CLV1_ARATH
ID CLV1_ARATH Reviewed; 980 AA.
AC Q9SYQ8; O04380; Q56Y00; Q9LQT2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Receptor protein kinase CLAVATA1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=CLV1; OrderedLocusNames=At1g75820; ORFNames=T4O12.5;
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9160749; DOI=10.1016/s0092-8674(00)80239-1;
RA Clark S.E., Williams R.W., Meyerowitz E.M.;
RT "The CLAVATA1 gene encodes a putative receptor kinase that controls shoot
RT and floral meristem size in Arabidopsis.";
RL Cell 89:575-585(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10080719; DOI=10.1023/a:1006127302671;
RA Williams R.W., Clark S.E., Meyerowitz E.M.;
RT "Genetic and physical characterization of a region of Arabidopsis
RT chromosome 1 containing the CLAVATA1 gene.";
RL Plant Mol. Biol. 39:171-176(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-781.
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 INTERACTION WITH CLV3.
RX PubMed=18202283; DOI=10.1126/science.1150083;
RA Ogawa M., Shinohara H., Sakagami Y., Matsubayashi Y.;
RT "Arabidopsis CLV3 peptide directly binds CLV1 ectodomain.";
RL Science 319:294-294(2008).
RN [8]
RP INTERACTION WITH CLV3 AND CLE2.
RX PubMed=19525968; DOI=10.1038/nchembio.182;
RA Ohyama K., Shinohara H., Ogawa-Ohnishi M., Matsubayashi Y.;
RT "A glycopeptide regulating stem cell fate in Arabidopsis thaliana.";
RL Nat. Chem. Biol. 5:578-580(2009).
RN [9]
RP INTERACTION WITH CRN.
RX PubMed=19843317; DOI=10.1111/j.1365-313x.2009.04049.x;
RA Zhu Y., Wang Y., Li R., Song X., Wang Q., Huang S., Jin J.B., Liu C.-M.,
RA Lin J.;
RT "Analysis of interactions among the CLAVATA3 receptors reveals a direct
RT interaction between CLAVATA2 and CORYNE in Arabidopsis.";
RL Plant J. 61:223-233(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19933383; DOI=10.1104/pp.109.149930;
RA Bleckmann A., Weidtkamp-Peters S., Seidel C.A.M., Simon R.;
RT "Stem cell signaling in Arabidopsis requires CRN to localize CLV2 to the
RT plasma membrane.";
RL Plant Physiol. 152:166-176(2010).
RN [11]
RP SUBUNIT.
RX PubMed=20220313; DOI=10.4161/psb.5.3.10790;
RA Zhu Y., Wan Y., Lin J.;
RT "Multiple receptor complexes assembled for transmitting CLV3 signaling in
RT Arabidopsis.";
RL Plant Signal. Behav. 5:300-302(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=21051944; DOI=10.4161/psb.5.11.13359;
RA Guo Y., Clark S.E.;
RT "Membrane distributions of two ligand-binding receptor complexes in the
RT CLAVATA pathway.";
RL Plant Signal. Behav. 5:1442-1445(2010).
RN [13]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=21705761; DOI=10.1534/genetics.111.130930;
RA Durbak A.R., Tax F.E.;
RT "CLAVATA signaling pathway receptors of Arabidopsis regulate cell
RT proliferation in fruit organ formation as well as in meristems.";
RL Genetics 189:177-194(2011).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=26990325; DOI=10.1111/nph.13913;
RA Hanemian M., Barlet X., Sorin C., Yadeta K.A., Keller H., Favery B.,
RA Simon R., Thomma B.P., Hartmann C., Crespi M., Marco Y., Tremousaygue D.,
RA Deslandes L.;
RT "Arabidopsis CLAVATA1 and CLAVATA2 receptors contribute to Ralstonia
RT solanacearum pathogenicity through a miR169-dependent pathway.";
RL New Phytol. 211:502-515(2016).
CC -!- FUNCTION: Involved in the detection of CLV3 and CLV3-like (CLE)
CC peptides, that act as extracellular signals regulating meristem
CC maintenance. Acts with CLV3p as a ligand-receptor pair in a signal
CC transduction pathway coordinating growth between adjacent meristematic
CC regions and controlling the balance between meristem cell proliferation
CC and differentiation. {ECO:0000269|PubMed:19933383}.
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 -!- 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;
CC -!- SUBUNIT: Self-interacts. Interacts with CRN; this interaction is
CC direct. Interacts with CLV3 and CLE2 mature peptides (MCLV3 and CLE2p,
CC respectively) via its extracellular leucine-rich repeat region.
CC {ECO:0000269|PubMed:18202283, ECO:0000269|PubMed:19525968,
CC ECO:0000269|PubMed:19843317, ECO:0000269|PubMed:19933383,
CC ECO:0000269|PubMed:20220313}.
CC -!- INTERACTION:
CC Q9SYQ8; C0LGG3: At1g51820; NbExp=3; IntAct=EBI-1646111, EBI-17066817;
CC Q9SYQ8; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-1646111, EBI-20651385;
CC Q9SYQ8; P46014: KAPP; NbExp=6; IntAct=EBI-1646111, EBI-1646157;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19933383,
CC ECO:0000269|PubMed:21051944}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:21051944}.
CC -!- TISSUE SPECIFICITY: In a central region of the shoot and in early
CC flower meristems.
CC -!- DISRUPTION PHENOTYPE: Ectopic fruit organ initiation after floral
CC meristem termination (PubMed:21705761). Enhanced disease resistance
CC response to the bacterial pathogen Ralstonia solanacearum and to the
CC biotrophic oomycete pathogen Hyaloperonospora arabidopsidis
CC (PubMed:26990325). {ECO:0000269|PubMed:21705761,
CC ECO:0000269|PubMed:26990325}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26772.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD94816.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BX815769; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U96879; AAB58929.1; -; Genomic_DNA.
DR EMBL; AF049870; AAD02501.1; -; Genomic_DNA.
DR EMBL; AC007396; AAF26772.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35762.1; -; Genomic_DNA.
DR EMBL; BX815769; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK221523; BAD94816.1; ALT_SEQ; mRNA.
DR RefSeq; NP_177710.1; NM_106232.4.
DR AlphaFoldDB; Q9SYQ8; -.
DR SMR; Q9SYQ8; -.
DR BioGRID; 29134; 22.
DR ELM; Q9SYQ8; -.
DR IntAct; Q9SYQ8; 14.
DR STRING; 3702.AT1G75820.1; -.
DR PaxDb; Q9SYQ8; -.
DR PRIDE; Q9SYQ8; -.
DR ProteomicsDB; 241068; -.
DR EnsemblPlants; AT1G75820.1; AT1G75820.1; AT1G75820.
DR GeneID; 843915; -.
DR Gramene; AT1G75820.1; AT1G75820.1; AT1G75820.
DR KEGG; ath:AT1G75820; -.
DR Araport; AT1G75820; -.
DR TAIR; locus:2204350; AT1G75820.
DR eggNOG; ENOG502QQ4T; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9SYQ8; -.
DR OMA; GQFMVFN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9SYQ8; -.
DR BRENDA; 2.7.10.2; 399.
DR PRO; PR:Q9SYQ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYQ8; baseline and differential.
DR Genevisible; Q9SYQ8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
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:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Differentiation;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; 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..980
FT /note="Receptor protein kinase CLAVATA1"
FT /id="PRO_0000024317"
FT TOPO_DOM 25..638
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 93..119
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 121..142
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 143..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..193
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 215..239
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 240..264
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 265..288
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 289..312
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 314..336
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 337..360
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 361..384
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 386..408
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 409..432
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 434..455
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 456..479
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 480..503
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 505..527
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 528..551
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 552..575
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 577..600
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 692..968
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 698..706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 766
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 804
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 860
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 867
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 868
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 235
FT /note="P -> R (in Ref. 1; AAB58929 and 2; AAD02501)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="A -> S (in Ref. 2; AAD02501)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="G -> D (in Ref. 2; AAD02501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 107598 MW; 2B2DC41AFF733B08 CRC64;
MAMRLLKTHL LFLHLYLFFS PCFAYTDMEV LLNLKSSMIG PKGHGLHDWI HSSSPDAHCS
FSGVSCDDDA RVISLNVSFT PLFGTISPEI GMLTHLVNLT LAANNFTGEL PLEMKSLTSL
KVLNISNNGN LTGTFPGEIL KAMVDLEVLD TYNNNFNGKL PPEMSELKKL KYLSFGGNFF
SGEIPESYGD IQSLEYLGLN GAGLSGKSPA FLSRLKNLRE MYIGYYNSYT GGVPPEFGGL
TKLEILDMAS CTLTGEIPTS LSNLKHLHTL FLHINNLTGH IPPELSGLVS LKSLDLSINQ
LTGEIPQSFI NLGNITLINL FRNNLYGQIP EAIGELPKLE VFEVWENNFT LQLPANLGRN
GNLIKLDVSD NHLTGLIPKD LCRGEKLEML ILSNNFFFGP IPEELGKCKS LTKIRIVKNL
LNGTVPAGLF NLPLVTIIEL TDNFFSGELP VTMSGDVLDQ IYLSNNWFSG EIPPAIGNFP
NLQTLFLDRN RFRGNIPREI FELKHLSRIN TSANNITGGI PDSISRCSTL ISVDLSRNRI
NGEIPKGINN VKNLGTLNIS GNQLTGSIPT GIGNMTSLTT LDLSFNDLSG RVPLGGQFLV
FNETSFAGNT YLCLPHRVSC PTRPGQTSDH NHTALFSPSR IVITVIAAIT GLILISVAIR
QMNKKKNQKS LAWKLTAFQK LDFKSEDVLE CLKEENIIGK GGAGIVYRGS MPNNVDVAIK
RLVGRGTGRS DHGFTAEIQT LGRIRHRHIV RLLGYVANKD TNLLLYEYMP NGSLGELLHG
SKGGHLQWET RHRVAVEAAK GLCYLHHDCS PLILHRDVKS NNILLDSDFE AHVADFGLAK
FLVDGAASEC MSSIAGSYGY IAPEYAYTLK VDEKSDVYSF GVVLLELIAG KKPVGEFGEG
VDIVRWVRNT EEEITQPSDA AIVVAIVDPR LTGYPLTSVI HVFKIAMMCV EEEAAARPTM
REVVHMLTNP PKSVANLIAF
