR EMBL; AK074775; BAC11201.1; -; mRNA.
DR EMBL; AC007600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093910; AAH93910.1; -; mRNA.
DR EMBL; BC093912; AAH93912.1; -; mRNA.
DR EMBL; BC110434; AAI10435.1; -; mRNA.
DR EMBL; BC143246; AAI43247.1; -; mRNA.
DR EMBL; AL834201; CAD38889.1; -; mRNA.
DR CCDS; CCDS10734.1; -. [Q86WA8-1]
DR CCDS; CCDS73880.1; -. [Q86WA8-2]
DR RefSeq; NP_001287877.1; NM_001300948.2. [Q86WA8-2]
DR RefSeq; NP_113678.2; NM_031490.4. [Q86WA8-1]
DR AlphaFoldDB; Q86WA8; -.
DR SMR; Q86WA8; -.
DR BioGRID; 123755; 55.
DR IntAct; Q86WA8; 24.
DR STRING; 9606.ENSP00000285737; -.
DR MEROPS; S16.006; -.
DR iPTMnet; Q86WA8; -.
DR PhosphoSitePlus; Q86WA8; -.
DR BioMuta; LONP2; -.
DR DMDM; 74727668; -.
DR EPD; Q86WA8; -.
DR jPOST; Q86WA8; -.
DR MassIVE; Q86WA8; -.
DR MaxQB; Q86WA8; -.
DR PaxDb; Q86WA8; -.
DR PeptideAtlas; Q86WA8; -.
DR PRIDE; Q86WA8; -.
DR ProteomicsDB; 70138; -. [Q86WA8-1]
DR ProteomicsDB; 7182; -.
DR Antibodypedia; 1715; 138 antibodies from 27 providers.
DR DNASU; 83752; -.
DR Ensembl; ENST00000285737.9; ENSP00000285737.4; ENSG00000102910.14. [Q86WA8-1]
DR Ensembl; ENST00000535754.5; ENSP00000445426.1; ENSG00000102910.14. [Q86WA8-2]
DR GeneID; 83752; -.
DR KEGG; hsa:83752; -.
DR MANE-Select; ENST00000285737.9; ENSP00000285737.4; NM_031490.5; NP_113678.2.
DR UCSC; uc002efi.2; human. [Q86WA8-1]
DR CTD; 83752; -.
DR DisGeNET; 83752; -.
DR GeneCards; LONP2; -.
DR HGNC; HGNC:20598; LONP2.
DR HPA; ENSG00000102910; Low tissue specificity.
DR MIM; 617774; gene.
DR neXtProt; NX_Q86WA8; -.
DR OpenTargets; ENSG00000102910; -.
DR PharmGKB; PA162394186; -.
DR VEuPathDB; HostDB:ENSG00000102910; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_4_2_1; -.
DR InParanoid; Q86WA8; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q86WA8; -.
DR TreeFam; TF317215; -.
DR PathwayCommons; Q86WA8; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q86WA8; -.
DR SIGNOR; Q86WA8; -.
DR BioGRID-ORCS; 83752; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; LONP2; human.
DR GenomeRNAi; 83752; -.
DR Pharos; Q86WA8; Tbio.
DR PRO; PR:Q86WA8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q86WA8; protein.
DR Bgee; ENSG00000102910; Expressed in right uterine tube and 201 other tissues.
DR ExpressionAtlas; Q86WA8; baseline and differential.
DR Genevisible; Q86WA8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007031; P:peroxisome organization; NAS:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IMP:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; IMP:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Hydrolase;
KW Nucleotide-binding; Peroxisome; Protease; Reference proteome;
KW Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..852
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000287640"
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 651..837
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT MOTIF 850..852
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 743
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 786
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 156..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056190"
FT MUTAGEN 743
FT /note="S->A: Reduces degradation of self-processed forms of
FT TYSND1. Loss of ACOX1-processing."
FT /evidence="ECO:0000269|PubMed:18281296,
FT ECO:0000269|PubMed:22002062"
FT MUTAGEN 850..852
FT /note="Missing: Loss of peroxisomal localization."
FT /evidence="ECO:0000269|PubMed:18281296"
FT CONFLICT 255
FT /note="S -> A (in Ref. 4; AAI10435)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="L -> F (in Ref. 2; BAC11201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 94617 MW; 00444E4FF47417AC CRC64;
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP
IAEVEQLDRL EEFPNTCKMR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR
EALPDILTSI IRTSNKEKLQ ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK
RVIAIRPIRR ITHISGTLED EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK KRVLEYLAVR
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF
DLSQVLFIAT ANTTATIPAA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ
IQIPQVTTLD IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC
REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR LSQPGVAIGL
AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YQLTNAFGSF
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV
GGIKDKVLAA HRAGLKQVII PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT
VKTRPGLLNS KL
