MALT1_MOUSE
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 03-AUG-2022, entry version 139.
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},
RC Lung {ECO:0000312|EMBL:BAC39355.1}, and
RC Thymus {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}.
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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; 6.
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; Q2TBA3; -.
DR PeptideAtlas; Q2TBA3; -.
DR PRIDE; Q2TBA3; -.
DR ProteomicsDB; 292010; -. [Q2TBA3-1]
DR ProteomicsDB; 292011; -. [Q2TBA3-2]
DR Antibodypedia; 1194; 772 antibodies from 45 providers.
DR DNASU; 240354; -.
DR Ensembl; ENSMUST00000049248; ENSMUSP00000048376; ENSMUSG00000032688. [Q2TBA3-2]
DR Ensembl; ENSMUST00000224056; ENSMUSP00000153585; ENSMUSG00000032688. [Q2TBA3-1]
DR GeneID; 240354; -.
DR KEGG; mmu:240354; -.
DR UCSC; uc008fez.1; mouse. [Q2TBA3-2]
DR UCSC; uc008ffa.1; mouse. [Q2TBA3-1]
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; PVPHYQW; -.
DR OrthoDB; 1270431at2759; -.
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 75 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 209 other tissues.
DR ExpressionAtlas; Q2TBA3; baseline and differential.
DR Genevisible; Q2TBA3; MM.
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; ISO:MGI.
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:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase 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:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; 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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP: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 Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.60.40.10; -; 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; IPR033540; MALT1.
DR InterPro; IPR037940; MALT1_Death.
DR InterPro; IPR041077; MALT1_Ig.
DR InterPro; IPR001309; Pept_C14_p20.
DR PANTHER; PTHR22576:SF40; PTHR22576:SF40; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18703; MALT1_Ig; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
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
