PSYR1_ARATH
ID PSYR1_ARATH Reviewed; 1095 AA.
AC Q9C7S5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Tyrosine-sulfated glycopeptide receptor 1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PSY1 receptor {ECO:0000303|PubMed:23062058};
GN Name=PSY1R {ECO:0000303|PubMed:23062058}; Synonyms=PSYR1 {ECO:0000305};
GN OrderedLocusNames=At1g72300 {ECO:0000312|Araport:AT1G72300};
GN ORFNames=T9N14.20 {ECO:0000312|EMBL:AAG51803.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17989228; DOI=10.1073/pnas.0706403104;
RA Amano Y., Tsubouchi H., Shinohara H., Ogawa M., Matsubayashi Y.;
RT "Tyrosine-sulfated glycopeptide involved in cellular proliferation and
RT expansion in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18333-18338(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23062058; DOI=10.1111/tpj.12050;
RA Mosher S., Seybold H., Rodriguez P., Stahl M., Davies K.A., Dayaratne S.,
RA Morillo S.A., Wierzba M., Favery B., Keller H., Tax F.E., Kemmerling B.;
RT "The tyrosine-sulfated peptide receptors PSKR1 and PSY1R modify the
RT immunity of Arabidopsis to biotrophic and necrotrophic pathogens in an
RT antagonistic manner.";
RL Plant J. 73:469-482(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH AHA1 AND AHA2, SUBUNIT,
RP SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP 1072-ASP--THR-1095.
RX PubMed=25267325; DOI=10.1111/tpj.12680;
RA Fuglsang A.T., Kristensen A., Cuin T.A., Schulze W.X., Persson J.,
RA Thuesen K.H., Ytting C.K., Oehlenschlaeger C.B., Mahmood K.,
RA Sondergaard T.E., Shabala S., Palmgren M.G.;
RT "Receptor kinase-mediated control of primary active proton pumping at the
RT plasma membrane.";
RL Plant J. 80:951-964(2014).
CC -!- FUNCTION: Tyrosine-sulfated glycopeptide receptor with a
CC serine/threonine-protein kinase activity (PubMed:17989228,
CC PubMed:25267325). Regulates, in response to tyrosine-sulfated
CC glycopeptide binding, a signaling cascade involved in cellular
CC proliferation and plant growth (PubMed:17989228). Not involved in PSK
CC perception (PubMed:17989228). Involved in plant immunity, with
CC antagonistic effects on bacterial and fungal resistances
CC (PubMed:23062058). Mediates activation of the plasma membrane H(+)-
CC ATPase by PSY1 (PubMed:25267325). Phosphorylates AHA2 at Thr-881
CC (PubMed:25267325). {ECO:0000269|PubMed:17989228,
CC ECO:0000269|PubMed:23062058, ECO:0000269|PubMed:25267325}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Homo- and heterodimers with PSKR1. Interacts (via C-terminus)
CC with AHA1 and AHA2 (via the R-domain). {ECO:0000269|PubMed:25267325}.
CC -!- INTERACTION:
CC Q9C7S5; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16904988, EBI-16902452;
CC Q9C7S5; Q94F62: BAK1; NbExp=2; IntAct=EBI-16904988, EBI-617138;
CC Q9C7S5; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16904988, EBI-16895926;
CC Q9C7S5; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-16904988, EBI-16924837;
CC Q9C7S5; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16904988, EBI-20651739;
CC Q9C7S5; Q9LFS4: NIK1; NbExp=3; IntAct=EBI-16904988, EBI-16146189;
CC Q9C7S5; Q9C7S5: PSY1R; NbExp=2; IntAct=EBI-16904988, EBI-16904988;
CC Q9C7S5; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-16904988, EBI-1238953;
CC Q9C7S5; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-16904988, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25267325};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, including in the shoot
CC apical meristem and in the elongation zone of the root meristem.
CC {ECO:0000269|PubMed:17989228}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:25267325}.
CC -!- DISRUPTION PHENOTYPE: Loss of sensitivity to PSY1 (PubMed:17989228).
CC Loss of PSY1 induced phosphorylation of AHA2 and reduced hypocotyl
CC elongation (PubMed:25267325). Increased symptom formation, disease
CC index, lesion size and fungal growth after infection with
CC A.brassicicola, but increased resistance to bacterial infection
CC (PubMed:23062058). {ECO:0000269|PubMed:17989228,
CC ECO:0000269|PubMed:23062058, ECO:0000269|PubMed:25267325}.
CC -!- MISCELLANEOUS: PSYR1 and PSKR1 mediate a signaling pathway by two
CC distinct ligands, which redundantly contribute to cellular
CC proliferation and plant growth. {ECO:0000269|PubMed:17989228}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC067754; AAG51803.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35300.1; -; Genomic_DNA.
DR EMBL; AY080797; AAL87278.1; -; mRNA.
DR EMBL; AY133783; AAM91717.1; -; mRNA.
DR EMBL; AK229165; BAF01036.1; -; mRNA.
DR PIR; G96746; G96746.
DR RefSeq; NP_177374.1; NM_105889.6.
DR AlphaFoldDB; Q9C7S5; -.
DR SMR; Q9C7S5; -.
DR BioGRID; 28782; 50.
DR IntAct; Q9C7S5; 56.
DR STRING; 3702.AT1G72300.1; -.
DR PaxDb; Q9C7S5; -.
DR PRIDE; Q9C7S5; -.
DR ProteomicsDB; 226040; -.
DR EnsemblPlants; AT1G72300.1; AT1G72300.1; AT1G72300.
DR GeneID; 843562; -.
DR Gramene; AT1G72300.1; AT1G72300.1; AT1G72300.
DR KEGG; ath:AT1G72300; -.
DR Araport; AT1G72300; -.
DR TAIR; locus:2207056; AT1G72300.
DR eggNOG; ENOG502QTQY; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; Q9C7S5; -.
DR OMA; PMIRTAQ; -.
DR OrthoDB; 84395at2759; -.
DR PhylomeDB; Q9C7S5; -.
DR PRO; PR:Q9C7S5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7S5; baseline and differential.
DR Genevisible; Q9C7S5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001653; F:peptide receptor activity; IMP:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:TAIR.
DR GO; GO:0045851; P:pH reduction; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031347; P:regulation of defense response; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 12.
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; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1095
FT /note="Tyrosine-sulfated glycopeptide receptor 1"
FT /id="PRO_0000365619"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 91..115
FT /note="LRR 1"
FT REPEAT 116..139
FT /note="LRR 2"
FT REPEAT 141..165
FT /note="LRR 3"
FT REPEAT 170..195
FT /note="LRR 4"
FT REPEAT 197..221
FT /note="LRR 5"
FT REPEAT 223..246
FT /note="LRR 6"
FT REPEAT 247..270
FT /note="LRR 7"
FT REPEAT 271..294
FT /note="LRR 8"
FT REPEAT 295..318
FT /note="LRR 9"
FT REPEAT 320..342
FT /note="LRR 10"
FT REPEAT 344..366
FT /note="LRR 11"
FT REPEAT 367..391
FT /note="LRR 12"
FT REPEAT 393..415
FT /note="LRR 13"
FT REPEAT 416..439
FT /note="LRR 14"
FT REPEAT 441..466
FT /note="LRR 15"
FT REPEAT 470..494
FT /note="LRR 16"
FT REPEAT 495..517
FT /note="LRR 17"
FT REPEAT 518..542
FT /note="LRR 18"
FT REPEAT 566..589
FT /note="LRR 19"
FT REPEAT 604..628
FT /note="LRR 20"
FT REPEAT 629..652
FT /note="LRR 21"
FT REPEAT 654..677
FT /note="LRR 22"
FT DOMAIN 803..1074
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 929
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 809..817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 831
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 876
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 916
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 971
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1072..1095
FT /note="Missing: Loss of kinase activity and loss of
FT interaction with AHA1 and AHA2."
FT /evidence="ECO:0000269|PubMed:25267325"
SQ SEQUENCE 1095 AA; 121521 MW; 52DECA8C2E0669BA CRC64;
MIDEKMRSKS IGPFVRQVKP LSPHMVLFVL LYVLSISVFF LTVSEAVCNL QDRDSLLWFS
GNVSSPVSPL HWNSSIDCCS WEGISCDKSP ENRVTSIILS SRGLSGNLPS SVLDLQRLSR
LDLSHNRLSG PLPPGFLSAL DQLLVLDLSY NSFKGELPLQ QSFGNGSNGI FPIQTVDLSS
NLLEGEILSS SVFLQGAFNL TSFNVSNNSF TGSIPSFMCT ASPQLTKLDF SYNDFSGDLS
QELSRCSRLS VLRAGFNNLS GEIPKEIYNL PELEQLFLPV NRLSGKIDNG ITRLTKLTLL
ELYSNHIEGE IPKDIGKLSK LSSLQLHVNN LMGSIPVSLA NCTKLVKLNL RVNQLGGTLS
AIDFSRFQSL SILDLGNNSF TGEFPSTVYS CKMMTAMRFA GNKLTGQISP QVLELESLSF
FTFSDNKMTN LTGALSILQG CKKLSTLIMA KNFYDETVPS NKDFLRSDGF PSLQIFGIGA
CRLTGEIPAW LIKLQRVEVM DLSMNRFVGT IPGWLGTLPD LFYLDLSDNF LTGELPKELF
QLRALMSQKA YDATERNYLE LPVFVNPNNV TTNQQYNQLS SLPPTIYIKR NNLTGTIPVE
VGQLKVLHIL ELLGNNFSGS IPDELSNLTN LERLDLSNNN LSGRIPWSLT GLHFLSYFNV
ANNTLSGPIP TGTQFDTFPK ANFEGNPLLC GGVLLTSCDP TQHSTTKMGK GKVNRTLVLG
LVLGLFFGVS LILVLLALLV LSKRRVNPGD SENAELEINS NGSYSEVPPG SDKDISLVLL
FGNSRYEVKD LTIFELLKAT DNFSQANIIG CGGFGLVYKA TLDNGTKLAV KKLTGDYGMM
EKEFKAEVEV LSRAKHENLV ALQGYCVHDS ARILIYSFME NGSLDYWLHE NPEGPAQLDW
PKRLNIMRGA SSGLAYMHQI CEPHIVHRDI KSSNILLDGN FKAYVADFGL SRLILPYRTH
VTTELVGTLG YIPPEYGQAW VATLRGDVYS FGVVMLELLT GKRPMEVFRP KMSRELVAWV
HTMKRDGKPE EVFDTLLRES GNEEAMLRVL DIACMCVNQN PMKRPNIQQV VDWLKNIEAE
KNQNNREEPE EEEET
