LTN1_HUMAN
ID LTN1_HUMAN Reviewed; 1766 AA.
AC O94822; A6NL41; A7E2D0; B2RTS0; C9J7U3; J3KPL4; Q05C47; Q9H8M4; Q9NUY5;
AC Q9P0E9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 6.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=E3 ubiquitin-protein ligase listerin;
DE EC=2.3.2.27 {ECO:0000305|PubMed:25578875};
DE AltName: Full=RING finger protein 160;
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
DE AltName: Full=Zinc finger protein 294;
GN Name=LTN1; Synonyms=C21orf10, C21orf98, KIAA0714, RNF160, ZNF294;
GN ORFNames=HSPC087;
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), AND VARIANT SER-403.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-403.
RC TISSUE=Bone marrow;
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 1-696 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 73-1766 (ISOFORM 2), AND VARIANT SER-403.
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-473 (ISOFORM 1), AND VARIANT
RP SER-403.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORM 3).
RC TISSUE=Testis;
RA Arakawa T., Carninci P., Fukuda S., Hasegawa A., Hayashida K., Hori F.,
RA Kai C., Kawai J., Kojima M., Murata M., Nakamura M., Nishiyori H.,
RA Nomura K., Ohno M., Sasaki D., Shibazaki E., Tagami M., Tagami Y.,
RA Hayashizaki Y.;
RT "RIKEN full-length enriched human cDNA library.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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.
RX PubMed=23685075; DOI=10.1016/j.molcel.2013.04.015;
RA Shao S., von der Malsburg K., Hegde R.S.;
RT "Listerin-dependent nascent protein ubiquitination relies on ribosome
RT subunit dissociation.";
RL Mol. Cell 50:637-648(2013).
RN [10]
RP FUNCTION.
RX PubMed=25132172; DOI=10.1016/j.molcel.2014.07.006;
RA Shao S., Hegde R.S.;
RT "Reconstitution of a minimal ribosome-associated ubiquitination pathway
RT with purified factors.";
RL Mol. Cell 55:880-890(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [12] {ECO:0007744|PDB:3J92}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) AS PART OF THE RIBOSOME
RP QUALITY CONTROL COMPLEX, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBUNIT.
RX PubMed=25578875; DOI=10.1016/j.molcel.2014.12.015;
RA Shao S., Brown A., Santhanam B., Hegde R.S.;
RT "Structure and assembly pathway of the ribosome quality control complex.";
RL Mol. Cell 57:433-444(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Component of the ribosome
CC quality control complex (RQC), a ribosome-associated complex that
CC mediates ubiquitination and extraction of incompletely synthesized
CC nascent chains for proteasomal degradation (PubMed:23685075,
CC PubMed:25132172, PubMed:25578875, PubMed:28757607). Ubiquitination
CC leads to VCP/p97 recruitment for extraction and degradation of the
CC incomplete translation product (By similarity).
CC {ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:23685075,
CC ECO:0000269|PubMed:25132172, ECO:0000269|PubMed:25578875}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305|PubMed:25578875};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:25578875}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of at least the E3 ubiquitin ligase LTN1 and NEMF associated
CC with the 60S ribosomal subunit (PubMed:25578875). The complex probably
CC also contains TCF25 as well as VCP/p97 and its ubiquitin-binding
CC cofactors (By similarity). {ECO:0000250|UniProtKB:Q04781,
CC ECO:0000269|PubMed:25578875}.
CC -!- INTERACTION:
CC O94822; Q92985: IRF7; NbExp=2; IntAct=EBI-1044684, EBI-968267;
CC O94822; Q86WV6: STING1; NbExp=2; IntAct=EBI-1044684, EBI-2800345;
CC O94822; P58753: TIRAP; NbExp=2; IntAct=EBI-1044684, EBI-528644;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28757607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94822-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94822-2; Sequence=VSP_040138;
CC Name=3;
CC IsoId=O94822-3; Sequence=VSP_044911;
CC -!- PTM: Autoubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28910.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH29371.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA34434.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB90430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018257; BAA34434.2; ALT_INIT; mRNA.
DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF260011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163248; CAB90429.3; -; Genomic_DNA.
DR EMBL; AL163249; CAB90430.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC029371; AAH29371.1; ALT_SEQ; mRNA.
DR EMBL; BC140790; AAI40791.1; -; mRNA.
DR EMBL; BC150284; AAI50285.1; -; mRNA.
DR EMBL; AK001915; BAA91976.1; ALT_INIT; mRNA.
DR EMBL; AK023499; BAB14589.1; -; mRNA.
DR EMBL; AF161350; AAF28910.1; ALT_FRAME; mRNA.
DR EMBL; DB452437; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33527.2; -. [O94822-1]
DR RefSeq; NP_001307695.1; NM_001320766.1.
DR RefSeq; NP_056380.2; NM_015565.2. [O94822-1]
DR PDB; 3J92; EM; 3.60 A; 0/w/z=1-1766.
DR PDBsum; 3J92; -.
DR AlphaFoldDB; O94822; -.
DR SMR; O94822; -.
DR BioGRID; 117509; 192.
DR IntAct; O94822; 74.
DR MINT; O94822; -.
DR STRING; 9606.ENSP00000478783; -.
DR GlyGen; O94822; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; O94822; -.
DR PhosphoSitePlus; O94822; -.
DR BioMuta; LTN1; -.
DR EPD; O94822; -.
DR jPOST; O94822; -.
DR MassIVE; O94822; -.
DR MaxQB; O94822; -.
DR PaxDb; O94822; -.
DR PeptideAtlas; O94822; -.
DR PRIDE; O94822; -.
DR ProteomicsDB; 50463; -. [O94822-1]
DR ProteomicsDB; 50464; -. [O94822-2]
DR Antibodypedia; 41917; 131 antibodies from 21 providers.
DR DNASU; 26046; -.
DR Ensembl; ENST00000361371.10; ENSP00000354977.4; ENSG00000198862.14. [O94822-1]
DR Ensembl; ENST00000389194.7; ENSP00000373846.3; ENSG00000198862.14. [O94822-1]
DR Ensembl; ENST00000614971.4; ENSP00000478783.1; ENSG00000198862.14. [O94822-3]
DR GeneID; 26046; -.
DR KEGG; hsa:26046; -.
DR MANE-Select; ENST00000361371.10; ENSP00000354977.4; NM_015565.3; NP_056380.3.
DR UCSC; uc002ymr.2; human. [O94822-1]
DR CTD; 26046; -.
DR DisGeNET; 26046; -.
DR GeneCards; LTN1; -.
DR HGNC; HGNC:13082; LTN1.
DR HPA; ENSG00000198862; Low tissue specificity.
DR MIM; 613083; gene.
DR neXtProt; NX_O94822; -.
DR OpenTargets; ENSG00000198862; -.
DR PharmGKB; PA37658; -.
DR VEuPathDB; HostDB:ENSG00000198862; -.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; O94822; -.
DR OMA; CRNNFVY; -.
DR OrthoDB; 19753at2759; -.
DR PhylomeDB; O94822; -.
DR TreeFam; TF314286; -.
DR PathwayCommons; O94822; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O94822; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26046; 16 hits in 1114 CRISPR screens.
DR ChiTaRS; LTN1; human.
DR GenomeRNAi; 26046; -.
DR Pharos; O94822; Tbio.
DR PRO; PR:O94822; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O94822; protein.
DR Bgee; ENSG00000198862; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; O94822; baseline and differential.
DR Genevisible; O94822; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:1990112; C:RQC complex; IDA:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039795; LTN1/Rkr1.
DR InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389; PTHR12389; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Metal-binding;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1766
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000056304"
FT REPEAT 59..96
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 100..138
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 273..314
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 335..372
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 380..418
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 433..473
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 513..551
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 611..658
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 676..714
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 768..810
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 911..949
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1068..1105
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1184..1227
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1314..1352
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1377..1414
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1475..1512
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT ZN_FING 1715..1762
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 1
FT /note="M -> MDRVGGGKGPGGSYYRVSSSAARSRKLCPGRVNRGLSAQSTAATATM
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_044911"
FT VAR_SEQ 438..1766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040138"
FT VARIANT 403
FT /note="L -> S (in dbSNP:rs2254796)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9872452,
FT ECO:0000269|Ref.6"
FT /id="VAR_020957"
FT VARIANT 500
FT /note="A -> V (in dbSNP:rs16983580)"
FT /id="VAR_057218"
FT VARIANT 565
FT /note="G -> C (in dbSNP:rs34191159)"
FT /id="VAR_057219"
FT VARIANT 761
FT /note="V -> I (in dbSNP:rs34635840)"
FT /id="VAR_057220"
FT CONFLICT 1
FT /note="M -> K (in Ref. 5; BAA91976)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> T (in Ref. 7; DB452437)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="I -> T (in Ref. 5; BAA91976)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="A -> G (in Ref. 6; AAF28910)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Y -> D (in Ref. 5; BAB14589)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Q -> H (in Ref. 5; BAB14589/BAA91976)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="F -> Y (in Ref. 5; BAA91976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1766 AA; 200552 MW; 9312CB2283C50AEE CRC64;
MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SQSDLGYVPA IQGAEEIDSL
VDSDFRMVLR KLSKKDVTTK LKAMQEFGTM CTERDTETVK GVLPYWPRIF CKISLDHDRR
VREATQQAFE KLILKVKKQL APYLKSLMGY WLMAQCDTYT PAAFAAKDAF EAAFPPSKQP
EAIAFCKDEI TSVLQDHLIK ETPDTLSDPQ TVPEEEREAK FYRVVTCSLL ALKRLLCLLP
DNELDSLEEK FKSLLSQNKF WKYGKHSVPQ IRSAYFELVS ALCQRIPQLM KEEASKVSPS
VLLSIDDSDP IVCPALWEAV LYTLTTIEDC WLHVNAKKSV FPKLSTVIRE GGRGLATVIY
PYLLPFISKL PQSITNPKLD FFKNFLTSLV AGLSTERTKT SSLESSAVIS AFFECLRFIM
QQNLGEEEIE QMLVNDQLIP FIDAVLKDPG LQHGQLFNHL AETLSSWEAK ADTEKDEKTA
HNLENVLIHF WERLSEICVA KISEPEADVE SVLGVSNLLQ VLQKPKSSLK SSKKKNGKVR
FADEILESNK ENEKCVSSEG EKIEGWELTT EPSLTHNSSG LLSPLRKKPL EDLVCKLADI
SINYVNERKS EQHLRFLSTL LDSFSSSRVF KMLLGDEKQS IVQAKPLEIA KLVQKNPAVQ
FLYQKLIGWL NEDQRKDFGF LVDILYSALR CCDNDMERKK VLDDLTKVDL KWNSLLKIIE
KACPSSDKHA LVTPWLKGDI LGEKLVNLAD CLCNEDLESR VSSESHFSER WTLLSLVLSQ
HVKNDYLIGD VYVERIIVRL HETLFKTKKL SEAESSDSSV SFICDVAYNY FSSAKGCLLM
PSSEDLLLTL FQLCAQSKEK THLPDFLICK LKNTWLSGVN LLVHQTDSSY KESTFLHLSA
LWLKNQVQAS SLDINSLQVL LSAVDDLLNT LLESEDSYLM GVYIGSVMPN DSEWEKMRQS
LPMQWLHRPL LEGRLSLNYE CFKTDFKEQD IKTLPSHLCT SALLSKMVLI ALRKETVLEN
NELEKIIAEL LYSLQWCEEL DNPPIFLIGF CEILQKMNIT YDNLRVLGNT SGLLQLLFNR
SREHGTLWSL IIAKLILSRS ISSDEVKPHY KRKESFFPLT EGNLHTIQSL CPFLSKEEKK
EFSAQCIPAL LGWTKKDLCS TNGGFGHLAI FNSCLQTKSI DDGELLHGIL KIIISWKKEH
EDIFLFSCNL SEASPEVLGV NIEIIRFLSL FLKYCSSPLA ESEWDFIMCS MLAWLETTSE
NQALYSIPLV QLFACVSCDL ACDLSAFFDS TTLDTIGNLP VNLISEWKEF FSQGIHSLLL
PILVTVTGEN KDVSETSFQN AMLKPMCETL TYISKEQLLS HKLPARLVAD QKTNLPEYLQ
TLLNTLAPLL LFRARPVQIA VYHMLYKLMP ELPQYDQDNL KSYGDEEEEP ALSPPAALMS
LLSIQEDLLE NVLGCIPVGQ IVTIKPLSED FCYVLGYLLT WKLILTFFKA ASSQLRALYS
MYLRKTKSLN KLLYHLFRLM PENPTYAETA VEVPNKDPKT FFTEELQLSI RETTMLPYHI
PHLACSVYHM TLKDLPAMVR LWWNSSEKRV FNIVDRFTSK YVSSVLSFQE ISSVQTSTQL
FNGMTVKARA TTREVMATYT IEDIVIELII QLPSNYPLGS IIVESGKRVG VAVQQWRNWM
LQLSTYLTHQ NGSIMEGLAL WKNNVDKRFE GVEDCMICFS VIHGFNYSLP KKACRTCKKK
FHSACLYKWF TSSNKSTCPL CRETFF
