RLK7_ARATH
ID RLK7_ARATH Reviewed; 977 AA.
AC F4I2N7; O04517; Q56X19; Q8W4B5; Q941F6;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Receptor-like protein kinase 7 {ECO:0000303|PubMed:20811905};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=RLK7 {ECO:0000303|PubMed:20811905};
GN OrderedLocusNames=At1g09970 {ECO:0000312|Araport:AT1G09970};
GN ORFNames=F21M12.36 {ECO:0000312|EMBL:AAB60752.1};
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] (ISOFORM 2).
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 [MRNA] (ISOFORM 1).
RA Zeitler B., Reed R., Watson A., Zeitler J., Miller S., Baca J.,
RA Basinger H., Bassett S., Brentlinger K., Calabro K., Crider H., Danzl N.,
RA Daw G., Gordon K., Haney C., Hendrix S., Hensley G., Ihle N., Karney D.,
RA Keene K., Kraft J., Kurtis J., Lindsey N., Mesa O., Munoz J., Nevarez D.,
RA Parkin E., Ranjel A., Rayhorn D., Reed C., Rogers D., Rogers T., Runge J.,
RA Sherwood C., Smart T., Sutton J., Tate W., Thompson R., White C.,
RA Wollenberg M., Chambers J., Tax F.;
RT "The sequence of the Arabidopsis thaliana leucine-rich-repeat receptor-like
RT kinase F21M12.36 mRNA as determined by the Spring 2001 MCB 473 class.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 655-977 (ISOFORM 2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20811905; DOI=10.1007/s00425-010-1260-4;
RA Pitorre D., Llauro C., Jobet E., Guilleminot J., Brizard J.P., Delseny M.,
RA Lasserre E.;
RT "RLK7, a leucine-rich repeat receptor-like kinase, is required for proper
RT germination speed and tolerance to oxidative stress in Arabidopsis
RT thaliana.";
RL Planta 232:1339-1353(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH PIP1.
RX PubMed=25188390; DOI=10.1371/journal.ppat.1004331;
RA Hou S., Wang X., Chen D., Yang X., Wang M., Turra D., Di Pietro A.,
RA Zhang W.;
RT "The secreted peptide PIP1 amplifies immunity through receptor-like kinase
RT 7.";
RL PLoS Pathog. 10:E1004331-E1004331(2014).
CC -!- FUNCTION: Plays a role in pattern-triggered immunity (PTI) signaling
CC induced by pathogen-associated molecular patterns (PAMPs). Acts as a
CC receptor for PIP1 defense peptide. PIP1 is an endogenous secreted
CC peptide that acts as elicitor of immune response and positive regulator
CC of defense response (PubMed:25188390). Involved in the control of seed
CC germination speed, in tolerance to oxidative stress and in maintaining
CC seed longevity (PubMed:20811905). {ECO:0000269|PubMed:20811905,
CC ECO:0000269|PubMed:25188390}.
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: Interacts with PIP1. {ECO:0000269|PubMed:25188390}.
CC -!- INTERACTION:
CC F4I2N7-2; C0LGE0: At1g07650; NbExp=3; IntAct=EBI-20651307, EBI-16954597;
CC F4I2N7-2; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20651307, EBI-20651541;
CC F4I2N7-2; Q9LT96: At5g49770; NbExp=3; IntAct=EBI-20651307, EBI-17123993;
CC F4I2N7-2; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-20651307, EBI-16934827;
CC F4I2N7-2; Q9LVP0: At5g63930; NbExp=2; IntAct=EBI-20651307, EBI-16955586;
CC F4I2N7-2; C0LGN7: LRR-RLK; NbExp=2; IntAct=EBI-20651307, EBI-20651518;
CC F4I2N7-2; Q9LPT1: PRK5; NbExp=2; IntAct=EBI-20651307, EBI-16914400;
CC F4I2N7-2; F4I2N7-2: RLK7; NbExp=2; IntAct=EBI-20651307, EBI-20651307;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4I2N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4I2N7-2; Sequence=VSP_059529;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and dry seeds. Expressed
CC at junctions between organs, such as the insertion zones of stamens,
CC petals and sepals, the transition zones of floral stem and pedicel,
CC pedicel and silique, and floral stem and cauline leaves.
CC {ECO:0000269|PubMed:20811905}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expressed from the heart stage to
CC dry seeds. In germinating seeds, expression decreases during imbibition
CC and increasees again 72 hours after imbibition, during the
CC establishment of the seedling. {ECO:0000269|PubMed:20811905}.
CC -!- DISRUPTION PHENOTYPE: Slightly delayed seed germination.
CC {ECO:0000269|PubMed:20811905}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60752.1; 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; FJ708631; ACN59227.1; -; mRNA.
DR EMBL; AY050535; AAL12626.1; -; mRNA.
DR EMBL; AC000132; AAB60752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28522.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28523.1; -; Genomic_DNA.
DR EMBL; AY062680; AAL32758.1; -; mRNA.
DR EMBL; AK221860; BAD94141.1; -; mRNA.
DR PIR; B86234; B86234.
DR RefSeq; NP_172468.3; NM_100871.3. [F4I2N7-1]
DR RefSeq; NP_850942.1; NM_180611.2. [F4I2N7-2]
DR AlphaFoldDB; F4I2N7; -.
DR SMR; F4I2N7; -.
DR IntAct; F4I2N7; 59.
DR STRING; 3702.AT1G09970.2; -.
DR PaxDb; F4I2N7; -.
DR PRIDE; F4I2N7; -.
DR ProteomicsDB; 228180; -. [F4I2N7-1]
DR EnsemblPlants; AT1G09970.1; AT1G09970.1; AT1G09970. [F4I2N7-2]
DR EnsemblPlants; AT1G09970.2; AT1G09970.2; AT1G09970. [F4I2N7-1]
DR GeneID; 837531; -.
DR Gramene; AT1G09970.1; AT1G09970.1; AT1G09970. [F4I2N7-2]
DR Gramene; AT1G09970.2; AT1G09970.2; AT1G09970. [F4I2N7-1]
DR KEGG; ath:AT1G09970; -.
DR Araport; AT1G09970; -.
DR TAIR; locus:2024432; AT1G09970.
DR eggNOG; ENOG502QVPY; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; F4I2N7; -.
DR OMA; ELTHFYA; -.
DR OrthoDB; 121113at2759; -.
DR PhylomeDB; F4I2N7; -.
DR PRO; PR:F4I2N7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I2N7; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042277; F:peptide binding; IPI:TAIR.
DR GO; GO:0001653; F:peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..977
FT /note="Receptor-like protein kinase 7"
FT /evidence="ECO:0000255"
FT /id="PRO_5003309427"
FT TOPO_DOM 29..608
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 71..95
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 96..119
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 121..145
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..194
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 195..218
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 219..242
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 244..265
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 267..289
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 290..312
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 313..337
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 339..361
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 362..385
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 386..409
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 411..433
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 434..457
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 458..481
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 482..505
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 507..529
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 530..553
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 555..578
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 666..959
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 805
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 672..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
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 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 853
FT /note="Missing (in isoform 2)"
FT /id="VSP_059529"
FT CONFLICT 509
FT /note="S -> N (in Ref. 2; AAL12626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 107450 MW; F1254498F7F728FA CRC64;
MAPSLRNFNF FHRFSTFLVF SLFSVVSSDD LQVLLKLKSS FADSNLAVFD SWKLNSGIGP
CSFIGVTCNS RGNVTEIDLS RRGLSGNFPF DSVCEIQSLE KLSLGFNSLS GIIPSDLKNC
TSLKYLDLGN NLFSGAFPEF SSLNQLQFLY LNNSAFSGVF PWKSLRNATS LVVLSLGDNP
FDATADFPVE VVSLKKLSWL YLSNCSIAGK IPPAIGDLTE LRNLEISDSG LTGEIPSEIS
KLTNLWQLEL YNNSLTGKLP TGFGNLKNLT YLDASTNLLQ GDLSELRSLT NLVSLQMFEN
EFSGEIPLEF GEFKDLVNLS LYTNKLTGSL PQGLGSLADF DFIDASENLL TGPIPPDMCK
NGKMKALLLL QNNLTGSIPE SYANCLTLQR FRVSENNLNG TVPAGLWGLP KLEIIDIEMN
NFEGPITADI KNGKMLGALY LGFNKLSDEL PEEIGDTESL TKVELNNNRF TGKIPSSIGK
LKGLSSLKMQ SNGFSGEIPD SIGSCSMLSD VNMAQNSISG EIPHTLGSLP TLNALNLSDN
KLSGRIPESL SSLRLSLLDL SNNRLSGRIP LSLSSYNGSF NGNPGLCSTT IKSFNRCINP
SRSHGDTRVF VLCIVFGLLI LLASLVFFLY LKKTEKKEGR SLKHESWSIK SFRKMSFTED
DIIDSIKEEN LIGRGGCGDV YRVVLGDGKE VAVKHIRCSS TQKNFSSAMP ILTEREGRSK
EFETEVQTLS SIRHLNVVKL YCSITSDDSS LLVYEYLPNG SLWDMLHSCK KSNLGWETRY
DIALGAAKGL EYLHHGYERP VIHRDVKSSN ILLDEFLKPR IADFGLAKIL QASNGGPEST
HVVAGTYGYI APAEYGYASK VTEKCDVYSF GVVLMELVTG KKPIEAEFGE SKDIVNWVSN
NLKSKESVME IVDKKIGEMY REDAVKMLRI AIICTARLPG LRPTMRSVVQ MIEDAEPCRL
MGIVISKESD VKVKEIS
