BAME2_ARATH
ID BAME2_ARATH Reviewed; 1002 AA.
AC Q9M2Z1; Q0WLN9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM2;
DE EC=2.7.11.1;
DE AltName: Full=Protein BARELY ANY MERISTEM 2;
DE Flags: Precursor;
GN Name=BAM2; OrderedLocusNames=At3g49670; ORFNames=T16K5.20;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=16751349; DOI=10.1105/tpc.105.036871;
RA Hord C.L.H., Chen C., Deyoung B.J., Clark S.E., Ma H.;
RT "The BAM1/BAM2 receptor-like kinases are important regulators of
RT Arabidopsis early anther development.";
RL Plant Cell 18:1667-1680(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16367950; DOI=10.1111/j.1365-313x.2005.02592.x;
RA DeYoung B.J., Bickle K.L., Schrage K.J., Muskett P., Patel K., Clark S.E.;
RT "The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-like proteins are
RT required for meristem function in Arabidopsis.";
RL Plant J. 45:1-16(2006).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18780746; DOI=10.1534/genetics.108.091108;
RA Deyoung B.J., Clark S.E.;
RT "BAM receptors regulate stem cell specification and organ development
RT through complex interactions with CLAVATA signaling.";
RL Genetics 180:895-904(2008).
RN [9]
RP INTERACTION WITH MCLV3; CLE11; CLE18; CLE19; CLE22; CLE25; CLE26; CLE40;
RP CLE41; CLE42; BAM1 AND CLV1, AND SUBCELLULAR LOCATION.
RX PubMed=20626648; DOI=10.1111/j.1365-313x.2010.04295.x;
RA Guo Y., Han L., Hymes M., Denver R., Clark S.E.;
RT "CLAVATA2 forms a distinct CLE-binding receptor complex regulating
RT Arabidopsis stem cell specification.";
RL Plant J. 63:889-900(2010).
CC -!- FUNCTION: Necessary for male gametophyte development, as well as ovule
CC specification and function. Involved in cell-cell communication process
CC required during early anther development, and regulating cell division
CC and differentiation to organize cell layers. Required for the
CC development of high-ordered vascular strands within the leaf and a
CC correlated control of leaf shape, size and symmetry. May regulate the
CC CLV1-dependent CLV3-mediated signaling in meristems maintenance.
CC {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:16751349,
CC ECO:0000269|PubMed:18780746}.
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: Interacts with BAM1 and CLV1. Binds to the CLV3, CLE11, CLE18,
CC CLE19, CLE22, CLE25, CLE26, CLE40, CLE41 and CLE42 mature peptides,
CC probably via its extracellular leucine-rich repeat region.
CC {ECO:0000269|PubMed:20626648}.
CC -!- INTERACTION:
CC Q9M2Z1; F4I065: At1g49100; NbExp=2; IntAct=EBI-16933791, EBI-20654598;
CC Q9M2Z1; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16933791, EBI-20651541;
CC Q9M2Z1; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16933791, EBI-20651413;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20626648};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20626648}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, rosette leaves,
CC stems, inflorescences, flowers and siliques.
CC {ECO:0000269|PubMed:16367950}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a ring surrounding the center of
CC meristems extended in the cortex of developing stems and older
CC pedicels. Present in all developing floral organs, especially in
CC anthers and gynoecium (mainly in ovules). Observed in anthers at stage
CC 2 in the archesporial cells. At stage 3, localized in the primary
CC sporogenous and primary parietal cells. Subsequently preferentially
CC expressed in the sporogenous cells at anther stage 4. Later restricted
CC to the tapetum and pollen mother cells (PMCs) before disappearing
CC progressively. {ECO:0000269|PubMed:16367950,
CC ECO:0000269|PubMed:16751349}.
CC -!- DISRUPTION PHENOTYPE: Rescues partially CLV3 disruption. When
CC associated with BAM1 disruption, abnormal anthers at a very early stage
CC and later lack of endothecium, middle and tapetum layers. Loss of stem
CC cells at the shoot and flower meristems. {ECO:0000269|PubMed:16367950,
CC ECO:0000269|PubMed:16751349, ECO:0000269|PubMed:18780746}.
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; AL132965; CAB66905.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78574.1; -; Genomic_DNA.
DR EMBL; BT005722; AAO64138.1; -; mRNA.
DR EMBL; BT006113; AAP04098.1; -; mRNA.
DR EMBL; FJ708737; ACN59331.1; -; mRNA.
DR EMBL; AK228595; BAF00510.1; -; mRNA.
DR EMBL; AK230159; BAF01968.1; -; mRNA.
DR PIR; T46033; T46033.
DR RefSeq; NP_190536.1; NM_114827.4.
DR AlphaFoldDB; Q9M2Z1; -.
DR SMR; Q9M2Z1; -.
DR BioGRID; 9447; 39.
DR IntAct; Q9M2Z1; 39.
DR STRING; 3702.AT3G49670.1; -.
DR iPTMnet; Q9M2Z1; -.
DR PaxDb; Q9M2Z1; -.
DR PRIDE; Q9M2Z1; -.
DR ProteomicsDB; 240710; -.
DR EnsemblPlants; AT3G49670.1; AT3G49670.1; AT3G49670.
DR GeneID; 824129; -.
DR Gramene; AT3G49670.1; AT3G49670.1; AT3G49670.
DR KEGG; ath:AT3G49670; -.
DR Araport; AT3G49670; -.
DR TAIR; locus:2097310; AT3G49670.
DR eggNOG; ENOG502QQRQ; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9M2Z1; -.
DR OMA; SNKEHVI; -.
DR OrthoDB; 154810at2759; -.
DR PhylomeDB; Q9M2Z1; -.
DR PRO; PR:Q9M2Z1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Z1; baseline and differential.
DR Genevisible; Q9M2Z1; AT.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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:0048437; P:floral organ development; IGI:TAIR.
DR GO; GO:0048229; P:gametophyte development; IGI:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; PF12799; LRR_4; 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; 13.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1002
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase BAM2"
FT /id="PRO_0000403353"
FT TOPO_DOM 23..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..92
FT /note="LRR 1"
FT REPEAT 93..116
FT /note="LRR 2"
FT REPEAT 118..140
FT /note="LRR 3"
FT REPEAT 141..165
FT /note="LRR 4"
FT REPEAT 167..188
FT /note="LRR 5"
FT REPEAT 189..213
FT /note="LRR 6"
FT REPEAT 215..238
FT /note="LRR 7"
FT REPEAT 239..262
FT /note="LRR 8"
FT REPEAT 263..285
FT /note="LRR 9"
FT REPEAT 286..309
FT /note="LRR 10"
FT REPEAT 311..334
FT /note="LRR 11"
FT REPEAT 335..358
FT /note="LRR 12"
FT REPEAT 359..382
FT /note="LRR 13"
FT REPEAT 384..406
FT /note="LRR 14"
FT REPEAT 407..430
FT /note="LRR 15"
FT REPEAT 431..456
FT /note="LRR 16"
FT REPEAT 458..479
FT /note="LRR 17"
FT REPEAT 480..503
FT /note="LRR 18"
FT REPEAT 505..527
FT /note="LRR 19"
FT REPEAT 528..551
FT /note="LRR 20"
FT REPEAT 552..575
FT /note="LRR 21"
FT REPEAT 577..600
FT /note="LRR 22"
FT DOMAIN 690..967
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 969..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 816
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 696..704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 765
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 803
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 859
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 866
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
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 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
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 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1002 AA; 109244 MW; 859FF7FAB857EDAF CRC64;
MKLLLLLLLL LLLHISHSFT VAKPITELHA LLSLKSSFTI DEHSPLLTSW NLSTTFCSWT
GVTCDVSLRH VTSLDLSGLN LSGTLSSDVA HLPLLQNLSL AANQISGPIP PQISNLYELR
HLNLSNNVFN GSFPDELSSG LVNLRVLDLY NNNLTGDLPV SLTNLTQLRH LHLGGNYFSG
KIPATYGTWP VLEYLAVSGN ELTGKIPPEI GNLTTLRELY IGYYNAFENG LPPEIGNLSE
LVRFDAANCG LTGEIPPEIG KLQKLDTLFL QVNAFTGTIT QELGLISSLK SMDLSNNMFT
GEIPTSFSQL KNLTLLNLFR NKLYGAIPEF IGEMPELEVL QLWENNFTGS IPQKLGENGR
LVILDLSSNK LTGTLPPNMC SGNRLMTLIT LGNFLFGSIP DSLGKCESLT RIRMGENFLN
GSIPKELFGL PKLSQVELQD NYLTGELPIS GGGVSGDLGQ ISLSNNQLSG SLPAAIGNLS
GVQKLLLDGN KFSGSIPPEI GRLQQLSKLD FSHNLFSGRI APEISRCKLL TFVDLSRNEL
SGDIPNELTG MKILNYLNLS RNHLVGSIPV TIASMQSLTS VDFSYNNLSG LVPSTGQFSY
FNYTSFVGNS HLCGPYLGPC GKGTHQSHVK PLSATTKLLL VLGLLFCSMV FAIVAIIKAR
SLRNASEAKA WRLTAFQRLD FTCDDVLDSL KEDNIIGKGG AGIVYKGTMP KGDLVAVKRL
ATMSHGSSHD HGFNAEIQTL GRIRHRHIVR LLGFCSNHET NLLVYEYMPN GSLGEVLHGK
KGGHLHWNTR YKIALEAAKG LCYLHHDCSP LIVHRDVKSN NILLDSNFEA HVADFGLAKF
LQDSGTSECM SAIAGSYGYI APEYAYTLKV DEKSDVYSFG VVLLELITGK KPVGEFGDGV
DIVQWVRSMT DSNKDCVLKV IDLRLSSVPV HEVTHVFYVA LLCVEEQAVE RPTMREVVQI
LTEIPKIPLS KQQAAESDVT EKAPAINESS PDSGSPPDLL SN
