NLRC3_MOUSE
ID NLRC3_MOUSE Reviewed; 1064 AA.
AC Q5DU56; A1L3P6; Q3TAB7; Q8BJF4; Q8BV65;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein NLRC3;
GN Name=Nlrc3;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic eye, Spleen, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22863753; DOI=10.1038/ni.2378;
RA Schneider M., Zimmermann A.G., Roberts R.A., Zhang L., Swanson K.V.,
RA Wen H., Davis B.K., Allen I.C., Holl E.K., Ye Z., Rahman A.H., Conti B.J.,
RA Eitas T.K., Koller B.H., Ting J.P.;
RT "The innate immune sensor NLRC3 attenuates Toll-like receptor signaling via
RT modification of the signaling adaptor TRAF6 and transcription factor NF-
RT kappaB.";
RL Nat. Immunol. 13:823-831(2012).
RN [5]
RP FUNCTION, INTERACTION WITH TBK1 AND TMEM173, AND DISRUPTION PHENOTYPE.
RX PubMed=24560620; DOI=10.1016/j.immuni.2014.01.010;
RA Zhang L., Mo J., Swanson K.V., Wen H., Petrucelli A., Gregory S.M.,
RA Zhang Z., Schneider M., Jiang Y., Fitzgerald K.A., Ouyang S., Liu Z.J.,
RA Damania B., Shu H.B., Duncan J.A., Ting J.P.;
RT "NLRC3, a member of the NLR family of proteins, is a negative regulator of
RT innate immune signaling induced by the DNA sensor STING.";
RL Immunity 40:329-341(2014).
RN [6]
RP FUNCTION, INTERACTION WITH PIK3R1/PIK3R2, AND DISRUPTION PHENOTYPE.
RX PubMed=27951586; DOI=10.1038/nature20597;
RA Karki R., Man S.M., Malireddi R.K., Kesavardhana S., Zhu Q., Burton A.R.,
RA Sharma B.R., Qi X., Pelletier S., Vogel P., Rosenstiel P., Kanneganti T.D.;
RT "NLRC3 is an inhibitory sensor of PI3K-mTOR pathways in cancer.";
RL Nature 540:583-587(2016).
CC -!- FUNCTION: Negative regulator of the innate immune response. Attenuates
CC signaling pathways activated by Toll-like receptors (TLRs) and the DNA
CC sensor STING/TMEM173 in response to pathogen-associated molecular
CC patterns, such as intracellular poly(dA:dT), but not poly(I:C), or in
CC response to DNA virus infection, including that of Herpes simplex virus
CC 1 (HSV1) (PubMed:22863753, PubMed:24560620). May affect TLR4 signaling
CC by acting at the level of TRAF6 ubiquitination, decreasing the
CC activating 'Lys-63'-linked ubiquitination and leaving unchanged the
CC degradative 'Lys-48'-linked ubiquitination (PubMed:22863753). Inhibits
CC the PI3K-AKT-mTOR pathway possibly by directly interacting with the
CC posphatidylinositol 3-kinase regulatory subunit p85 (PIK3R1/PIK3R2) and
CC disrupting the association between PIK3R1/PIK3R2 and the catalytic
CC subunit p110 (PIK3CA/PIK3CB/PIK3CD) and reducing PIK3R1/PIK3R2
CC activation. Via its regulation of the PI3K-AKT-mTOR pathway, controls
CC cell proliferation, predominantly in intestinal epithelial cells
CC (PubMed:27951586). May also affect NOD1- or NOD2-mediated NF-kappa-B
CC activation (By similarity). Might also affect the inflammatory response
CC by preventing NLRP3 inflammasome formation, CASP1 cleavage and IL1B
CC maturation (By similarity). {ECO:0000250|UniProtKB:Q7RTR2,
CC ECO:0000269|PubMed:22863753, ECO:0000269|PubMed:24560620,
CC ECO:0000269|PubMed:27951586}.
CC -!- SUBUNIT: Directly interacts (via CARD) with TMEM173/STING; this
CC interaction reduces TMEM173 trafficking to the perinuclear region in
CC response to interferon stimulatory DNA. Also interacts, but to a lesser
CC extent, with TBK1 (PubMed:24560620). Interacts with TRAF6; this
CC interaction results in decreased TRAF6 'Lys-63'-linked
CC polyubiquitination, but leaves 'Lys-48'-linked chains unchanged,
CC promoting TRAF6 protein degradation (By similarity). Interacts with
CC PIK3R1/PIK3R2; this interaction disrupts the association between
CC PIK3R1/PIK3R2 and the p110 catalytic subunit PIK3CA/PIK3CB/PIK3CD and
CC reduces PIK3R1/PIK3R2 activation (PubMed:27951586). Weakly interacts
CC with PYCARD/ASC. Interacts with CASP1 and CASP5 (By similarity).
CC {ECO:0000250|UniProtKB:Q7RTR2, ECO:0000269|PubMed:24560620,
CC ECO:0000269|PubMed:27951586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7RTR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5DU56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DU56-2; Sequence=VSP_027141, VSP_027143, VSP_027145;
CC Name=3;
CC IsoId=Q5DU56-3; Sequence=VSP_027139, VSP_027144;
CC Name=4;
CC IsoId=Q5DU56-4; Sequence=VSP_027139, VSP_027144, VSP_027148,
CC VSP_027149;
CC Name=5;
CC IsoId=Q5DU56-5; Sequence=VSP_027140, VSP_027142, VSP_027146,
CC VSP_027147;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow-derived macrophages.
CC {ECO:0000269|PubMed:22863753}.
CC -!- DOMAIN: The leucine-rich repeat domain may reduce the interaction with
CC TMEM173/STING. {ECO:0000250|UniProtKB:Q7RTR2}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under basal conditions
CC (PubMed:22863753). Mutant mice show an enhanced response to
CC lipopolysaccharide (LPS)-induced endotoxic shock (PubMed:22863753).
CC Herpes simplex virus 1-infected knockout mice exhibit enhanced innate
CC immunity and reduced morbidity and viral load compared to wild-type
CC animals (PubMed:24560620). Mutant mice are hyper-susceptible to
CC colitis-associated colorectal tumorigenesis (PubMed:27951586).
CC {ECO:0000269|PubMed:22863753, ECO:0000269|PubMed:24560620,
CC ECO:0000269|PubMed:27951586}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90390.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220314; BAD90390.1; ALT_INIT; mRNA.
DR EMBL; AK079766; BAC37747.1; -; mRNA.
DR EMBL; AK084199; BAC39136.1; -; mRNA.
DR EMBL; AK171971; BAE42752.1; -; mRNA.
DR EMBL; BC130223; AAI30224.1; -; mRNA.
DR CCDS; CCDS70677.1; -. [Q5DU56-3]
DR RefSeq; NP_780756.1; NM_175547.3. [Q5DU56-3]
DR AlphaFoldDB; Q5DU56; -.
DR SMR; Q5DU56; -.
DR STRING; 10090.ENSMUSP00000137628; -.
DR PhosphoSitePlus; Q5DU56; -.
DR EPD; Q5DU56; -.
DR MaxQB; Q5DU56; -.
DR PaxDb; Q5DU56; -.
DR PRIDE; Q5DU56; -.
DR ProteomicsDB; 252906; -. [Q5DU56-1]
DR ProteomicsDB; 252907; -. [Q5DU56-2]
DR ProteomicsDB; 252908; -. [Q5DU56-3]
DR ProteomicsDB; 252909; -. [Q5DU56-4]
DR ProteomicsDB; 252910; -. [Q5DU56-5]
DR Antibodypedia; 56241; 52 antibodies from 20 providers.
DR DNASU; 268857; -.
DR Ensembl; ENSMUST00000180200; ENSMUSP00000137325; ENSMUSG00000049871. [Q5DU56-3]
DR GeneID; 268857; -.
DR KEGG; mmu:268857; -.
DR UCSC; uc007xzd.1; mouse. [Q5DU56-3]
DR UCSC; uc007xze.1; mouse. [Q5DU56-4]
DR CTD; 197358; -.
DR MGI; MGI:2444070; Nlrc3.
DR VEuPathDB; HostDB:ENSMUSG00000049871; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000159861; -.
DR HOGENOM; CLU_017147_4_1_1; -.
DR InParanoid; Q5DU56; -.
DR OrthoDB; 259987at2759; -.
DR PhylomeDB; Q5DU56; -.
DR BioGRID-ORCS; 268857; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q5DU56; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5DU56; protein.
DR Bgee; ENSMUSG00000049871; Expressed in peripheral lymph node and 96 other tissues.
DR ExpressionAtlas; Q5DU56; baseline and differential.
DR Genevisible; Q5DU56; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IDA:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; IMP:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:CACAO.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:CACAO.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:HGNC.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:CACAO.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; ISS:HGNC.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13516; LRR_6; 9.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Leucine-rich repeat;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1064
FT /note="Protein NLRC3"
FT /id="PRO_0000296188"
FT DOMAIN 138..459
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 338..362
FT /note="LRR 1"
FT REPEAT 570..593
FT /note="LRR 2"
FT REPEAT 632..662
FT /note="LRR 3"
FT REPEAT 664..687
FT /note="LRR 4"
FT REPEAT 692..715
FT /note="LRR 5"
FT REPEAT 720..743
FT /note="LRR 6"
FT REPEAT 748..771
FT /note="LRR 7"
FT REPEAT 776..799
FT /note="LRR 8"
FT REPEAT 804..827
FT /note="LRR 9"
FT REPEAT 832..855
FT /note="LRR 10"
FT REPEAT 860..883
FT /note="LRR 11"
FT REPEAT 888..911
FT /note="LRR 12"
FT REPEAT 916..939
FT /note="LRR 13"
FT REPEAT 972..995
FT /note="LRR 14"
FT REPEAT 1000..1022
FT /note="LRR 15"
FT REPEAT 1028..1051
FT /note="LRR 16"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT VAR_SEQ 1..667
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027139"
FT VAR_SEQ 1..636
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027140"
FT VAR_SEQ 1..27
FT /note="MRRRYSHDPPGSFRETKVFGFRGEYGC -> MQAEPFSTLEQPPWQEGDNIG
FT SPGSVLALYSQLLAANTDSTRKQEVWTDRETCLAYSVGSPAEQV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027141"
FT VAR_SEQ 637..641
FT /note="YCQSL -> MAPLP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027142"
FT VAR_SEQ 643..688
FT /note="LDNNQFQDPVMELLGSVLSGKDCRIRKISLAENQIGNKGAKALARS -> WV
FT WGPCRERAKEKEPLEWFLASSHPFPCSLLRLLEFHSWVLSHHSN (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027143"
FT VAR_SEQ 668..670
FT /note="RKI -> MAG (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027144"
FT VAR_SEQ 689..1064
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027145"
FT VAR_SEQ 841..875
FT /note="RENSISPEGAQALTQALCRNNTLKHLDLTANLLHD -> MSPQPARKLHQPR
FT GSPGPHSSSLQEQHSEALGPDS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027146"
FT VAR_SEQ 876..1064
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027147"
FT VAR_SEQ 979
FT /note="D -> E (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027148"
FT VAR_SEQ 980..1064
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027149"
SQ SEQUENCE 1064 AA; 115993 MW; 00FEB5FEDB6083C0 CRC64;
MRRRYSHDPP GSFRETKVFG FRGEYGCKAL VDLLAGKGSQ LLQVRDKMPD SPLGSQSNES
RIPKHSEALL SRVGNDPELG SPSHRLASLM LVEGLTDLQL KEHDFTQVEA TRGVWHPARV
ITLDRLFLPL SRVSIPPRVS LTIGVAGVGK TTLVRHFVHC WARGQVGKGF SRVLPLTFRD
LNTYEKLSAD RLIQSIFSSI GEASLVATAP DRVLLVLDGL DECKTPLEFS NTMACSDPKK
EIQVDHLITN IIRGNLFPEI SVWITSRPSA AGQIPGGLVD RMTEIRGLTE EEIKVCLEQM
FPEEQNLLGQ VLSQVQANRA LYLMCTVPAF CRLTGLALGH LYRTRLAVQD IELPLPQTLC
ELYSWYFRMA LGGEGQDKEK VSPRIKQVTQ GARKMVGTLG RLAFHGLVKK KYVFYEQDMK
AFGVDLALLQ NTLCSCLLQR EETLASSVAY CFIHLSLQEF VAATYYYSAS KRAIFDLFTE
SGMSWPRLGF LAHFRCAAQR ATQAKDGRLD VFLRFLSGLL SPRVNTLLAG SLLSQGEHQS
YRDQVAEVLQ GFLHPDAAVC ARAINVLYCL SELRHTELAC SVEEAMRSGT LAGMTSPSHR
TALAYLLQMS DICSPEADFS LCLSQHVLQS LLPQLLYCQS LRLDNNQFQD PVMELLGSVL
SGKDCRIRKI SLAENQIGNK GAKALARSLL VNRSLITLDL RSNSIGPPGA KALADALKIN
RTLTSLSLQS NVIKDDGVMC VAEALVSNQT ISMLQLQKNL IGLIGAQQMA DALKQNRSLK
ALMFSSNTIG DRGAIALAEA LKVNQILENL DLQSNSISDM GVTVLMRALC SNQTLSSLNL
RENSISPEGA QALTQALCRN NTLKHLDLTA NLLHDRGAQA IAVAVGENHS LTHLHLQWNF
IQAGAARALG QALQLNRTLT TLDLQENAIG DEGASSVAGA LKVNTTLIAL YLQVASIGSQ
GAQALGEALT VNRTLEILDL RGNDVGAAGA KALANALKLN SSLRRLNLQE NSLGMDGAIF
VASALSENHG LHHINLQGNP IGESAARMIS EAIKTNAPTC TVEI
