BIR1E_MOUSE
ID BIR1E_MOUSE Reviewed; 1403 AA.
AC Q9R016; O09121; O09122; P81703; Q8CGT2; Q9R029;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Baculoviral IAP repeat-containing protein 1e;
DE AltName: Full=Neuronal apoptosis inhibitory protein 5;
GN Name=Naip5 {ECO:0000303|PubMed:12526741, ECO:0000303|PubMed:29146805};
GN Synonyms=Birc1e, Naip-rs3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10501978; DOI=10.1007/s003359901155;
RA Huang S., Scharf J.M., Growney J.D., Endrizzi M.G., Dietrich W.F.;
RT "The mouse Naip gene cluster on chromosome 13 encodes several distinct
RT functional transcripts.";
RL Mamm. Genome 10:1032-1035(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10486205; DOI=10.1006/geno.1999.5910;
RA Endrizzi M., Huang S., Scharf J.M., Kelter A.R., Wirth B., Kunkel L.M.,
RA Miller W., Dietrich W.F.;
RT "Comparative sequence analysis of the mouse and human Lgn1/SMA interval.";
RL Genomics 60:137-151(1999).
RN [3] {ECO:0000312|EMBL:AAN60211.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=P/J {ECO:0000312|EMBL:AAN60211.1};
RX PubMed=12526741; DOI=10.1016/s0960-9822(02)01359-3;
RA Wright E.K., Goodart S.A., Growney J.D., Hadinoto V., Endrizzi M.G.,
RA Long E.M., Sadigh K., Abney A.L., Bernstein-Hanley I., Dietrich W.F.;
RT "Naip5 affects host susceptibility to the intracellular pathogen Legionella
RT pneumophila.";
RL Curr. Biol. 13:27-36(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH70433.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH70433.1};
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-168.
RC STRAIN=129/SvJ;
RX PubMed=8975718; DOI=10.1006/geno.1996.0644;
RA Scharf J.M., Damron D., Frisella A., Bruno S., Beggs A.H., Kunkel L.M.,
RA Dietrich W.F.;
RT "The mouse region syntenic for human spinal muscular atrophy lies within
RT the Lgn1 critical interval and contains multiple copies of Naip exon 5.";
RL Genomics 38:405-417(1996).
RN [7]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH S.TYPHIMURIUM FLAGELLIN.
RX PubMed=21874021; DOI=10.1038/nature10394;
RA Kofoed E.M., Vance R.E.;
RT "Innate immune recognition of bacterial ligands by NAIPs determines
RT inflammasome specificity.";
RL Nature 477:592-595(2011).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH S.TYPHIMURIUM FLAGELLIN.
RX PubMed=21918512; DOI=10.1038/nature10510;
RA Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., Liu L., Shao F.;
RT "The NLRC4 inflammasome receptors for bacterial flagellin and type III
RT secretion apparatus.";
RL Nature 477:596-600(2011).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=18414036; DOI=10.4161/cc.7.8.5783;
RA Dubrez-Daloz L., Dupoux A., Cartier J.;
RT "IAPs: more than just inhibitors of apoptosis proteins.";
RL Cell Cycle 7:1036-1046(2008).
RN [10] {ECO:0007744|PDB:6B5B}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.20 ANGSTROMS) IN COMPLEX WITH NLRC4 AND
RP L.PNEUMOPHILA FLAGELLIN, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP 626-ILE-ILE-627; 837-GLN-THR-838; 839-PHE-LEU-840; 841-TRP-PHE-842;
RP 843-GLN-PHE-844; GLY-847; 848-LEU-TRP-849; 974-TYR-GLU-975 AND
RP 1329-CYS-ARG-1330.
RX PubMed=29146805; DOI=10.1126/science.aao1140;
RA Tenthorey J.L., Haloupek N., Lopez-Blanco J.R., Grob P., Adamson E.,
RA Hartenian E., Lind N.A., Bourgeois N.M., Chacon P., Nogales E., Vance R.E.;
RT "The structural basis of flagellin detection by NAIP5: A strategy to limit
RT pathogen immune evasion.";
RL Science 358:888-893(2017).
RN [11] {ECO:0007744|PDB:5YUD}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.28 ANGSTROMS) IN COMPLEX WITH ATP AND
RP S.TYPHIMURIUM FLAGELLIN, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP 1-MET--GLU-40; ARG-11; ILE-15; 106-GLY--SER-108; LEU-840; PHE-844; GLY-847;
RP SER-857 AND 1390-PHE--GLU-1403.
RX PubMed=29182158; DOI=10.1038/cr.2017.148;
RA Yang X., Yang F., Wang W., Lin G., Hu Z., Han Z., Qi Y., Zhang L., Wang J.,
RA Sui S.F., Chai J.;
RT "Structural basis for specific flagellin recognition by the NLR protein
RT NAIP5.";
RL Cell Res. 28:35-47(2018).
CC -!- FUNCTION: Sensor component of the NLRC4 inflammasome that specifically
CC recognizes and binds flagellin from pathogenic bacteria such as
CC Legionella or Salmonella (PubMed:12526741, PubMed:21874021,
CC PubMed:21918512, PubMed:29146805, PubMed:29182158). Association of
CC pathogenic bacteria proteins drives in turn drive assembly and
CC activation of the NLRC4 inflammasome, promoting caspase-1 activation,
CC cytokine production and macrophage pyroptosis (PubMed:21874021,
CC PubMed:21918512, PubMed:29146805, PubMed:29182158). The NLRC4
CC inflammasome is activated as part of the innate immune response to a
CC range of intracellular bacteria. The NLRC4 inflammasome senses Gram-
CC negative bacteria such as L.pneumophila and P.aeruginosa, enteric
CC pathogens S.typhimurium (Salmonella) and S.flexneri (PubMed:21874021,
CC PubMed:21918512, PubMed:29146805, PubMed:29182158). May contribute to
CC prevent motor-neuron apoptosis induced by a variety of signals (By
CC similarity). {ECO:0000250|UniProtKB:Q13075,
CC ECO:0000269|PubMed:12526741, ECO:0000269|PubMed:21874021,
CC ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29146805,
CC ECO:0000269|PubMed:29182158}.
CC -!- SUBUNIT: Component of the NLRC4 inflammasome, at least composed of
CC NLRC4, caspase-1 (CASP1) and some NAIP protein. Flagellin binding by
CC NAIP5 triggers assembly of the inflammasome, a huge complex that
CC contains a single NAIP5 chain and multiple copies of NLRC4
CC (PubMed:29182158). {ECO:0000269|PubMed:21874021,
CC ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29146805,
CC ECO:0000269|PubMed:29182158}.
CC -!- SUBUNIT: (Microbial infection) Interacts with S.typhimurium
CC (Salmonella) flagellin. {ECO:0000269|PubMed:21874021,
CC ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29182158}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila flagellin.
CC {ECO:0000269|PubMed:29146805}.
CC -!- INTERACTION:
CC Q9R016; Q3UP24: Nlrc4; NbExp=18; IntAct=EBI-15944130, EBI-16006652;
CC Q9R016; Q48824: flaA; Xeno; NbExp=2; IntAct=EBI-15944130, EBI-15944232;
CC Q9R016; P06179: fliC; Xeno; NbExp=9; IntAct=EBI-15944130, EBI-2011501;
CC -!- TISSUE SPECIFICITY: Detected in macrophages (at protein level).
CC {ECO:0000269|PubMed:12526741}.
CC -!- POLYMORPHISM: Part of the Lgn1 locus that determines susceptibility to
CC the intracellular pathogen L.pneumophila. Susceptibility differs
CC between inbred mouse strains. Strain C57BL/6J is not permissive, i.e.
CC L.pneumophila cannot multiply in C57BL/6J macrophages, contrary to the
CC situation in mouse strain A/J. Strain FVB/NJ macrophages display
CC intermediate permissiveness for intracellular proliferation of
CC L.pneumophila. {ECO:0000269|PubMed:12526741}.
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; AF135492; AAD56764.1; -; mRNA.
DR EMBL; AF131205; AAD56760.1; -; Genomic_DNA.
DR EMBL; AY146999; AAN60211.1; -; mRNA.
DR EMBL; CT009518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC070433; AAH70433.1; -; mRNA.
DR EMBL; U66326; AAC52974.1; -; Genomic_DNA.
DR CCDS; CCDS26727.1; -.
DR RefSeq; NP_035000.2; NM_010870.2.
DR RefSeq; XP_011242930.1; XM_011244628.1.
DR RefSeq; XP_017170904.1; XM_017315415.1.
DR PDB; 5YUD; EM; 4.28 A; A=1-1403.
DR PDB; 6B5B; EM; 5.20 A; A=1-1403.
DR PDBsum; 5YUD; -.
DR PDBsum; 6B5B; -.
DR AlphaFoldDB; Q9R016; -.
DR SMR; Q9R016; -.
DR DIP; DIP-59148N; -.
DR IntAct; Q9R016; 8.
DR STRING; 10090.ENSMUSP00000058611; -.
DR MEROPS; I32.001; -.
DR iPTMnet; Q9R016; -.
DR PhosphoSitePlus; Q9R016; -.
DR MaxQB; Q9R016; -.
DR PaxDb; Q9R016; -.
DR PRIDE; Q9R016; -.
DR ProteomicsDB; 273675; -.
DR ProteomicsDB; 344822; -.
DR DNASU; 17951; -.
DR Ensembl; ENSMUST00000049789; ENSMUSP00000058611; ENSMUSG00000071203.
DR GeneID; 17951; -.
DR KEGG; mmu:17951; -.
DR UCSC; uc007rql.1; mouse.
DR CTD; 17951; -.
DR MGI; MGI:1298220; Naip5.
DR VEuPathDB; HostDB:ENSMUSG00000071203; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000163369; -.
DR HOGENOM; CLU_005648_0_0_1; -.
DR InParanoid; Q9R016; -.
DR OMA; ANCASEG; -.
DR OrthoDB; 268914at2759; -.
DR PhylomeDB; Q9R016; -.
DR TreeFam; TF105356; -.
DR BioGRID-ORCS; 17951; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Naip5; mouse.
DR PRO; PR:Q9R016; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9R016; protein.
DR Bgee; ENSMUSG00000071203; Expressed in intestinal villus and 77 other tissues.
DR GO; GO:0072557; C:IPAF inflammasome complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR GO; GO:0035635; P:entry of bacterium into host cell; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR CDD; cd00022; BIR; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR028789; Naip.
DR InterPro; IPR040535; NLRC4_HD.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46914; PTHR46914; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17889; NLRC4_HD; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SMART; SM00238; BIR; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; ATP-binding; Immunity; Inflammatory response;
KW Innate immunity; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..1403
FT /note="Baculoviral IAP repeat-containing protein 1e"
FT /id="PRO_0000122344"
FT REPEAT 60..127
FT /note="BIR 1"
FT REPEAT 159..227
FT /note="BIR 2"
FT REPEAT 278..345
FT /note="BIR 3"
FT DOMAIN 464..759
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 473..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:29182158,
FT ECO:0007744|PDB:5YUD"
FT MUTAGEN 1..40
FT /note="Missing: Abolishes production of IL1B in response to
FT bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 11
FT /note="R->I: Strongly reduces production of IL1B in
FT response to bacterial flagellin; then associated with F-
FT 15."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 15
FT /note="I->F: Strongly reduces production of IL1B in
FT response to bacterial flagellin; then associated with I-
FT 11."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 106..108
FT /note="GNS->STR: Strongly reduces production of IL1B in
FT response to bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 626..627
FT /note="II->AA: Strongly reduced interaction with
FT flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 837..838
FT /note="QT->AA: Mildly reduced interaction with flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 839..840
FT /note="FL->AA: Mildly reduced interaction with flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 840
FT /note="L->R: Strongly reduces production of IL1B in
FT response to bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 841..842
FT /note="WF->AA: Mildly reduced interaction with flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 843..844
FT /note="QF->AA: Strongly reduced interaction with
FT flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 844
FT /note="F->C: Strongly reduces production of IL1B in
FT response to bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 847
FT /note="G->E: Strongly reduces production of IL1B in
FT response to bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 847
FT /note="G->K: Nearly abolishes interaction with flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 848..849
FT /note="LW->AA: Strongly reduced interaction with
FT flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 857
FT /note="S->Y: No effect on production of IL1B in response to
FT bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT MUTAGEN 974..975
FT /note="YE->AA: Strongly reduced interaction with
FT flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 1329..1330
FT /note="CR->AA: Reduced interaction with flagellin."
FT /evidence="ECO:0000269|PubMed:29146805"
FT MUTAGEN 1390..1403
FT /note="Missing: Abolishes production of IL1B in response to
FT bacterial flagellin."
FT /evidence="ECO:0000269|PubMed:29182158"
FT CONFLICT 92
FT /note="R -> K (in Ref. 2; AAD56760 and 6; AAC52974)"
FT CONFLICT 144
FT /note="R -> S (in Ref. 2; AAD56760 and 6; AAC52974)"
FT CONFLICT 242
FT /note="S -> G (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="T -> A (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="A -> D (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="A -> T (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="V -> A (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> I (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="E -> D (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116
FT /note="N -> D (in Ref. 1; AAD56764 and 2; AAD56760)"
FT CONFLICT 1123
FT /note="R -> G (in Ref. 1; AAD56764 and 2; AAD56760)"
FT CONFLICT 1129
FT /note="L -> H (in Ref. 1; AAD56764)"
FT CONFLICT 1137
FT /note="Q -> R (in Ref. 1; AAD56764)"
FT CONFLICT 1242
FT /note="V -> I (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="D -> N (in Ref. 2; AAD56760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 159839 MW; 04C04877908103EE CRC64;
MAEHGESSED RISEIDYEFL PELSALLGVD AFQVAKSQEE EEHKERMKMK KGFNSQMRSE
AKRLKTFETY DTFRSWTPQE MAAAGFYHTG VRLGVQCFCC SLILFGNSLR KLPIERHKKL
RPECEFLQGK DVGNIGKYDI RVKRPEKMLR GGKARYHEEE ARLESFEDWP FYAHGTSPRV
LSAAGFVFTG KRDTVQCFSC GGSLGNWEEG DDPWKEHAKW FPKCEFLQSK KSSEEIAQYI
QSYEGFVHVT GEHFVKSWVR RELPMVSAYC NDSVFANEEL RMDMFKDWPQ ESPVGVEALV
RAGFFYTGKK DIVRCFSCGG CLEKWAEGDD PMEDHIKFFP ECVFLQTLKS SAEVIPTLQS
QYALPEATET TRESNHGDAA AVHSTVVDLG RSEAQWFQEA RSLSEQLRDN YTKATFRHMN
LPEVCSSLGT DHLLSCDVSI ISKHISQPVQ EALTIPEVFS NLNSVMCVEG ETGSGKTTFL
KRIAFLWASG CCPLLYRFQL VFYLSLSSIT PDQGLANIIC AQLLGAGGCI SEVCLSSSIQ
QLQHQVLFLL DDYSGLASLP QALHTLITKN YLSRTCLLIA VHTNRVRDIR LYLGTSLEIQ
EFPFYNTVSV LRKFFSHDII CVEKLIIYFI DNKDLQGVYK TPLFVAAVCT DWIQNASAQD
KFQDVTLFQS YMQYLSLKYK ATAEPLQATV SSCGQLALTG LFSSCFEFNS DDLAEAGVDE
DEKLTTLLMS KFTAQRLRPV YRFLGPLFQE FLAAVRLTEL LSSDRQEDQD LGLYYLRQID
SPLKAINSFN IFLYYVSSHS SSKAAPTVVS HLLQLVDEKE SLENMSENED YMKLHPQTFL
WFQFVRGLWL VSPESSSSFV SEHLLRLALI FAYESNTVAE CSPFILQFLR GKTLALRVLN
LQYFRDHPES LLLLRSLKVS INGNKMSSYV DYSFKTYFEN LQPPAIDEEY TSAFEHISEW
RRNFAQDEEI IKNYENIRPR ALPDISEGYW KLSPKPCKIP KLEVQVNNTD AADQALLQVL
MEVFSASQSI EFRLFNSSGF LESICPALEL SKASVTKCSM SRLELSRAEQ ELLLTLPALQ
SLEVSETNQL PEQLFHNLHK FLGLKELCVR LDGKPNVLSV LPREFPNLLH MEKLSIQTST
ESDLSKLVKF IQNFPNLHVF HLKCDFLSNC ESLMAVLASC KKLREIEFSG RCFEAMTFVN
ILPNFVSLKI LNLKDQQFPD KETSEKFAQA LGSLRNLEEL LVPTGDGIHQ VAKLIVRQCL
QLPCLRVLTF HDILDDDSVI EIARAATSGG FQKLENLDIS MNHKITEEGY RNFFQALDNL
PNLQELNICR NIPGRIQVQA TTVKALGQCV SRLPSLIRLH MLSWLLDEED MKVINDVKER
HPQSKRLIIF WKLIVPFSPV ILE
