IOS1_ARATH
ID IOS1_ARATH Reviewed; 894 AA.
AC Q9C8I6; Q7FL10;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase IOS1 {ECO:0000303|PubMed:21711359};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein IMPAIRED OOMYCETE SUSCEPTIBILITY 1 {ECO:0000303|PubMed:21711359};
DE Flags: Precursor;
GN Name=IOS1 {ECO:0000303|PubMed:21711359};
GN OrderedLocusNames=At1g51800 {ECO:0000312|Araport:AT1G51800};
GN ORFNames=F19C24.3 {ECO:0000312|EMBL:AAG50874.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY H.ARABIDOPSIDIS.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=21711359; DOI=10.1111/j.1365-3040.2011.02390.x;
RA Hok S., Danchin E.G., Allasia V., Panabieres F., Attard A., Keller H.;
RT "An Arabidopsis (malectin-like) leucine-rich repeat receptor-like kinase
RT contributes to downy mildew disease.";
RL Plant Cell Environ. 34:1944-1957(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY E.CRUCIFERARUM; H.ARABIDOPSIDIS AND P.PARASITICA.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=25274985; DOI=10.1104/pp.114.248518;
RA Hok S., Allasia V., Andrio E., Naessens E., Ribes E., Panabieres F.,
RA Attard A., Ris N., Clement M., Barlet X., Marco Y., Grill E., Eichmann R.,
RA Weis C., Hueckelhoven R., Ammon A., Ludwig-Mueller J., Voll L.M.,
RA Keller H.;
RT "The receptor kinase IMPAIRED OOMYCETE SUSCEPTIBILITY1 attenuates abscisic
RT acid responses in Arabidopsis.";
RL Plant Physiol. 166:1506-1518(2014).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BAK1; FLS2; CERK1 AND EFR,
RP INDUCTION BY FLG22 OR ELF18, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT and BAK1-independent pattern-triggered immunity.";
RL Plant Cell 28:1701-1721(2016).
CC -!- FUNCTION: Regulates negatively the abscisic acid (ABA) signaling
CC pathway (PubMed:25274985). Required for full susceptibility to
CC filamentous (hemi)biotrophic oomycetes (e.g. H.arabidopsidis and
CC P.parasitica) and fungal (e.g. E.cruciferarum) pathogens, probably by
CC triggering the repression of ABA-sensitive COLD REGULATED and
CC RESISTANCE TO DESICCATION genes during infection, but independently of
CC immune responses (PubMed:21711359, PubMed:25274985). Involved in BAK1-
CC dependent and BAK1-independent microbe-associated molecular patterns
CC (MAMPs)-triggered immunity (PTI) leading to defense responses,
CC including callose deposition and MAPK cascade activation, toward
CC pathogenic bacteria (e.g. P.syringae). Required for chitin-mediated PTI
CC (PubMed:27317676). {ECO:0000269|PubMed:21711359,
CC ECO:0000269|PubMed:25274985, ECO:0000269|PubMed:27317676}.
CC -!- SUBUNIT: Homodimerization. Interacts with BAK1 and FLS2; triggers FLS2-
CC BAK1 complex formation upon microbe-associated molecular patterns
CC (MAMPs) treatment. Binds also to CERK1 and EFR.
CC {ECO:0000269|PubMed:27317676}.
CC -!- INTERACTION:
CC Q9C8I6; C0LGI5: At1g69990; NbExp=4; IntAct=EBI-16924837, EBI-20651225;
CC Q9C8I6; Q8VYT3: At4g30520; NbExp=3; IntAct=EBI-16924837, EBI-16902452;
CC Q9C8I6; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16924837, EBI-6298290;
CC Q9C8I6; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-16924837, EBI-20653342;
CC Q9C8I6; Q94F62: BAK1; NbExp=2; IntAct=EBI-16924837, EBI-617138;
CC Q9C8I6; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16924837, EBI-590903;
CC Q9C8I6; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16924837, EBI-20651413;
CC Q9C8I6; Q42371: ERECTA; NbExp=3; IntAct=EBI-16924837, EBI-16940407;
CC Q9C8I6; C0LGW6: ERL1; NbExp=4; IntAct=EBI-16924837, EBI-16914248;
CC Q9C8I6; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16924837, EBI-16895926;
CC Q9C8I6; Q9FL28: FLS2; NbExp=2; IntAct=EBI-16924837, EBI-1799448;
CC Q9C8I6; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-16924837, EBI-16924837;
CC Q9C8I6; Q9C7S5: PSY1R; NbExp=3; IntAct=EBI-16924837, EBI-16904988;
CC Q9C8I6; Q9ZRF9: RPK1; NbExp=4; IntAct=EBI-16924837, EBI-1238953;
CC Q9C8I6; Q94AG2: SERK1; NbExp=4; IntAct=EBI-16924837, EBI-1555537;
CC Q9C8I6; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-16924837, EBI-6290483;
CC Q9C8I6; Q8RWZ1: SUB; NbExp=3; IntAct=EBI-16924837, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27317676};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:25274985}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in tissue with fates
CC controlled by the phytohormone abscisic acid (ABA). In roots, expressed
CC in the radicle emerging from the testa, in the elongation zones of
CC roots, and in root cap border cells undergoing detachment. In
CC hypocotyls, detected only during etiolation in the dark. In cotyledons
CC and leaves, restricted to cells surrounding stomata. In reproductive
CC organs, observed in the style after pollination, in the abscission
CC zones of sepals and petals, in the transmitting tract of developing
CC fruits, and in the abscission zones of mature siliques. Also present in
CC pollen tubes. {ECO:0000269|PubMed:25274985}.
CC -!- INDUCTION: Accumulates during infection by filamentous (hemi)biotrophic
CC oomycetes (e.g. H.arabidopsidis and P.parasitica) and fungal (e.g.
CC E.cruciferarum) pathogens, being locally expressed in cells surrounding
CC the pathogens both at early and late stages of infection
CC (PubMed:21711359, PubMed:25274985). Induced by microbe-associated
CC molecular patterns (MAMPs) flg22 or elf18 (PubMed:27317676).
CC {ECO:0000269|PubMed:21711359, ECO:0000269|PubMed:25274985,
CC ECO:0000269|PubMed:27317676}.
CC -!- DISRUPTION PHENOTYPE: Reduced infection by filamentous (hemi)biotrophic
CC oomycetes (e.g. H.arabidopsidis and P.parasitica) and fungal (e.g.
CC E.cruciferarum) pathogens, independently of plant defense mechanism
CC (PubMed:21711359, PubMed:25274985). Hypersensitivity to abscisic acid
CC (ABA), displaying enhanced ABA-mediated inhibition of seed germination,
CC root elongation, and stomatal opening. Impaired repression of ABA-
CC sensitive COLD REGULATED and RESISTANCE TO DESICCATION genes upon
CC oomycete infection. No obvious modification of defense-related gene
CC induction during pathogen attack (PubMed:25274985). Hypersusceptibility
CC to the necrotrophic bacteria P.syringae. Defective pattern-triggered
CC immunity (PTI) responses, delayed up-regulation of PTI marker genes,
CC reduced callose deposition, and mitogen-activated protein kinase
CC activation upon microbe-associated molecular patterns (MAMPs)
CC treatment. Impaired beta-aminobutyric acid (BABA)-induced resistance
CC and priming (PubMed:27317676). {ECO:0000269|PubMed:21711359,
CC ECO:0000269|PubMed:25274985, ECO:0000269|PubMed:27317676}.
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; FJ708650; ACN59246.1; -; mRNA.
DR EMBL; AC025294; AAG50874.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32717.1; -; Genomic_DNA.
DR EMBL; AK118836; BAC43425.2; -; mRNA.
DR PIR; B96557; B96557.
DR RefSeq; NP_175591.1; NM_104059.3.
DR AlphaFoldDB; Q9C8I6; -.
DR SMR; Q9C8I6; -.
DR IntAct; Q9C8I6; 39.
DR STRING; 3702.AT1G51800.1; -.
DR iPTMnet; Q9C8I6; -.
DR PaxDb; Q9C8I6; -.
DR PRIDE; Q9C8I6; -.
DR ProteomicsDB; 228844; -.
DR EnsemblPlants; AT1G51800.1; AT1G51800.1; AT1G51800.
DR GeneID; 841606; -.
DR Gramene; AT1G51800.1; AT1G51800.1; AT1G51800.
DR KEGG; ath:AT1G51800; -.
DR Araport; AT1G51800; -.
DR TAIR; locus:2017557; AT1G51800.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9C8I6; -.
DR OMA; KEVDAMM; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9C8I6; -.
DR PRO; PR:Q9C8I6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8I6; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0090406; C:pollen tube; 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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:1902289; P:negative regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000071; P:regulation of defense response by callose deposition; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0010200; P:response to chitin; IMP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0002239; P:response to oomycetes; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 1.
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 Abscisic acid signaling pathway; ATP-binding; Cell membrane; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..894
FT /note="LRR receptor-like serine/threonine-protein kinase
FT IOS1"
FT /id="PRO_5010147867"
FT TOPO_DOM 24..515
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 431..457
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 459..479
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT DOMAIN 586..858
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 710
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 592..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 658
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 750
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 758
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 83
FT /note="S -> N (in Ref. 4; BAC43425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 99639 MW; 48F63F845804E27E CRC64;
MAFSSCFLLV LLQIFSALLL CLAQDQSGFI SLDCGSPRET SFREKTTNIT YISDANFINT
GVGGSIKQGY RTQFQQQTWN LRSFPQGIRN CYTLNLTIGD EYLIRANFLH GGYDDKPSTQ
FELYLGPNLW STVTTTNETE ASIFEMIHIL TTDRLQICLV KTGNATPFIS ALELRKLMNT
TYLTRQGSLQ TFIRADVGAT VNQGYRYGID VFDRVWTPYN FGNWSQISTN QSVNINNDYQ
PPEIAMVTAS VPTDPDAAMN ISLVGVERTV QFYVFMHFAE IQELKSNDTR EFNIMYNNKH
IYGPFRPLNF TTSSVFTPTE VVADANGQYI FSLQRTGNST LPPLLNAMEI YSVNLLPQQE
TDRKEVDAMM NIKSAYGVNK IDWEGDPCVP LDYKWSGVNC TYVDNETPKI ISLDLSTSGL
TGEILEFISD LTSLEVLDLS NNSLTGSVPE FLANMETLKL INLSGNELNG SIPATLLDKE
RRGSITLSIE GNTGLCSSTS CATTKKKKKN TVIAPVAASL VSVFLIGAGI VTFLILKRKK
RTKLGLNPNS GTGTTPLHSR SHHGFEPPVI AKNRKLTYID VVKITNNFER VLGRGGFGVV
YYGVLNNEPV AVKMLTESTA LGYKQFKAEV ELLLRVHHKD LTCLVGYCEE GDKMSLIYEF
MANGDLKEHL SGKRGPSILT WEGRLRIAAE SAQGLEYLHN GCKPQIVHRD IKTTNILLNE
KFQAKLADFG LSRSFPLGTE THVSTIVAGT PGYLDPEYYR TNWLTEKSDV FSFGVVLLEL
VTNQPVIDMK REKSHIAEWV GLMLSRGDIN SIVDPKLQGD FDPNTIWKVV ETAMTCLNPS
SSRRPTMTQV VMDLKECLNM EMARNMGSRM TDSTNDSSIE LSMNFTTELN PGAR
