EMS1_ARATH
ID EMS1_ARATH Reviewed; 1192 AA.
AC Q9LYN8; C0LGS9; Q8GSM5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Leucine-rich repeat receptor protein kinase EMS1 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Protein EXCESS MICROSPOROCYTES 1 {ECO:0000303|PubMed:12154130};
DE AltName: Full=Protein EXTRA SPOROGENOUS CELLS {ECO:0000303|PubMed:12401166};
DE Flags: Precursor;
GN Name=EMS1 {ECO:0000303|PubMed:12154130};
GN Synonyms=ESP, EXS {ECO:0000303|PubMed:12401166};
GN OrderedLocusNames=At5g07280; ORFNames=T28J14.220;
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], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF LEU-4; LYS-104 AND VAL-1185.
RC STRAIN=cv. C24; TISSUE=Flower;
RX PubMed=12401166; DOI=10.1016/s0960-9822(02)01151-x;
RA Canales C.S., Bhatt A.M., Scott R.J., Dickinson H.G.;
RT "EXS, a putative LRR receptor kinase, regulates male germline cell number
RT and tapetal identity and promotes seed development in Arabidopsis.";
RL Curr. Biol. 12:1718-1727(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF LEU-4; LYS-104 AND VAL-1185.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12154130; DOI=10.1101/gad.997902;
RA Zhao D.-Z., Wang G.-F., Speal B., Ma H.;
RT "The EXCESS MICROSPOROCYTES1 gene encodes a putative leucine-rich repeat
RT receptor protein kinase that controls somatic and reproductive cell fates
RT in the Arabidopsis anther.";
RL Genes Dev. 16:2021-2031(2002).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
RP INTERACTION WITH TPD1.
RX PubMed=18250314; DOI=10.1073/pnas.0708795105;
RA Jia G., Liu X., Owen H.A., Zhao D.;
RT "Signaling of cell fate determination by the TPD1 small protein and EMS1
RT receptor kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2220-2225(2008).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity
CC required for the specification of the correct number of male
CC archesporial initials and for the subsequent specification of tapetal
CC and middle cell layer identities. In seeds, required for enhancing cell
CC size and the rate of embryonic development.
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 TPD1. {ECO:0000269|PubMed:18250314}.
CC -!- INTERACTION:
CC Q9LYN8; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-1640748, EBI-20651385;
CC Q9LYN8; Q6TLJ2: TPD1; NbExp=4; IntAct=EBI-1640748, EBI-1640767;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12154130,
CC ECO:0000269|PubMed:12401166}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12154130, ECO:0000269|PubMed:12401166}.
CC -!- TISSUE SPECIFICITY: Present in young buds, open flowers and siliques
CC but absent from mature leaves and roots. Strongly expressed in the
CC young organ primordia, and as the anthers and ovules developed, became
CC focused in the microsporangia and in the distal and chalazal regions of
CC the ovule. In cv. Landsberg erecta, only expressed in the anthers of
CC young floral buds.
CC -!- DEVELOPMENTAL STAGE: Expressed during the differentiation of
CC microsporocytes and tapetal cells. Also expressed in the meiocytes and
CC young pollen grains until pollen mitosis II.
CC {ECO:0000269|PubMed:12154130, ECO:0000269|PubMed:12401166}.
CC -!- PTM: Autophosphorylates in vitro.
CC -!- MISCELLANEOUS: Some ecotypic variation may occur: in cv. Landsberg
CC erecta, meiocytes of a null mutant fail to undergo cytokinesis while in
CC cv. C24, cytokinesis clearly takes place, with the mutant meiocytes
CC degenerating shortly after the tetrad stage.
CC -!- MISCELLANEOUS: In cv. C24, the gene is expressed in the young ovular
CC primordia, but the protein is not present in these organs.
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; AJ496433; CAD42912.1; -; mRNA.
DR EMBL; AJ488154; CAD32463.1; -; mRNA.
DR EMBL; FJ708773; ACN59364.1; -; mRNA.
DR EMBL; AL163652; CAB87284.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91132.1; -; Genomic_DNA.
DR PIR; T48499; T48499.
DR RefSeq; NP_196345.1; NM_120810.3.
DR AlphaFoldDB; Q9LYN8; -.
DR SMR; Q9LYN8; -.
DR BioGRID; 15898; 29.
DR DIP; DIP-29701N; -.
DR IntAct; Q9LYN8; 27.
DR STRING; 3702.AT5G07280.1; -.
DR PaxDb; Q9LYN8; -.
DR PRIDE; Q9LYN8; -.
DR ProteomicsDB; 224428; -.
DR EnsemblPlants; AT5G07280.1; AT5G07280.1; AT5G07280.
DR GeneID; 830619; -.
DR Gramene; AT5G07280.1; AT5G07280.1; AT5G07280.
DR KEGG; ath:AT5G07280; -.
DR Araport; AT5G07280; -.
DR TAIR; locus:2182870; AT5G07280.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LYN8; -.
DR OMA; GHREFIA; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9LYN8; -.
DR PRO; PR:Q9LYN8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYN8; baseline and differential.
DR Genevisible; Q9LYN8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0019199; F:transmembrane receptor protein kinase activity; ISS:TAIR.
DR GO; GO:0010234; P:anther wall tapetum cell fate specification; IMP:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA: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; 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; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 14.
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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Meiosis; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1192
FT /note="Leucine-rich repeat receptor protein kinase EMS1"
FT /id="PRO_0000024331"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 64..87
FT /note="LRR 1"
FT REPEAT 90..112
FT /note="LRR 2"
FT REPEAT 114..137
FT /note="LRR 3"
FT REPEAT 138..160
FT /note="LRR 4"
FT REPEAT 163..185
FT /note="LRR 5"
FT REPEAT 187..209
FT /note="LRR 6"
FT REPEAT 235..257
FT /note="LRR 7"
FT REPEAT 259..281
FT /note="LRR 8"
FT REPEAT 283..304
FT /note="LRR 9"
FT REPEAT 330..352
FT /note="LRR 10"
FT REPEAT 354..376
FT /note="LRR 11"
FT REPEAT 378..400
FT /note="LRR 12"
FT REPEAT 402..425
FT /note="LRR 13"
FT REPEAT 426..447
FT /note="LRR 14"
FT REPEAT 449..471
FT /note="LRR 15"
FT REPEAT 473..496
FT /note="LRR 16"
FT REPEAT 497..520
FT /note="LRR 17"
FT REPEAT 521..543
FT /note="LRR 18"
FT REPEAT 545..567
FT /note="LRR 19"
FT REPEAT 581..603
FT /note="LRR 20"
FT REPEAT 605..628
FT /note="LRR 21"
FT REPEAT 629..651
FT /note="LRR 22"
FT REPEAT 653..675
FT /note="LRR 23"
FT REPEAT 677..697
FT /note="LRR 24"
FT REPEAT 701..723
FT /note="LRR 25"
FT REPEAT 725..748
FT /note="LRR 26"
FT REPEAT 749..772
FT /note="LRR 27"
FT REPEAT 773..795
FT /note="LRR 28"
FT DOMAIN 917..1192
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1043
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 923..931
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 945
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 914
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 990
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1085
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 4
FT /note="L->LIL: In rev.1; no effect."
FT /evidence="ECO:0000269|PubMed:12154130,
FT ECO:0000269|PubMed:12401166"
FT MUTAGEN 4
FT /note="L->LSIL: In rev.2; no effect."
FT /evidence="ECO:0000269|PubMed:12154130,
FT ECO:0000269|PubMed:12401166"
FT MUTAGEN 104
FT /note="K->N: In exs-2; male sterility."
FT /evidence="ECO:0000269|PubMed:12154130,
FT ECO:0000269|PubMed:12401166"
FT MUTAGEN 1185
FT /note="V->E: In exs-1; male sterility."
FT /evidence="ECO:0000269|PubMed:12154130,
FT ECO:0000269|PubMed:12401166"
FT CONFLICT 131..132
FT /note="RL -> SR (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="Q -> E (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="P -> L (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="I -> T (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="H -> Q (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> S (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="M -> I (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="H -> R (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="E -> D (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="A -> V (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="M -> I (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="V -> I (in Ref. 1; CAD42912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1192 AA; 129800 MW; D02C8B8FF6B09F7D CRC64;
MAFLTALFLF LFFSFSSSAI VDLSSETTSL ISFKRSLENP SLLSSWNVSS SASHCDWVGV
TCLLGRVNSL SLPSLSLRGQ IPKEISSLKN LRELCLAGNQ FSGKIPPEIW NLKHLQTLDL
SGNSLTGLLP RLLSELPQLL YLDLSDNHFS GSLPPSFFIS LPALSSLDVS NNSLSGEIPP
EIGKLSNLSN LYMGLNSFSG QIPSEIGNIS LLKNFAAPSC FFNGPLPKEI SKLKHLAKLD
LSYNPLKCSI PKSFGELHNL SILNLVSAEL IGLIPPELGN CKSLKSLMLS FNSLSGPLPL
ELSEIPLLTF SAERNQLSGS LPSWMGKWKV LDSLLLANNR FSGEIPHEIE DCPMLKHLSL
ASNLLSGSIP RELCGSGSLE AIDLSGNLLS GTIEEVFDGC SSLGELLLTN NQINGSIPED
LWKLPLMALD LDSNNFTGEI PKSLWKSTNL MEFTASYNRL EGYLPAEIGN AASLKRLVLS
DNQLTGEIPR EIGKLTSLSV LNLNANMFQG KIPVELGDCT SLTTLDLGSN NLQGQIPDKI
TALAQLQCLV LSYNNLSGSI PSKPSAYFHQ IEMPDLSFLQ HHGIFDLSYN RLSGPIPEEL
GECLVLVEIS LSNNHLSGEI PASLSRLTNL TILDLSGNAL TGSIPKEMGN SLKLQGLNLA
NNQLNGHIPE SFGLLGSLVK LNLTKNKLDG PVPASLGNLK ELTHMDLSFN NLSGELSSEL
STMEKLVGLY IEQNKFTGEI PSELGNLTQL EYLDVSENLL SGEIPTKICG LPNLEFLNLA
KNNLRGEVPS DGVCQDPSKA LLSGNKELCG RVVGSDCKIE GTKLRSAWGI AGLMLGFTII
VFVFVFSLRR WAMTKRVKQR DDPERMEESR LKGFVDQNLY FLSGSRSREP LSINIAMFEQ
PLLKVRLGDI VEATDHFSKK NIIGDGGFGT VYKACLPGEK TVAVKKLSEA KTQGNREFMA
EMETLGKVKH PNLVSLLGYC SFSEEKLLVY EYMVNGSLDH WLRNQTGMLE VLDWSKRLKI
AVGAARGLAF LHHGFIPHII HRDIKASNIL LDGDFEPKVA DFGLARLISA CESHVSTVIA
GTFGYIPPEY GQSARATTKG DVYSFGVILL ELVTGKEPTG PDFKESEGGN LVGWAIQKIN
QGKAVDVIDP LLVSVALKNS QLRLLQIAML CLAETPAKRP NMLDVLKALK EI
