M3K1_ARATH
ID M3K1_ARATH Reviewed; 608 AA.
AC Q39008; O81470; Q39020; Q8W4N5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 1;
DE Short=ARAKIN;
DE Short=AtMEKK1;
DE Short=MAP kinase kinase kinase 1;
DE EC=2.7.11.25 {ECO:0000269|PubMed:23857079};
GN Name=MEKK1; OrderedLocusNames=At4g08500; ORFNames=T15F16.5;
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 [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8570631; DOI=10.1073/pnas.93.2.765;
RA Mizoguchi T., Irie K., Hirayama T., Hayashida N., Yamaguchi-Shinozaki K.,
RA Matsumoto K., Shinozaki K.;
RT "A gene encoding a mitogen-activated protein kinase kinase kinase is
RT induced simultaneously with genes for a mitogen-activated protein kinase
RT and an S6 ribosomal protein kinase by touch, cold, and water stress in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:765-769(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-608.
RX PubMed=8597596; DOI=10.1016/0167-4781(95)00233-2;
RA Covic L., Lew R.R.;
RT "Arabidopsis thaliana cDNA isolated by functional complementation shows
RT homology to serine/threonine protein kinases.";
RL Biochim. Biophys. Acta 1305:125-129(1996).
RN [6]
RP INDUCTION.
RX PubMed=10556579; DOI=10.1016/s0167-4889(99)00096-8;
RA Covic L., Silva N.F., Lew R.R.;
RT "Functional characterization of ARAKIN (ATMEKK1): a possible mediator in an
RT osmotic stress response pathway in higher plants.";
RL Biochim. Biophys. Acta 1451:242-254(1999).
RN [7]
RP SUBUNIT, AND INTERACTION WITH MKK1; MMK2 AND MPK4.
RX PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
RA Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J., Matsumoto K.,
RA Shinozaki K.;
RT "Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and
RT analysis of a MAP kinase cascade in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 253:532-543(1998).
RN [8]
RP FUNCTION.
RX PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
RN [9]
RP NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [10]
RP FUNCTION.
RX PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
RA Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
RA Dangl J.L., Hirt H.;
RT "The MKK2 pathway mediates cold and salt stress signaling in Arabidopsis.";
RL Mol. Cell 15:141-152(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH MKK1; MKK2 AND MPK4.
RX PubMed=18982020; DOI=10.1038/cr.2008.300;
RA Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
RT "MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein
RT kinase cascade to regulate innate immunity in plants.";
RL Cell Res. 18:1190-1198(2008).
RN [12]
RP INTERACTION WITH CRLK1, AND SUBCELLULAR LOCATION.
RX PubMed=20724845; DOI=10.4161/psb.5.8.12225;
RA Yang T., Shad Ali G., Yang L., Du L., Reddy A.S., Poovaiah B.W.;
RT "Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts with
RT MEKK1 in plants.";
RL Plant Signal. Behav. 5:991-994(2010).
RN [13]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
RA Furuya T., Matsuoka D., Nanmori T.;
RT "Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as a
RT part of the cold stress response.";
RL J. Plant Res. 126:833-840(2013).
RN [14]
RP INTERACTION WITH RACK1A; RACK1B AND RACK1C.
RX PubMed=25731164; DOI=10.1038/nature14243;
RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S.,
RA Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.;
RT "Pathogen-secreted proteases activate a novel plant immune pathway.";
RL Nature 521:213-216(2015).
CC -!- FUNCTION: The MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway
CC that modulates the expression of genes responding to biotic and abiotic
CC stresses and also plays an important role in pathogen defense by
CC negatively regulating innate immunity. Involved in the innate immune
CC MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6)
CC downstream of bacterial flagellin receptor FLS2. May be involved in the
CC cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1,
CC MKK1/MKK2 and MPK4/MPK6). Activates by phosphorylation the downstream
CC MKK2, MKK4 and MKK5 in a calcium-dependent manner.
CC {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15225555,
CC ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:23857079}.
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=2.7.11.25;
CC Evidence={ECO:0000269|PubMed:23857079};
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=2.7.11.25; Evidence={ECO:0000269|PubMed:23857079};
CC -!- ACTIVITY REGULATION: Activated by cold via CRLK1-mediated
CC phosphorylation and leading to elevated kinase activity towards MKK2.
CC {ECO:0000269|PubMed:23857079}.
CC -!- SUBUNIT: Interacts with MKK1, MMK2 and MPK4. May form a ternary complex
CC composed of MEKK1 and MKK1/MKK2 and MPK4 (PubMed:18982020,
CC PubMed:9878570). Interacts with RACK1A, RACK1B and RACK1C
CC (PubMed:25731164). Binds to CRLK1 (PubMed:20724845).
CC {ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:20724845,
CC ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:9878570}.
CC -!- INTERACTION:
CC Q39008; Q94A06: MKK1; NbExp=4; IntAct=EBI-994439, EBI-994464;
CC Q39008; Q9SUP6: WRKY53; NbExp=5; IntAct=EBI-994439, EBI-1235980;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20724845}.
CC Endosome {ECO:0000269|PubMed:20724845}.
CC -!- INDUCTION: By touch, cold and salinity stress.
CC {ECO:0000269|PubMed:10556579, ECO:0000269|PubMed:8570631}.
CC -!- PTM: Phosphorylated by CRLK1 in response to cold.
CC {ECO:0000269|PubMed:23857079}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99196.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA99196.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; D50468; BAA09057.1; -; mRNA.
DR EMBL; AF076275; AAC28196.1; -; Genomic_DNA.
DR EMBL; AL161511; CAB77975.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82651.1; -; Genomic_DNA.
DR EMBL; AY062459; AAL32537.1; -; mRNA.
DR EMBL; BT000116; AAN15435.1; -; mRNA.
DR EMBL; L43125; AAA99196.1; ALT_SEQ; Genomic_DNA.
DR PIR; T01833; T01833.
DR RefSeq; NP_192590.1; NM_116919.4.
DR AlphaFoldDB; Q39008; -.
DR SMR; Q39008; -.
DR BioGRID; 11709; 9.
DR IntAct; Q39008; 3.
DR STRING; 3702.AT4G08500.1; -.
DR iPTMnet; Q39008; -.
DR PaxDb; Q39008; -.
DR PRIDE; Q39008; -.
DR ProteomicsDB; 238790; -.
DR EnsemblPlants; AT4G08500.1; AT4G08500.1; AT4G08500.
DR GeneID; 826409; -.
DR Gramene; AT4G08500.1; AT4G08500.1; AT4G08500.
DR KEGG; ath:AT4G08500; -.
DR Araport; AT4G08500; -.
DR TAIR; locus:2133559; AT4G08500.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_2_6_1; -.
DR InParanoid; Q39008; -.
DR OMA; HIDYEAA; -.
DR OrthoDB; 630495at2759; -.
DR PhylomeDB; Q39008; -.
DR BRENDA; 2.7.11.25; 399.
DR PRO; PR:Q39008; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39008; baseline and differential.
DR Genevisible; Q39008; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:TAIR.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:1902065; P:response to L-glutamate; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IDA:TAIR.
DR GO; GO:0010449; P:root meristem growth; IGI:TAIR.
DR GO; GO:0022622; P:root system development; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 ATP-binding; Cell membrane; Endosome; Immunity; Innate immunity; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..608
FT /note="Mitogen-activated protein kinase kinase kinase 1"
FT /id="PRO_0000245826"
FT DOMAIN 333..587
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..325
FT /note="Regulatory region"
FT /evidence="ECO:0000269|PubMed:9878570"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..234
FT /note="Binding with MPK4"
FT /evidence="ECO:0000269|PubMed:9878570"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 339..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81472"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81472"
FT CONFLICT 39
FT /note="D -> A (in Ref. 1; AAC28196)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> L (in Ref. 4; AAL32537/AAN15435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 66024 MW; 70C1A1C314E2DFDD CRC64;
MDRILARMKK STGRRGGDKN ITPVRRLERR DAARNINYDA ASCSSSSAED LSVSTSSLMT
RSLEFPEPTS FRIGGGVGEM DRIYRSLGVS GPDDLAISFD AWEACKKRSS SDVVNRFKSF
DLDKVRDQDL SEEGPSGVVV GSDSMNHKVQ GQDLSEAGPS GGIVTELSEI GNLITPVDRL
VADGVVENRR VMERTPTIVK SKGYLVPNNV VAVGVGVGGG IKGLRPPVLK PPPAMKRPPI
DHRGSSWDFL THFAPSETVK RPSSSSSSSE DGCDEEEGKE EEAEAEEMGA RFIQLGDTAD
ETCSFTTNEG DSSSTVSNTS PIYPDGGAII TSWQKGQLLG RGSFGSVYEG ISGDGDFFAV
KEVSLLDQGS QAQECIQQLE GEIKLLSQLQ HQNIVRYRGT AKDGSNLYIF LELVTQGSLL
KLYQRYQLRD SVVSLYTRQI LDGLKYLHDK GFIHRDIKCA NILVDANGAV KLADFGLAKV
SKFNDIKSCK GTPFWMAPEV INRKDSDGYG SPADIWSLGC TVLEMCTGQI PYSDLEPVQA
LFRIGRGTLP EVPDTLSLDA RLFILKCLKV NPEERPTAAE LLNHPFVRRP LPSVGSGGSG
SASPLLRR
