ID MALT1_MOUSE Reviewed; 832 AA. AC Q2TBA3; Q2TBA2; Q811E3; Q8BFT0; Q8C7N9; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 147. DE RecName: Full=Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog; DE EC=3.4.22.- {ECO:0000269|PubMed:25282160}; DE AltName: Full=Paracaspase; GN Name=Malt1 {ECO:0000312|MGI:MGI:2445027}; 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] {ECO:0000305, ECO:0000312|EMBL:BAC31096.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 542-832 (ISOFORMS1/2). RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31096.1}; RC TISSUE=Hippocampus {ECO:0000312|EMBL:BAC33935.1}, Lung RC {ECO:0000312|EMBL:BAC39355.1}, and Thymus RC {ECO:0000312|EMBL:BAC31096.1}; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI10488.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=Czech II {ECO:0000312|EMBL:AAH46536.1}; RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH46536.1}; 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 [3] RP FUNCTION. RX PubMed=25282160; DOI=10.1038/ni.3008; RA Jeltsch K.M., Hu D., Brenner S., Zoeller J., Heinz G.A., Nagel D., RA Vogel K.U., Rehage N., Warth S.C., Edelmann S.L., Gloury R., Martin N., RA Lohs C., Lech M., Stehklein J.E., Geerlof A., Kremmer E., Weber A., RA Anders H.J., Schmitz I., Schmidt-Supprian M., Fu M., Holtmann H., RA Krappmann D., Ruland J., Kallies A., Heikenwalder M., Heissmeyer V.; RT "Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their RT cooperatively repressed targets to promote T(H)17 differentiation."; RL Nat. Immunol. 15:1079-1089(2014). RN [4] RP IDENTIFICATION IN A CBM COMPLEX. RX PubMed=22265677; DOI=10.1016/j.immuni.2011.11.015; RA Strasser D., Neumann K., Bergmann H., Marakalala M.J., Guler R., RA Rojowska A., Hopfner K.P., Brombacher F., Urlaub H., Baier G., Brown G.D., RA Leitges M., Ruland J.; RT "Syk kinase-coupled C-type lectin receptors engage protein kinase C-delta RT to elicit Card9 adaptor-mediated innate immunity."; RL Immunity 36:32-42(2012). CC -!- FUNCTION: Protease that enhances BCL10-induced activation: acts via CC formation of CBM complexes that channel adaptive and innate immune CC signaling downstream of CARD domain-containing proteins (CARD9, CARD11 CC and CARD14) to activate NF-kappa-B and MAP kinase p38 pathways which CC stimulate expression of genes encoding pro-inflammatory cytokines and CC chemokines (By similarity). Mediates BCL10 cleavage: MALT1-dependent CC BCL10 cleavage plays an important role in T-cell antigen receptor- CC induced integrin adhesion (By similarity). Involved in the induction of CC T helper 17 cells (Th17) differentiation (By similarity). Cleaves RC3H1 CC and ZC3H12A in response to T-cell receptor (TCR) stimulation which CC releases their cooperatively repressed targets to promote Th17 cell CC differentiation (PubMed:25282160). Also mediates cleavage of N4BP1 in CC T-cells following TCR-mediated activation, leading to N4BP1 CC inactivation. May also have ubiquitin ligase activity: binds to TRAF6, CC inducing TRAF6 oligomerization and activation of its ligase activity CC (By similarity). {ECO:0000250|UniProtKB:Q9UDY8, CC ECO:0000269|PubMed:25282160}. CC -!- SUBUNIT: Homooligomer; forms oligomers which bind to TRAF6. Forms a CC complex with CARD14 and MALT1; resulting in the formation of a CBM CC (CARD14-BCL10-MALT1) complex. Forms a complex with CARD11 and MALT1; CC resulting in the formation of a CBM (CARD11-BCL10-MALT1) complex (By CC similarity). Forms a complex with CARD9 and MALT1; resulting in the CC formation of a CBM (CARD9-BCL10-MALT1) complex (PubMed:22265677). CC {ECO:0000250|UniProtKB:Q9UDY8, ECO:0000269|PubMed:22265677}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:Q9UDY8}. Nucleus {ECO:0000250|UniProtKB:Q9UDY8}. CC Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear CC structures together with BCL10 (By similarity). CC {ECO:0000250|UniProtKB:Q9UDY8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000303|PubMed:15489334}; CC IsoId=Q2TBA3-1; Sequence=Displayed; CC Name=2 {ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072}; CC IsoId=Q2TBA3-2; Sequence=VSP_052279; CC -!- SIMILARITY: Belongs to the peptidase C14B family. {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; AK041919; BAC31096.1; -; mRNA. DR EMBL; AK049821; BAC33935.1; -; mRNA. DR EMBL; AK085071; BAC39355.1; -; mRNA. DR EMBL; BC046536; AAH46536.1; -; mRNA. DR EMBL; BC110487; AAI10488.1; -; mRNA. DR EMBL; BC110488; AAI10489.1; -; mRNA. DR CCDS; CCDS29306.1; -. [Q2TBA3-2] DR CCDS; CCDS89264.1; -. [Q2TBA3-1] DR RefSeq; NP_766421.1; NM_172833.2. [Q2TBA3-2] DR RefSeq; XP_006526000.1; XM_006525937.2. DR PDB; 3V4L; X-ray; 3.15 A; A=338-729. DR PDBsum; 3V4L; -. DR AlphaFoldDB; Q2TBA3; -. DR SMR; Q2TBA3; -. DR BioGRID; 232195; 16. DR DIP; DIP-60308N; -. DR IntAct; Q2TBA3; 3. DR STRING; 10090.ENSMUSP00000048376; -. DR MEROPS; C14.026; -. DR iPTMnet; Q2TBA3; -. DR PhosphoSitePlus; Q2TBA3; -. DR EPD; Q2TBA3; -. DR MaxQB; Q2TBA3; -. DR PaxDb; 10090-ENSMUSP00000048376; -. DR PeptideAtlas; Q2TBA3; -. DR ProteomicsDB; 292010; -. [Q2TBA3-1] DR ProteomicsDB; 292011; -. [Q2TBA3-2] DR Pumba; Q2TBA3; -. DR Antibodypedia; 1194; 850 antibodies from 45 providers. DR DNASU; 240354; -. DR Ensembl; ENSMUST00000049248.7; ENSMUSP00000048376.6; ENSMUSG00000032688.10. [Q2TBA3-2] DR Ensembl; ENSMUST00000224056.3; ENSMUSP00000153585.2; ENSMUSG00000032688.10. [Q2TBA3-1] DR GeneID; 240354; -. DR KEGG; mmu:240354; -. DR UCSC; uc008fez.1; mouse. [Q2TBA3-2] DR UCSC; uc008ffa.1; mouse. [Q2TBA3-1] DR AGR; MGI:2445027; -. DR CTD; 10892; -. DR MGI; MGI:2445027; Malt1. DR VEuPathDB; HostDB:ENSMUSG00000032688; -. DR eggNOG; ENOG502QUZM; Eukaryota. DR GeneTree; ENSGT00390000018044; -. DR HOGENOM; CLU_014796_0_0_1; -. DR InParanoid; Q2TBA3; -. DR OMA; CLMSDGP; -. DR OrthoDB; 3080800at2759; -. DR PhylomeDB; Q2TBA3; -. DR TreeFam; TF319744; -. DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation. DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-MMU-5660668; CLEC7A/inflammasome pathway. DR BioGRID-ORCS; 240354; 5 hits in 80 CRISPR screens. DR ChiTaRS; Malt1; mouse. DR PRO; PR:Q2TBA3; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; Q2TBA3; Protein. DR Bgee; ENSMUSG00000032688; Expressed in spleen and 212 other cell types or tissues. DR ExpressionAtlas; Q2TBA3; baseline and differential. DR GO; GO:0032449; C:CBM complex; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002096; C:polkadots; IDA:CACAO. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl. DR GO; GO:0008233; F:peptidase activity; ISO:MGI. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0043621; F:protein self-association; ISO:MGI. DR GO; GO:0036094; F:small molecule binding; ISO:MGI. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI. DR GO; GO:0042113; P:B cell activation; IMP:MGI. DR GO; GO:0001923; P:B-1 B cell differentiation; IMP:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEP:UniProtKB. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0051168; P:nuclear export; ISO:MGI. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI. DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:MGI. DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:MGI. DR GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IMP:MGI. DR GO; GO:0009620; P:response to fungus; IMP:MGI. DR GO; GO:0042098; P:T cell proliferation; IMP:MGI. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR CDD; cd08783; Death_MALT1; 1. DR CDD; cd00096; Ig; 2. DR Gene3D; 2.60.40.3360; -; 1. DR Gene3D; 3.40.50.1460; -; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR029030; Caspase-like_dom_sf. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR037940; MALT1_Death. DR InterPro; IPR041077; MALT1_Ig. DR InterPro; IPR033540; MALT1_IG-like_dom_sf. DR InterPro; IPR011600; Pept_C14_caspase. DR InterPro; IPR001309; Pept_C14_p20. DR PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1. DR PANTHER; PTHR22576:SF40; MUCOSA-ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1; 1. DR Pfam; PF13927; Ig_3; 2. DR Pfam; PF18703; MALT1_Ig; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF52129; Caspase-like; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50208; CASPASE_P20; 1. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; Q2TBA3; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Disulfide bond; KW Hydrolase; Immunity; Immunoglobulin domain; Nucleus; Phosphoprotein; KW Protease; Reference proteome; Repeat; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q9UDY8" FT CHAIN 2..832 FT /note="Mucosa-associated lymphoid tissue lymphoma FT translocation protein 1 homolog" FT /id="PRO_0000272961" FT DOMAIN 45..132 FT /note="Death" FT /evidence="ECO:0000255" FT DOMAIN 131..207 FT /note="Ig-like C2-type 1" FT /evidence="ECO:0000255" FT DOMAIN 218..314 FT /note="Ig-like C2-type 2" FT /evidence="ECO:0000255" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..570 FT /note="Caspase-like" FT /evidence="ECO:0000255" FT MOTIF 377..384 FT /note="Nuclear export signal" FT /evidence="ECO:0000250|UniProtKB:Q9UDY8" FT COMPBIAS 16..34 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 423 FT /evidence="ECO:0000255" FT ACT_SITE 472 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:Q9UDY8" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UDY8" FT DISULFID 154..196 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 257..299 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 318..328 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_052279" FT CONFLICT 265 FT /note="P -> S (in Ref. 2; AAI10489)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="P -> H (in Ref. 2; AAI10488)" FT /evidence="ECO:0000305" FT CONFLICT 793 FT /note="T -> A (in Ref. 2; AAH46536)" FT /evidence="ECO:0000305" FT STRAND 351..357 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 369..383 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 387..393 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 396..407 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 415..427 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 430..434 FT /evidence="ECO:0007829|PDB:3V4L" FT TURN 444..446 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 450..458 FT /evidence="ECO:0007829|PDB:3V4L" FT TURN 459..461 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 463..471 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 494..500 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 518..523 FT /evidence="ECO:0007829|PDB:3V4L" FT TURN 524..528 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 533..545 FT /evidence="ECO:0007829|PDB:3V4L" FT TURN 548..553 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 557..560 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 579..589 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 598..601 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 607..616 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 619..628 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 633..641 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 651..653 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 654..658 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 659..662 FT /evidence="ECO:0007829|PDB:3V4L" FT TURN 668..670 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 675..680 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 683..685 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 690..700 FT /evidence="ECO:0007829|PDB:3V4L" FT STRAND 707..717 FT /evidence="ECO:0007829|PDB:3V4L" FT HELIX 719..723 FT /evidence="ECO:0007829|PDB:3V4L" SQ SEQUENCE 832 AA; 93216 MW; 891D59585A360D68 CRC64; MSLWGQPLQA SPPLAVRQPP TASSGPSTSP PAGATLNRLP EPLLRRLSES LDRAPEGRGW RQLAELAGSR GRLRLSGLDL EQCSLKVLEP EGSPSLCLLK LMGEKGCTVT ELSDFLQALE HTEVLPLLNP PGLKITVNPE SKAVLAGQFV KLCCRATGHP FVQYQWFKMN KEIPYGNSSE LVFNTVHVKD AGFYVCRVNN SSTFEFSQWS QLDVCDVAEV TDSFQGSMDG ISESRLQICV EPRSQRLVPG SMLLLQCVAI GSPMPHYQWF KDESPLTHET KKHYTVPYVD IEHEGTYWCH VYNDRDSQDS KKAEVTIGRT DEAVECTEDE LNNLGHPDNK EQTGQPLAKD KVALLIGNMS YWEHPKLKAP LVDVYELTNL LRQLDFKVVS LLDLTEYEMC NAVDEFLLLL DKGVYGLLYY AGHGYENFGN SFMVPVDAPN PYRSENCLCV QNILKLMQEK ETGLNVFLLD MCRKRNDYDD TIPILDALKV TANIVFGYAT CQGAEAFEIQ HSGLANGIFM KFLKDRLLED KKITVLLDEV AEDMGKCHLT KGRQALEIRS SLSEKRALTD PVQGAPCSAE ALVRNLQWAK AHELPESMCL KFQCGVHIQL GFAAEFSNVM IIYTSIVHKP PEIIMCDAYV TDFPLDLDID PKHANKGTPE ETGSYLVSKD LPKHCLYTRL SSLQKLKEHL IFTVCLSYQY SGLEDTVEEK QEVNVGKPLI AKLDMHRGLG RKTCFQACRM PDEPYHSSTS TSAGAGHFHS SQDSFHDVYH SHLGNADSGM PPDRCHCSRT PHTFISNYPP HHYCQFGRSN VPVETTDEMP FSFSDRLMIS EN //