XA21_ORYSJ
ID XA21_ORYSJ Reviewed; 1037 AA.
AC Q2R2D5; A0A0P0Y3N4; A0PI95; A3CCH4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Receptor kinase-like protein Xa21 {ECO:0000303|PubMed:22735448};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q1MX30, ECO:0000255|PROSITE-ProRule:PRU00159};
DE Contains:
DE RecName: Full=Receptor kinase-like protein Xa21, processed {ECO:0000303|PubMed:22735448};
DE Flags: Precursor;
GN Name=XA21 {ECO:0000303|PubMed:22735448};
GN OrderedLocusNames=LOC_Os11g36180 {ECO:0000312|EMBL:ABA94328.1},
GN Os11g0569733 {ECO:0000312|EMBL:BAT14519.1};
GN ORFNames=OsJ_34314 {ECO:0000312|EMBL:EAZ18787.1},
GN OSNPB_110569733 {ECO:0000312|EMBL:BAT14519.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-760.
RX PubMed=17112320; DOI=10.1371/journal.pgen.0020199;
RA Tang T., Lu J., Huang J., He J., McCouch S.R., Shen Y., Kai Z.,
RA Purugganan M.D., Shi S., Wu C.-I.;
RT "Genomic variation in rice: genesis of highly polymorphic linkage blocks
RT during domestication.";
RL PLoS Genet. 2:E199-E199(2006).
RN [6]
RP FUNCTION (RECEPTOR KINASE-LIKE PROTEIN XA21), FUNCTION (RECEPTOR
RP KINASE-LIKE PROTEIN XA21, PROCESSED), SUBCELLULAR LOCATION, INTERACTION
RP WITH WRKY62, MUTAGENESIS OF 689-HIS--LYS-694, NUCLEAR LOCALIZATION SIGNAL,
RP AND PROTEOLYTIC PROCESSING.
RX PubMed=22735448; DOI=10.1038/ncomms1932;
RA Park C.J., Ronald P.C.;
RT "Cleavage and nuclear localization of the rice XA21 immune receptor.";
RL Nat. Commun. 3:920-920(2012).
RN [7]
RP INTERACTION WITH SERK2.
RX PubMed=24482436; DOI=10.1093/mp/ssu003;
RA Chen X., Zuo S., Schwessinger B., Chern M., Canlas P.E., Ruan D., Zhou X.,
RA Wang J., Daudi A., Petzold C.J., Heazlewood J.L., Ronald P.C.;
RT "An XA21-associated kinase (OsSERK2) regulates immunity mediated by the
RT XA21 and XA3 immune receptors.";
RL Mol. Plant 7:874-892(2014).
CC -!- FUNCTION: [Receptor kinase-like protein Xa21]: Receptor kinase that
CC detects X.oryzae pv. oryzae protein Ax21 to promote innate immunity.
CC Following X.oryzae pv. oryzae protein Ax21 detection, undergoes
CC cleavage, releasing the processed protein kinase Xa21 chain.
CC {ECO:0000269|PubMed:22735448}.
CC -!- FUNCTION: [Receptor kinase-like protein Xa21, processed]: The processed
CC protein kinase Xa21 chain released by protein cleavage after X.oryzae
CC pv. oryzae protein Ax21 detection translocates into the nucleus where
CC it can bind and regulate WRKY62, a transcription factor. Confers
CC resistance to the bacterial pathogen X.oryzae pv. oryzae (Xoo).
CC {ECO:0000269|PubMed:22735448}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q1MX30};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX30};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q1MX30};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q1MX30};
CC Note=Enzymatic activity is fifteen time stronger with Mn(2+) than with
CC Mg(2+). {ECO:0000250|UniProtKB:Q1MX30};
CC -!- SUBUNIT: [Receptor kinase-like protein Xa21, processed]: Interacts with
CC WRKY62/XB10 in the nucleus (PubMed:22735448). Interacts with SERK2
CC (PubMed:24482436). {ECO:0000269|PubMed:22735448,
CC ECO:0000269|PubMed:24482436}.
CC -!- SUBCELLULAR LOCATION: [Receptor kinase-like protein Xa21]: Cell
CC membrane {ECO:0000269|PubMed:22735448}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22735448}; Single-pass membrane protein
CC {ECO:0000255}. Note=Present in cortical and perinuclear endoplasmic
CC reticulum. Cleaved upon X.oryzae pv. oryzae protein Ax21 recognition;
CC the kinase containing fragment is translocated into the nucleus.
CC {ECO:0000269|PubMed:22735448}.
CC -!- SUBCELLULAR LOCATION: [Receptor kinase-like protein Xa21, processed]:
CC Nucleus {ECO:0000269|PubMed:22735448}.
CC -!- PTM: Undergoes protein cleavage upon X.oryzae pv. oryzae protein Ax21
CC detection, thus releasing the processed protein kinase Xa21 chain.
CC {ECO:0000269|PubMed:22735448}.
CC -!- PTM: Autophosphorylated on serine and threonine residues; these
CC phosphorylation prevents proteolytic degradation.
CC {ECO:0000250|UniProtKB:Q1MX30}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT14519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAZ18787.1; Type=Erroneous gene model prediction; Evidence={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; DP000010; ABA94328.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT14519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000148; EAZ18787.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY885781; AAY32490.1; -; Genomic_DNA.
DR EMBL; AY885775; AAY32484.1; -; Genomic_DNA.
DR EMBL; AY885776; AAY32485.1; -; Genomic_DNA.
DR EMBL; AY885777; AAY32486.1; -; Genomic_DNA.
DR EMBL; AY885778; AAY32487.1; -; Genomic_DNA.
DR EMBL; AY885779; AAY32488.1; -; Genomic_DNA.
DR EMBL; AY885780; AAY32489.1; -; Genomic_DNA.
DR RefSeq; XP_015616297.1; XM_015760811.1.
DR AlphaFoldDB; Q2R2D5; -.
DR SMR; Q2R2D5; -.
DR STRING; 4530.OS11T0569733-00; -.
DR PRIDE; Q2R2D5; -.
DR GeneID; 107276510; -.
DR KEGG; osa:107276510; -.
DR HOGENOM; CLU_000288_22_0_1; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 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 membrane; Endoplasmic reticulum; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1037
FT /note="Receptor kinase-like protein Xa21"
FT /id="PRO_5004214548"
FT CHAIN ?..1037
FT /note="Receptor kinase-like protein Xa21, processed"
FT /id="PRO_0000436962"
FT TOPO_DOM 25..665
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 89..112
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 113..137
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 138..161
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 163..185
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 187..210
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 211..234
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 236..259
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 260..283
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 285..308
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 310..331
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 333..355
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 362..385
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 387..411
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 412..435
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 437..459
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 460..482
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 483..507
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 509..532
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 533..556
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 557..580
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 581..604
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 606..629
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 720..1019
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 689..694
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22735448"
FT ACT_SITE 854
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 726..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1MX30"
FT MOD_RES 700
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q1MX30"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1MX30"
FT MOD_RES 717
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q1MX30"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 689..694
FT /note="HKRTKK->AAATAA: Impaired nuclear localization."
FT /evidence="ECO:0000269|PubMed:22735448"
SQ SEQUENCE 1037 AA; 112106 MW; 8918581636B45DBB CRC64;
MARSPTSVMI SSLLLLLLIG PASSDDAAAA AAARTSTGGV AGDELALLSF KSSLLHQGGL
SLASWNTSGH GQHCTWVGVV CGRRRRRHPH RVVKLLLRSS NLSGIISPSL GNLSFLRELD
LSDNYLSGEI PPELSRLSRL QLLELSGNSI QGSIPAAIGA CTKLTSLDLS HNQLRGMIPR
EIGASLKHLS NLYLHTNGLS GEIPSALGNL TSLQYFDLSC NRLSGAIPSS LGQLSSSLLT
MNLRQNNLSG MIPNSIWNLS SLRAFSVSEN KLGGMIPTNA FKTLHLLEVI DMGTNRFYGK
IPASVANASH LTQLQIDGNL FSGIITSGFG RLRNLTTLYL WRNLFQTREQ EDWGFISDLT
NCSKLQTLDL GENNLGGVLP NSFSNLSTSL SFLALDLNKI TGSIPKDIGN LIGLQHLYLC
NNNFRGSLPS SLGRLRNLGI LVAYENNLSG SIPLAIGNLT ELNILLLGTN KFSGWIPYTL
SNLTNLLSLG LSTNNLSGPI PSELFNIQTL SIMINVSKNN LEGSIPQEIG HLKNLVEFHA
ESNRLSGKIP NTLGDCQLLR YLYLQNNLLS GSIPSALGQL KGLETLDLSS NNLSGQIPTS
LADITMLHSL NLSFNSFMGE VPTIGAFADA SGISIQGNAK LCGGIPDLHL PRCCPLLENR
KHFPVLPISV SLVAALAILS SLYLLITWHK RTKKGAPSRT SMKGHPLVSY SQLVKATDGF
APTNLLGSGS FGSVYKGKLN IQDHVAVKVL KLENPKALKS FTAECEALRN MRHRNLVKIV
TICSSIDNRG NDFKAIVYDF MPSGSLEDWI HPETNDPADQ RHLNLHRRVT ILLDVACALD
YLHRHGPEPV VHCDVKSSNV LLDSDMVAHV GDFGLARILV DGTSLIQQST SSMGFRGTIG
YAAPEYGVGH IASTHGDIYS YGILVLEIVT GKRPTDSTFR PDLGLRQYVE LGLHGRVTDV
VDTKLILDSE NWLNSTNNSP CRRITECIVS LLRLGLSCSQ VLPLSRTPTG DIIDELNAIK
QNLSGLFPVC EGASLEF
