PBL2_ARATH
ID PBL2_ARATH Reviewed; 426 AA.
AC O49839;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable serine/threonine-protein kinase PBL2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 2 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein kinase 2A {ECO:0000305};
GN Name=PBL2 {ECO:0000303|PubMed:20413097};
GN Synonyms=APK2A {ECO:0000303|PubMed:9150601},
GN KIN1 {ECO:0000303|PubMed:21219905};
GN OrderedLocusNames=At1g14370 {ECO:0000312|Araport:AT1G14370};
GN ORFNames=F14L17.14 {ECO:0000312|EMBL:AAF43937.1};
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], REGULATION BY AGAMOUS, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9150601; DOI=10.1093/oxfordjournals.pcp.a029160;
RA Ito T., Takahashi N., Shimura Y., Okada K.;
RT "A serine/threonine protein kinase gene isolated by an in vivo binding
RT procedure using the Arabidopsis floral homeotic gene product, AGAMOUS.";
RL Plant Cell Physiol. 38:248-258(1997).
RN [2]
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 [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 FUNCTION, INTERACTION WITH FLS2, INDUCTION BY FLAGELLIN, GENE FAMILY,
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [6]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2, AND MYRISTOYLATION AT GLY-2.
RX PubMed=21219905; DOI=10.1016/j.febslet.2011.01.001;
RA Stael S., Bayer R.G., Mehlmer N., Teige M.;
RT "Protein N-acylation overrides differing targeting signals.";
RL FEBS Lett. 585:517-522(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
RN [8]
RP FUNCTION, MUTAGENESIS OF LYS-124; ASP-219; GLY-247; SER-253; THR-254 AND
RP TYR-262, DISRUPTION PHENOTYPE, SUBUNIT, URIDYLYLATION BY XANTHOMONAS
RP CAMPESTRIS EFFECTOR AVRAC/XOPAC, URIDYLYLATION AT SER-253 AND THR-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) IN COMPLEX WITH ATP
RP ANALOGS, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=30948527; DOI=10.1126/science.aav5870;
RA Wang J., Hu M., Wang J., Qi J., Han Z., Wang G., Qi Y., Wang H.-W.,
RA Zhou J.-M., Chai J.;
RT "Reconstitution and structure of a plant NLR resistosome conferring
RT immunity.";
RL Science 364:0-0(2019).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH ATP
RP ANALOGS, FUNCTION, SUBUNIT, URIDYLYLATION AT SER-253 AND THR-254, AND
RP INTERACTION WITH RKS1.
RC STRAIN=cv. Columbia;
RX PubMed=30948526; DOI=10.1126/science.aav5868;
RA Wang J., Wang J., Hu M., Wu S., Qi J., Wang G., Han Z., Qi Y., Gao N.,
RA Wang H.-W., Zhou J.-M., Chai J.;
RT "Ligand-triggered allosteric ADP release primes a plant NLR complex.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Involved in disease resistance signaling (PubMed:20413097,
CC PubMed:23951354, PubMed:26355215). Contributes to pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense
CC responses downstream of FLS2 (PubMed:20413097). Acts as a BIK1 decoy
CC and enables Xanthomonas campestris AvrAC/XopAC detection; X.campestris
CC effector AvrAC/XopAC-mediated uridylylation promotes the formation of a
CC complex with RKS1 and RPP13L4/ZAR1 which, in turn, activates effector-
CC triggered immunity (ETI) against X.campestris (PubMed:23951354,
CC PubMed:26355215, PubMed:30948526). Promotes, when uridylylated by
CC AvrAC/XopAC, the release of ADP from the inactive RKS1-ZAR1 complex,
CC thus activating the resistosome (PubMed:30948526).
CC {ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23951354,
CC ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:30948526}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with FLS2 (PubMed:20413097). Interacts with the
CC Xanthomonas campestris effector XopAC/AvrAC; the recognition of
CC X.campestris effector XopAC/AvrAC requires the presence of RKS1 and
CC RPP13L4/ZAR1 (PubMed:23951354, PubMed:26355215). Component of a stable
CC high-order oligomeric complex made of RKS1 and RPP13L4/ZAR1 which
CC recruits X.campestris effector XopAC/AvrAC-mediated uridylylated PBL2
CC in the presence of ATP to form a wheel-like pentameric resistosome;
CC this complex triggers immunity toward X.campestris in vascular tissues
CC (PubMed:26355215, PubMed:30948527, PubMed:30948526). Binds to RKS1 when
CC uridylylated (PubMed:30948526). {ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:26355215,
CC ECO:0000269|PubMed:30948526, ECO:0000269|PubMed:30948527}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905};
CC Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus
CC {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the
CC plasma membrane. {ECO:0000269|PubMed:21219905}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves, moderately in roots,
CC and barely in flowers, mostly in pedicels.
CC {ECO:0000269|PubMed:9150601}.
CC -!- INDUCTION: Negatively regulated by AGAMOUS (AG) in floral organ
CC primordia (PubMed:9150601). Induced by flagellin (flg22)
CC (PubMed:20413097). {ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:9150601}.
CC -!- PTM: Uridylylated at Ser-253 and Thr-254 by Xanthomonas campestris
CC effector AvrAC/XopAC; this uridylylation is necessary for specific
CC recruitment to RKS1 and to trigger immunity.
CC {ECO:0000269|PubMed:26355215}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20413097). Increased sensitivity to the pathogenic
CC biotrophic bacteria Xanthomonas campestris pv. campestris (Xcc) in
CC vascular tissues (PubMed:26355215). {ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:26355215}.
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; D88206; BAA24694.1; -; mRNA.
DR EMBL; AC012188; AAF43937.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29153.1; -; Genomic_DNA.
DR EMBL; AF334731; AAG50109.1; -; mRNA.
DR EMBL; AY059894; AAL24376.1; -; mRNA.
DR PIR; T52285; T52285.
DR RefSeq; NP_172889.1; NM_101304.4.
DR PDB; 6J5T; EM; 3.40 A; A/D/I/J/M=1-426.
DR PDB; 6J5U; EM; 3.90 A; C=1-426.
DR PDB; 6J5V; EM; 4.25 A; C=1-426.
DR PDB; 6J6I; EM; 3.70 A; A=1-426.
DR PDBsum; 6J5T; -.
DR PDBsum; 6J5U; -.
DR PDBsum; 6J5V; -.
DR PDBsum; 6J6I; -.
DR AlphaFoldDB; O49839; -.
DR SMR; O49839; -.
DR BioGRID; 23239; 5.
DR IntAct; O49839; 5.
DR STRING; 3702.AT1G14370.1; -.
DR iPTMnet; O49839; -.
DR PaxDb; O49839; -.
DR PRIDE; O49839; -.
DR ProteomicsDB; 236279; -.
DR EnsemblPlants; AT1G14370.1; AT1G14370.1; AT1G14370.
DR GeneID; 837999; -.
DR Gramene; AT1G14370.1; AT1G14370.1; AT1G14370.
DR KEGG; ath:AT1G14370; -.
DR Araport; AT1G14370; -.
DR TAIR; locus:2012492; AT1G14370.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; O49839; -.
DR OMA; GTKHTQM; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O49839; -.
DR PRO; PR:O49839; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49839; baseline and differential.
DR Genevisible; O49839; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0030957; F:Tat protein binding; IPI:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF07714; PK_Tyr_Ser-Thr; 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 3D-structure; ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:21219905"
FT CHAIN 2..426
FT /note="Probable serine/threonine-protein kinase PBL2"
FT /id="PRO_0000389476"
FT DOMAIN 86..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:30948526, ECO:0000269|PubMed:30948527,
FT ECO:0007744|PDB:6J5T, ECO:0007744|PDB:6J5U,
FT ECO:0007744|PDB:6J5V, ECO:0007744|PDB:6J6I"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 169
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 253
FT /note="O-UMP-serine"
FT /evidence="ECO:0000269|PubMed:26355215,
FT ECO:0000269|PubMed:30948526"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 254
FT /note="O-UMP-threonine"
FT /evidence="ECO:0000269|PubMed:26355215,
FT ECO:0000269|PubMed:30948526"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 267
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:21219905"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 2
FT /note="G->A: Drastic reduction of plasma membrane
FT localization and strong increase of nuclear localization."
FT /evidence="ECO:0000269|PubMed:21219905"
FT MUTAGEN 124
FT /note="K->E: Normal uridylylation and cell death induction
FT in response to the Xanthomonas campestris effector
FT XopAC/AvrAC in the presence of RKS1 and RPP13L4/ZAR1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 219
FT /note="D->A: Normal cell death induction in response to the
FT Xanthomonas campestris effector XopAC/AvrAC in the presence
FT of RKS1 and RPP13L4/ZAR1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 247
FT /note="G->R: Normal cell death induction in response to the
FT Xanthomonas campestris effector XopAC/AvrAC in the presence
FT of RKS1 and RPP13L4/ZAR1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 253
FT /note="S->A: Increased sensitivity to the pathogenic
FT biotrophic bacteria Xanthomonas campestris pv. campestris
FT (Xcc) in vascular tissues. Lost ability to trigger cell
FT death in response to the Xanthomonas campestris effector
FT XopAC/AvrAC in the presence of PBL2 and RKS1. Impaired
FT Xanthomonas campestris effector AvrAC/XopAC-mediated
FT uridylylation; when associated with A-254."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 254
FT /note="T->A: Increased sensitivity to the pathogenic
FT biotrophic bacteria Xanthomonas campestris pv. campestris
FT (Xcc) in vascular tissues. Lost ability to trigger cell
FT death in response to the Xanthomonas campestris effector
FT XopAC/AvrAC in the presence of PBL2 and RKS1. Impaired
FT Xanthomonas campestris effector AvrAC/XopAC-mediated
FT uridylylation; when associated with A-253."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 262
FT /note="Y->A: Normal cell death induction in response to the
FT Xanthomonas campestris effector XopAC/AvrAC in the presence
FT of RKS1 and RPP13L4/ZAR1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:6J5T"
SQ SEQUENCE 426 AA; 46296 MW; 51A7670B74C24DD3 CRC64;
MGNCLDSSAK VDNSNHSPHA NSASSGSKVS SKTSRSTGPS GLSTTSYSTD SSFGPLPTLR
TEGEILSSPN LKAFTFNELK NATKNFRQDN LLGEGGFGCV FKGWIDQTSL TASRPGSGIV
VAVKQLKPEG FQGHKEWLTE VNYLGQLSHP NLVLLVGYCA EGENRLLVYE FMPKGSLENH
LFRRGAQPLT WAIRMKVAVG AAKGLTFLHE AKSQVIYRDF KAANILLDAD FNAKLSDFGL
AKAGPTGDNT HVSTKVIGTH GYAAPEYVAT GRLTAKSDVY SFGVVLLELI SGRRAMDNSN
GGNEYSLVDW ATPYLGDKRK LFRIMDTKLG GQYPQKGAFT AANLALQCLN PDAKLRPKMS
EVLVTLEQLE SVAKPGTKHT QMESPRFHHS SVMQKSPVRY SHDRPLLHMT PGASPLPSYT
QSPRVR
