M2K3_ARATH
ID M2K3_ARATH Reviewed; 520 AA.
AC O80396;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitogen-activated protein kinase kinase 3 {ECO:0000303|PubMed:10048483, ECO:0000303|PubMed:12119167};
DE Short=AtMKK3 {ECO:0000303|PubMed:10048483, ECO:0000303|PubMed:12119167};
DE Short=MAP kinase kinase 3 {ECO:0000303|PubMed:10048483, ECO:0000303|PubMed:12119167};
DE EC=2.7.12.2;
GN Name=MKK3 {ECO:0000303|PubMed:10048483, ECO:0000303|PubMed:12119167};
GN OrderedLocusNames=At5g40440 {ECO:0000312|Araport:AT5G40440};
GN ORFNames=MPO12.19 {ECO:0000312|EMBL:BAB11601.1},
GN MPO12_150 {ECO:0000312|EMBL:BAB11601.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10048483; DOI=10.1093/dnares/5.6.341;
RA Ichimura K., Mizoguchi T., Hayashida N., Seki M., Shinozaki K.;
RT "Molecular cloning and characterization of three cDNAs encoding putative
RT mitogen-activated protein kinase kinases (MAPKKs) in Arabidopsis
RT thaliana.";
RL DNA Res. 5:341-348(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP GENE FAMILY, AND 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 [7]
RP GENE FAMILY.
RX PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT families.";
RL Trends Plant Sci. 11:192-198(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF SER-235 AND THR-241, AND PHOSPHORYLATION AT
RP SER-235 AND THR-241.
RX PubMed=17369371; DOI=10.1105/tpc.106.046581;
RA Takahashi F., Yoshida R., Ichimura K., Mizoguchi T., Seo S., Yonezawa M.,
RA Maruyama K., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "The mitogen-activated protein kinase cascade MKK3-MPK6 is an important
RT part of the jasmonate signal transduction pathway in Arabidopsis.";
RL Plant Cell 19:805-818(2007).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, INDUCTION BY PATHOGEN, MUTAGENESIS OF
RP SER-235 AND THR-241, INTERACTION WITH MPK1; MPK2 AND MPK7, AND
RP PHOSPHORYLATION AT SER-235 AND THR-241.
RX PubMed=17933903; DOI=10.1105/tpc.106.050039;
RA Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A.,
RA Teige M., Hirt H.;
RT "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream
RT of group C mitogen-activated protein kinases and participates in pathogen
RT signaling.";
RL Plant Cell 19:3266-3279(2007).
RN [10]
RP INTERACTION WITH MPK1; MPK2; MPK7 AND MPK14.
RX PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL Plant Signal. Behav. 3:1037-1041(2008).
RN [11]
RP INTERACTION WITH HOPF2.
RX PubMed=20571112; DOI=10.1105/tpc.110.075697;
RA Wang Y., Li J., Hou S., Wang X., Li Y., Ren D., Chen S., Tang X.,
RA Zhou J.M.;
RT "A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis
RT mitogen-activated protein kinase kinases.";
RL Plant Cell 22:2033-2044(2010).
RN [12]
RP FUNCTION, MUTAGENESIS OF SER-235 AND THR-241, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION AT SER-235 AND THR-241.
RX PubMed=21419340; DOI=10.1016/j.molcel.2011.02.029;
RA Takahashi F., Mizoguchi T., Yoshida R., Ichimura K., Shinozaki K.;
RT "Calmodulin-dependent activation of MAP kinase for ROS homeostasis in
RT Arabidopsis.";
RL Mol. Cell 41:649-660(2011).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MAPKKK17 AND MAPKKK18.
RC STRAIN=cv. Columbia;
RX PubMed=25720833; DOI=10.1111/tpj.12808;
RA Danquah A., de Zelicourt A., Boudsocq M., Neubauer J., Frei Dit Frey N.,
RA Leonhardt N., Pateyron S., Gwinner F., Tamby J.P., Ortiz-Masia D.,
RA Marcote M.J., Hirt H., Colcombet J.;
RT "Identification and characterization of an ABA-activated MAP kinase cascade
RT in Arabidopsis thaliana.";
RL Plant J. 82:232-244(2015).
RN [14]
RP INTERACTION WITH MAPKKK17; MPK1; MPK2 AND MPK7.
RC STRAIN=cv. Columbia;
RX PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT senescence via its kinase activity.";
RL Plant Mol. Biol. 87:565-575(2015).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH
RP MAPKKK20, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28848569; DOI=10.3389/fpls.2017.01352;
RA Benhamman R., Bai F., Drory S.B., Loubert-Hudon A., Ellis B., Matton D.P.;
RT "The Arabidopsis mitogen-activated protein kinase kinase kinase 20 (MKKK20)
RT acts upstream of MKK3 and MPK18 in two separate signaling pathways involved
RT in root microtubule functions.";
RL Front. Plant Sci. 8:1352-1352(2017).
RN [16]
RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES.
RX PubMed=30349547; DOI=10.3389/fpls.2018.01387;
RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.;
RT "Mitogen-activated protein kinase cascades in plant hormone signaling.";
RL Front. Plant Sci. 9:1387-1387(2018).
RN [17]
RP INTERACTION WITH MAPKKK20, AND SUBCELLULAR LOCATION.
RX PubMed=30081740; DOI=10.1080/15592324.2018.1503498;
RA Bai F., Matton D.P.;
RT "The Arabidopsis mitogen-activated protein kinase kinase kinase 20 (MKKK20)
RT C-terminal domain interacts with MKK3 and harbors a typical DEF mammalian
RT MAP kinase docking site.";
RL Plant Signal. Behav. 13:E1503498-E1503498(2018).
CC -!- FUNCTION: MKK3-MPK6 module plays an important role in the jasmonate
CC signal transduction pathway through the negative regulation of
CC MYC2/JIN1 expression. Activates by phosphorylation the downstream MPK6,
CC MPK7 and MPK8. MKK3-MPK7 module acts as a positive regulator of PR1
CC gene expression. MKK3-MPK8 module negatively regulates ROS accumulation
CC through controlling expression of the RBOHD gene. Component of the
CC abscisic acid (ABA) signaling pathway that may act as ABA signal
CC transducer in the context of abiotic stresses. Activator of the C group
CC MAP kinases. Activates MPK7 in response to ABA (PubMed:25720833).
CC Mitogen-activated protein kinase (MAPK) that is specifically regulated
CC by MAPKKK20 and mediates signaling that regulates cortical microtubule
CC functions (PubMed:28848569). {ECO:0000269|PubMed:17369371,
CC ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340,
CC ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:28848569}.
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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SUBUNIT: Interacts with MPK1, MPK2 and MPK7 (PubMed:17933903,
CC PubMed:19513235, PubMed:25680457). Interacts with P.syringae type III
CC effector HopF2 (PubMed:20571112). Interacts with MPK14
CC (PubMed:19513235). Binds to MAPKKK17 and MAPKKK18 (PubMed:25720833,
CC PubMed:25680457). Binds to MAPKKK20 (PubMed:28848569, PubMed:30081740).
CC {ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:19513235,
CC ECO:0000269|PubMed:20571112, ECO:0000269|PubMed:25680457,
CC ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:28848569,
CC ECO:0000269|PubMed:30081740}.
CC -!- INTERACTION:
CC O80396; A0A384KVW9: At3g50800; NbExp=3; IntAct=EBI-2358337, EBI-25520138;
CC O80396; Q39021: MPK1; NbExp=4; IntAct=EBI-2358337, EBI-1238932;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28848569}. Cytoplasm
CC {ECO:0000269|PubMed:28848569, ECO:0000269|PubMed:30081740}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in roots, seedlings, flower buds, flowers and siliques.
CC {ECO:0000269|PubMed:10048483, ECO:0000269|PubMed:21419340,
CC ECO:0000269|PubMed:28848569}.
CC -!- INDUCTION: By Pseudomonas syringae pv tomato strain DC3000 infection.
CC {ECO:0000269|PubMed:17933903}.
CC -!- PTM: Phosphorylation at Ser-235 and Thr-241 by MAP kinase kinase
CC kinases positively regulates kinase activity (Probable). Phosphorylated
CC by MAPKKK20 (PubMed:28848569). {ECO:0000269|PubMed:28848569,
CC ECO:0000305|PubMed:17369371, ECO:0000305|PubMed:17933903,
CC ECO:0000305|PubMed:21419340}.
CC -!- DISRUPTION PHENOTYPE: More sensitive to Pseudomonas syringae pv. tomato
CC DC3000 infection (PubMed:17933903). Hypersensitivity to abscisic acid
CC (ABA) in germination and root elongation (PubMed:25720833). Short roots
CC with abnormal twisting (e.g. leftward skewing) in media containing
CC microtubule-disrupting drugs (e.g. oryzalin) (PubMed:28848569).
CC {ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:25720833,
CC ECO:0000269|PubMed:28848569}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB015314; BAA28829.1; -; mRNA.
DR EMBL; AB006702; BAB11601.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94548.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70658.1; -; Genomic_DNA.
DR EMBL; AK117136; BAC41814.1; -; mRNA.
DR EMBL; BT006481; AAP21289.1; -; mRNA.
DR PIR; T51338; T51338.
DR RefSeq; NP_001318713.1; NM_001344328.1.
DR RefSeq; NP_198860.1; NM_123408.3.
DR AlphaFoldDB; O80396; -.
DR SMR; O80396; -.
DR BioGRID; 19293; 8.
DR IntAct; O80396; 6.
DR STRING; 3702.AT5G40440.1; -.
DR iPTMnet; O80396; -.
DR PaxDb; O80396; -.
DR PRIDE; O80396; -.
DR ProteomicsDB; 238546; -.
DR EnsemblPlants; AT5G40440.1; AT5G40440.1; AT5G40440.
DR EnsemblPlants; AT5G40440.4; AT5G40440.4; AT5G40440.
DR GeneID; 834042; -.
DR Gramene; AT5G40440.1; AT5G40440.1; AT5G40440.
DR Gramene; AT5G40440.4; AT5G40440.4; AT5G40440.
DR KEGG; ath:AT5G40440; -.
DR Araport; AT5G40440; -.
DR TAIR; locus:2170578; AT5G40440.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O80396; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; O80396; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:O80396; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O80396; baseline and differential.
DR Genevisible; O80396; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0009866; P:induced systemic resistance, ethylene mediated signaling pathway; IEP:TAIR.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IEP:TAIR.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR CDD; cd00780; NTF2; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
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; SSF54427; SSF54427; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 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 Abscisic acid signaling pathway; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..520
FT /note="Mitogen-activated protein kinase kinase 3"
FT /id="PRO_0000428622"
FT DOMAIN 83..339
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 366..516
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S7U9"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:17369371,
FT ECO:0000305|PubMed:17933903, ECO:0000305|PubMed:21419340"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:17369371,
FT ECO:0000305|PubMed:17933903, ECO:0000305|PubMed:21419340"
FT MOD_RES 245
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT MUTAGEN 235
FT /note="S->D: Constitutively active; when associated with D-
FT 241."
FT /evidence="ECO:0000269|PubMed:17369371,
FT ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT MUTAGEN 235
FT /note="S->E: Constitutively active; when associated with E-
FT 241."
FT /evidence="ECO:0000269|PubMed:17369371,
FT ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT MUTAGEN 241
FT /note="T->D: Constitutively active; when associated with D-
FT 235."
FT /evidence="ECO:0000269|PubMed:17369371,
FT ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT MUTAGEN 241
FT /note="T->E: Constitutively active; when associated with E-
FT 235."
FT /evidence="ECO:0000269|PubMed:17369371,
FT ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
SQ SEQUENCE 520 AA; 57529 MW; 9CD63397CCF38AA2 CRC64;
MAALEELKKK LSPLFDAEKG FSSSSSLDPN DSYLLSDGGT VNLLSRSYGV YNFNELGLQK
CTSSHVDESE SSETTYQCAS HEMRVFGAIG SGASSVVQRA IHIPNHRILA LKKINIFERE
KRQQLLTEIR TLCEAPCHEG LVDFHGAFYS PDSGQISIAL EYMNGGSLAD ILKVTKKIPE
PVLSSLFHKL LQGLSYLHGV RHLVHRDIKP ANLLINLKGE PKITDFGISA GLENSMAMCA
TFVGTVTYMS PERIRNDSYS YPADIWSLGL ALFECGTGEF PYIANEGPVN LMLQILDDPS
PTPPKQEFSP EFCSFIDACL QKDPDARPTA DQLLSHPFIT KHEKERVDLA TFVQSIFDPT
QRLKDLADML TIHYYSLFDG FDDLWHHAKS LYTETSVFSF SGKHNTGSTE IFSALSDIRN
TLTGDLPSEK LVHVVEKLHC KPCGSGGVII RAVGSFIVGN QFLICGDGVQ AEGLPSFKDL
GFDVASRRVG RFQEQFVVES GDLIGKYFLA KQELYITNLD
