NSY1_CAEEL
ID NSY1_CAEEL Reviewed; 1498 AA.
AC Q21029;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase nsy-1 {ECO:0000305};
DE EC=2.7.11.25 {ECO:0000269|PubMed:11336672, ECO:0000269|PubMed:11751572};
DE AltName: Full=Apoptosis signal-regulating kinase 1 {ECO:0000303|PubMed:11336672};
DE Short=ASK-1 {ECO:0000303|PubMed:11336672};
DE AltName: Full=Neuronal symmetry kinase 1 {ECO:0000312|WormBase:F59A6.1a};
GN Name=nsy-1 {ECO:0000312|WormBase:F59A6.1a};
GN ORFNames=F59A6.1 {ECO:0000312|WormBase:F59A6.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12142542; DOI=10.1126/science.1073759;
RA Kim D.H., Feinbaum R., Alloing G., Emerson F.E., Garsin D.A., Inoue H.,
RA Tanaka-Hino M., Hisamoto N., Matsumoto K., Tan M.-W., Ausubel F.M.;
RT "A conserved p38 MAP kinase pathway in Caenorhabditis elegans innate
RT immunity.";
RL Science 297:623-626(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UNC-43, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF LYS-693.
RX PubMed=11336672; DOI=10.1016/s0092-8674(01)00313-0;
RA Sagasti A., Hisamoto N., Hyodo J., Tanaka-Hino M., Matsumoto K.,
RA Bargmann C.I.;
RT "The CaMKII UNC-43 activates the MAPKKK NSY-1 to execute a lateral
RT signaling decision required for asymmetric olfactory neuron fates.";
RL Cell 105:221-232(2001).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SEK-1, AND
RP MUTAGENESIS OF LYS-693.
RX PubMed=11751572; DOI=10.1093/embo-reports/kvf001;
RA Tanaka-Hino M., Sagasti A., Hisamoto N., Kawasaki M., Nakano S.,
RA Ninomiya-Tsuji J., Bargmann C.I., Matsumoto K.;
RT "SEK-1 MAPKK mediates Ca2+ signaling to determine neuronal asymmetric
RT development in Caenorhabditis elegans.";
RL EMBO Rep. 3:56-62(2002).
RN [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15625192; DOI=10.1101/gad.1276505;
RA Chuang C.-F., Bargmann C.I.;
RT "A Toll-interleukin 1 repeat protein at the synapse specifies asymmetric
RT odorant receptor expression via ASK1 MAPKKK signaling.";
RL Genes Dev. 19:270-281(2005).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=15888317; DOI=10.1016/j.mad.2004.11.012;
RA Kondo M., Yanase S., Ishii T., Hartman P.S., Matsumoto K., Ishii N.;
RT "The p38 signal transduction pathway participates in the oxidative stress-
RT mediated translocation of DAF-16 to Caenorhabditis elegans nuclei.";
RL Mech. Ageing Dev. 126:642-647(2005).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=18394898; DOI=10.1016/j.cub.2008.02.079;
RA Pujol N., Cypowyj S., Ziegler K., Millet A., Astrain A., Goncharov A.,
RA Jin Y., Chisholm A.D., Ewbank J.J.;
RT "Distinct innate immune responses to infection and wounding in the C.
RT elegans epidermis.";
RL Curr. Biol. 18:481-489(2008).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=19497412; DOI=10.1016/j.cbi.2009.03.012;
RA Wang S., Wu L., Wang Y., Luo X., Lu Y.;
RT "Copper-induced germline apoptosis in Caenorhabditis elegans: the
RT independent roles of DNA damage response signaling and the dependent roles
RT of MAPK cascades.";
RL Chem. Biol. Interact. 180:151-157(2009).
RN [9]
RP FUNCTION.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21212236; DOI=10.1534/genetics.110.124883;
RA Hayakawa T., Kato K., Hayakawa R., Hisamoto N., Matsumoto K., Takeda K.,
RA Ichijo H.;
RT "Regulation of anoxic death in Caenorhabditis elegans by mammalian
RT apoptosis signal-regulating kinase (ASK) family proteins.";
RL Genetics 187:785-792(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
RA Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
RT "Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1
RT activity via p38 MAPK signaling during infection in C. elegans.";
RL PLoS Pathog. 7:E1002453-E1002453(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22308034; DOI=10.1074/jbc.m111.314146;
RA Lee K., Shim J., Bae J., Kim Y.J., Lee J.;
RT "Stabilization of RNT-1 protein, runt-related transcription factor (RUNX)
RT protein homolog of Caenorhabditis elegans, by oxidative stress through
RT mitogen-activated protein kinase pathway.";
RL J. Biol. Chem. 287:10444-10452(2012).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF 1003-GLN--ASN-1498.
RX PubMed=25204677; DOI=10.1186/s12915-014-0064-6;
RA Crook-McMahon H.M., Olahova M., Button E.L., Winter J.J., Veal E.A.;
RT "Genome-wide screening identifies new genes required for stress-induced
RT phase 2 detoxification gene expression in animals.";
RL BMC Biol. 12:64-64(2014).
RN [14]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=24448648; DOI=10.1126/scisignal.2004822;
RA Maruyama T., Araki T., Kawarazaki Y., Naguro I., Heynen S., Aza-Blanc P.,
RA Ronai Z., Matsuzawa A., Ichijo H.;
RT "Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate
RT stress responses.";
RL Sci. Signal. 7:RA8-RA8(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase which, by phosphorylating and
CC activating sek-1, plays an important role in the activation of the p38
CC pathway also composed of the downstream effectors sek-1 and pmk-1
CC (PubMed:11751572, PubMed:12142542, PubMed:21212236, PubMed:24448648).
CC Downstream of CaMKII unc-43 and adapter protein tir-1, plays a role in
CC determining asymmetric cell fates in olfactory AWC neurons during
CC neuronal development. Activation results in the repression of odorant
CC receptor str-2 expression in one of the 2 AWC neurons (PubMed:11336672,
CC PubMed:11751572, PubMed:15625192). Involved in resistance to pathogenic
CC Gram-positive and Gram-negative bacterial and fungal infection
CC (PubMed:12142542, PubMed:18394898, PubMed:24448648). Involved in
CC resistance to the nematotoxic C.cinerea galectin Cgl2
CC (PubMed:20062796). Probably by activating the sek1/pmk-1/skn-1 pathway,
CC involved in the up-regulation of gcs-1 and glutathione-S-transferase
CC gst-4 expression upon bacterial infection (PubMed:22216003). Probably
CC downstream of tir-1 and nipi-3, required for the expression of
CC antimicrobial peptide nlp-29 in the epidermis in response to fungal
CC infection or physical injury (PubMed:18394898). Plays a role in
CC resistance to several environmental stresses including oxidative,
CC protein misfolding (ER) and osmotic stresses, and DNA-damaging reagents
CC (PubMed:21212236, PubMed:15888317). Plays a role in the stabilization
CC of transcription factor rnt-1 in the intestine during oxidative stress
CC (PubMed:22308034). Involved in germline apoptosis induced by heavy
CC metals, such as Cu(2+) (PubMed:19497412). In addition, plays a role in
CC the up-regulation of gcs-1 upon arsenite treatment, most likely through
CC activation of pmk-1, to confer protection against toxicity induced by
CC heavy metals (PubMed:25204677). Plays a role downstream of tir-1 in
CC regulating susceptibility to anoxia (PubMed:21212236). Involved in egg
CC laying (PubMed:12142542). {ECO:0000269|PubMed:11336672,
CC ECO:0000269|PubMed:11751572, ECO:0000269|PubMed:12142542,
CC ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:15888317,
CC ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:19497412,
CC ECO:0000269|PubMed:20062796, ECO:0000269|PubMed:21212236,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22308034,
CC ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:25204677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000269|PubMed:11336672, ECO:0000269|PubMed:11751572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.25; Evidence={ECO:0000269|PubMed:11336672,
CC ECO:0000269|PubMed:11751572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11751572};
CC -!- SUBUNIT: Interacts with unc-43 (PubMed:11336672). Interacts with sek-1
CC (PubMed:11751572). {ECO:0000269|PubMed:11336672,
CC ECO:0000269|PubMed:11751572}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:15625192}. Perikaryon
CC {ECO:0000269|PubMed:15625192}. Note=Localizes to post-synaptic regions
CC and is enriched in punctate structures in AWC neuron axon where co-
CC localizes with tir-1. Localization is regulated by tir-1.
CC {ECO:0000269|PubMed:15625192}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, hypodermis, rectal gland
CC cell and neurons including sensory AWC neurons.
CC {ECO:0000269|PubMed:11336672}.
CC -!- PTM: May be phosphorylated upon pathogenic bacterial infection. May be
CC regulated by proteosomal degradation mediated by the E3-ubiquitin
CC ligase rle-1. {ECO:0000269|PubMed:24448648}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an increase in
CC survival rate in anoxic conditions (PubMed:21212236). Upon infection by
CC P.aeruginosa and E.faecalis, RNAi-mediated knockdown results in a
CC moderate reduction in the up-regulation of gst-4 and gcs-1 expression
CC (PubMed:22216003). Causes a severe reduction in rnt-1 accumulation in
CC the intestine during oxidative stress mediated by paraquat
CC (PubMed:22308034). {ECO:0000269|PubMed:21212236,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22308034}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284602; CCD70472.1; -; Genomic_DNA.
DR RefSeq; NP_001293513.1; NM_001306584.1.
DR AlphaFoldDB; Q21029; -.
DR SMR; Q21029; -.
DR IntAct; Q21029; 1.
DR STRING; 6239.F59A6.1; -.
DR EPD; Q21029; -.
DR PaxDb; Q21029; -.
DR PeptideAtlas; Q21029; -.
DR PRIDE; Q21029; -.
DR EnsemblMetazoa; F59A6.1a.1; F59A6.1a.1; WBGene00003822.
DR UCSC; F59A6.1; c. elegans.
DR WormBase; F59A6.1a; CE44901; WBGene00003822; nsy-1.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000171895; -.
DR HOGENOM; CLU_003687_1_1_1; -.
DR InParanoid; Q21029; -.
DR OMA; HIRGGMV; -.
DR OrthoDB; 226722at2759; -.
DR PhylomeDB; Q21029; -.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR SignaLink; Q21029; -.
DR PRO; PR:Q21029; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003822; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q21029; baseline and differential.
DR GO; GO:1904115; C:axon cytoplasm; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0045165; P:cell fate commitment; IMP:WormBase.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0000165; P:MAPK cascade; IGI:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:UniProtKB.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:WormBase.
DR GO; GO:1902097; P:positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0093002; P:response to nematicide; TAS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Coiled coil; Kinase; Magnesium;
KW Metal-binding; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..1498
FT /note="Mitogen-activated protein kinase kinase kinase nsy-
FT 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433800"
FT DOMAIN 664..925
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1276..1314
FT /evidence="ECO:0000255"
FT COMPBIAS 1027..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 790
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 670..678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 693
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:11336672,
FT ECO:0000269|PubMed:11751572"
FT MUTAGEN 1003..1498
FT /note="Missing: In ag3; reduces survival and reduces pmk-1
FT phosphorylation in response to the heavy metal arsenite."
FT /evidence="ECO:0000269|PubMed:25204677"
SQ SEQUENCE 1498 AA; 169654 MW; 751756B7483CDA2C CRC64;
MSQNNKRQVQ HNHEMSNDVC PLPLPPRGAP PPTAYHASRM AATSSSTNGS FEKSAIPGNA
RKLHVVIVID QKVQKNLRVR EMALKDVQKV ADTLNVNLTR IDFDKLDFGE TETLDLFYNA
DVALVDVTVT HQQPSLCYHI GVRESMGQSY NMILTYWSPD PEYHIMDALK KTHAHLPMIV
YIHHQDSNQL QSYDKNNNDD DSKPPFARTN VPAKTITFQH RMKQVLKSVQ VEASAHSREK
FMSDLRKARE ITDGDQKNDY LDKMRTRLDN PDVLHPDTVS LMMLSYRDNQ NYGGMIRLVD
DLKRIPDCLK VVDTPVIRYQ YAFALNRRNK DGDRDLALNT VLSLVEGTTE NEEKNGPLSP
DVVCLAGRIY KDKFIASNYE DRESLNSAIE WYRRAFEMSP LEYSGINLTT LLRASGEHFE
NNLEMQQIAV VLNSLLGRKG ALQNLMEYWD VATYFEVSVL AENYQKACEA ALMMVKLKPP
VWYLKSTMEN IKLINRCAAT ISPIEKEKQQ FLFWSEFFME ATEADTDISC PRYPVLILEL
NKEFTPSYLT LNNEEGTVIL SHVLENSQQK KIHQSELRGI HRWHFARNNI KAVTESKRDD
RQLFLYVHEN SDDFNLLFPT KAHCKKAYDD MKSMADVADG NYQGRVLSNP DNEKIRFEYE
LSNSNERVVL GKGTYGTVYA ARDMDTQRQI VVKEIEVKYD EEVQPLMEEI SLHSTLCHAN
IVQYLGCDLV GKDGSNDHFL IFMEHVPGGS LSSLLRSKWG PMNENAMNYY GKQILEGLKY
LHELKIVHRD IKGDNVLVNT YSGVCKISDF GTCKRLAGLN PVTETFTGTL QYMAPEVIDH
GQRGYGAPAD IWSFGCTMVE MATGRPPFVE MQNPQAAMFR VGMFKTHPPI PTEITEKCRN
FIKSCFLPEA CDRPSAKDLL QDPFIYHNHH SISRTRSGSI NKKPATKIEL NHDKEKKEKS
KNQREMLRST SHIGGMGVVE RSPPTPEPMS ATLTAGFSHV HSQTVSNALS TAREEKKLHL
KIDHARNRTF SSSSPVPDGQ SSAGTNMSHP GFQLSQPSSP IVDDTNHPHL IVSPISLNTM
GSPLSSAALL NRTISDESSN SSSRFFMLQK DSERRRSLGQ FMQDYKDLII DSWSTLLIKQ
SDTELVVTVY MLEMLLDGMR DFLLKKDNTK MQKMIDDIRG LLDYDTAKIG QINLALYHFS
DSIQPVLRRL DIKPHWMFAL SNLITSAVQC AISILSPDLS LLLHAQDNLP STSSIVAIRN
SSLSEGEALI ESRPPSREER VREDRKELRT LQEENEILIE RLLQVERELN AQLKSGITRA
NRFRDFAMYR NTYPPFRTPP VAHAPPTPPF SASCGAQPSG TFTNQPPSFA SIKPIAQKII
MPPGTENNYQ VTRVQEELVS WLRGLEIDER SIALIASEAY TKSDMMDFVT RDELLSIGVG
GGSSCRIMRA IGEVRERQRR QPVFLSPMRS RDDSLDDYHS SSADDMYTGA AAETSSGN
