JAR1_ARATH
ID JAR1_ARATH Reviewed; 575 AA.
AC Q9SKE2; C0Z3D1; Q42147; Q56YY1; Q949V9; Q9LKI2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Jasmonoyl--L-amino acid synthetase JAR1 {ECO:0000305};
DE EC=6.3.2.52 {ECO:0000269|PubMed:18247047};
DE AltName: Full=Jasmonate-amino acid synthetase JAR1 {ECO:0000305};
DE AltName: Full=Jasmonic acid-amido synthetase JAR1 {ECO:0000305};
DE AltName: Full=Protein FAR-RED INSENSITIVE 219 {ECO:0000303|PubMed:10921909};
DE AltName: Full=Protein JASMONATE RESISTANT 1 {ECO:0000303|PubMed:11607311};
GN Name=JAR1 {ECO:0000303|PubMed:11607311};
GN Synonyms=FIN219 {ECO:0000303|PubMed:10921909}; OrderedLocusNames=At2g46370;
GN ORFNames=F11C10.6;
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION BY AUXIN, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10921909;
RA Hsieh H.-L., Okamoto H., Wang M., Ang L.-H., Matsui M., Goodman H.,
RA Deng X.W.;
RT "FIN219, an auxin-regulated gene, defines a link between phytochrome A and
RT the downstream regulator COP1 in light control of Arabidopsis
RT development.";
RL Genes Dev. 14:1958-1970(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-129 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Protoplast;
RA Philipps G., Gigot C.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-575 (ISOFORM 1/2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11607311; DOI=10.1073/pnas.89.15.6837;
RA Staswick P.E., Su W., Howell S.H.;
RT "Methyl jasmonate inhibition of root growth and induction of a leaf protein
RT are decreased in an Arabidopsis thaliana mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6837-6840(1992).
RN [9]
RP FUNCTION IN INDUCED SYSTEMIC RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9724702; DOI=10.2307/3870620;
RA Pieterse C.M.J., van Wees S.C.M., van Pelt J.A., Knoester M., Laan R.,
RA Gerrits H., Weisbeek P.J., van Loon L.C.;
RT "A novel signaling pathway controlling induced systemic resistance in
RT Arabidopsis.";
RL Plant Cell 10:1571-1580(1998).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9807813; DOI=10.1046/j.1365-313x.1998.00265.x;
RA Staswick P.E., Yuen G.Y., Lehman C.C.;
RT "Jasmonate signaling mutants of Arabidopsis are susceptible to the soil
RT fungus Pythium irregulare.";
RL Plant J. 15:747-754(1998).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11006337; DOI=10.2307/3871179;
RA Rao M.V., Lee H., Creelman R.A., Mullet J.E., Davis K.R.;
RT "Jasmonic acid signaling modulates ozone-induced hypersensitive cell
RT death.";
RL Plant Cell 12:1633-1646(2000).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11041879; DOI=10.2307/3871195;
RA Asai T., Stone J.M., Heard J.E., Kovtun Y., Yorgey P., Sheen J.,
RA Ausubel F.M.;
RT "Fumonisin B1-induced cell death in arabidopsis protoplasts requires
RT jasmonate-, ethylene-, and salicylate-dependent signaling pathways.";
RL Plant Cell 12:1823-1836(2000).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11041881; DOI=10.2307/3871197;
RA Overmyer K., Tuominen H., Kettunen R., Betz C., Langebartels C.,
RA Sandermann H. Jr., Kangasjaervi J.;
RT "Ozone-sensitive arabidopsis rcd1 mutant reveals opposite roles for
RT ethylene and jasmonate signaling pathways in regulating superoxide-
RT dependent cell death.";
RL Plant Cell 12:1849-1862(2000).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11090217; DOI=10.2307/3871113;
RA Clarke J.D., Volko S.M., Ledford H., Ausubel F.M., Dong X.;
RT "Roles of salicylic acid, jasmonic acid, and ethylene in cpr-induced
RT resistance in arabidopsis.";
RL Plant Cell 12:2175-2190(2000).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12236603; DOI=10.1094/mpmi.2002.15.9.963;
RA Zhang B., Ramonell K., Somerville S., Stacey G.;
RT "Characterization of early, chitin-induced gene expression in
RT Arabidopsis.";
RL Mol. Plant Microbe Interact. 15:963-970(2002).
RN [16]
RP FUNCTION AS JASMONATE ADENYLASE, MUTAGENESIS OF SER-101; GLY-303 AND
RP GLU-334, AND DISRUPTION PHENOTYPE.
RX PubMed=12084835; DOI=10.1105/tpc.000885;
RA Staswick P.E., Tiryaki I., Rowe M.L.;
RT "Jasmonate response locus JAR1 and several related Arabidopsis genes encode
RT enzymes of the firefly luciferase superfamily that show activity on
RT jasmonic, salicylic, and indole-3-acetic acids in an assay for
RT adenylation.";
RL Plant Cell 14:1405-1415(2002).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12376653; DOI=10.1104/pp.005272;
RA Tiryaki I., Staswick P.E.;
RT "An Arabidopsis mutant defective in jasmonate response is allelic to the
RT auxin-signaling mutant axr1.";
RL Plant Physiol. 130:887-894(2002).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12744510; DOI=10.1094/mpmi.2003.16.5.398;
RA Mellersh D.G., Heath M.C.;
RT "An investigation into the involvement of defense signaling pathways in
RT components of the nonhost resistance of Arabidopsis thaliana to rust fungi
RT also reveals a model system for studying rust fungal compatibility.";
RL Mol. Plant Microbe Interact. 16:398-404(2003).
RN [19]
RP FUNCTION IN INDUCED SYSTEMIC RESISTANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=14558686; DOI=10.1094/mpmi.2003.16.10.851;
RA Iavicoli A., Boutet E., Buchala A., Metraux J.P.;
RT "Induced systemic resistance in Arabidopsis thaliana in response to root
RT inoculation with Pseudomonas fluorescens CHA0.";
RL Mol. Plant Microbe Interact. 16:851-858(2003).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12509524; DOI=10.1105/tpc.005165;
RA Ferrari S., Vairo D., Ausubel F.M., Cervone F., De Lorenzo G.;
RT "Tandemly duplicated Arabidopsis genes that encode polygalacturonase-
RT inhibiting proteins are regulated coordinately by different signal
RT transduction pathways in response to fungal infection.";
RL Plant Cell 15:93-106(2003).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12848825; DOI=10.1046/j.1365-313x.2003.01794.x;
RA Ferrari S., Plotnikova J.M., De Lorenzo G., Ausubel F.M.;
RT "Arabidopsis local resistance to Botrytis cinerea involves salicylic acid
RT and camalexin and requires EDS4 and PAD2, but not SID2, EDS5 or PAD4.";
RL Plant J. 35:193-205(2003).
RN [22]
RP FUNCTION AS JASMONATE ADENYLASE, AND CATALYTIC ACTIVITY.
RX PubMed=15258265; DOI=10.1105/tpc.104.023549;
RA Staswick P.E., Tiryaki I.;
RT "The oxylipin signal jasmonic acid is activated by an enzyme that
RT conjugates it to isoleucine in Arabidopsis.";
RL Plant Cell 16:2117-2127(2004).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15879447; DOI=10.1093/pcp/pci122;
RA Kishimoto K., Matsui K., Ozawa R., Takabayashi J.;
RT "Volatile C6-aldehydes and allo-ocimene activate defense genes and induce
RT resistance against Botrytis cinerea in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1093-1102(2005).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16639567; DOI=10.1007/s00442-006-0422-3;
RA Caputo C., Rutitzky M., Ballare C.L.;
RT "Solar ultraviolet-B radiation alters the attractiveness of Arabidopsis
RT plants to diamondback moths (Plutella xylostella L.): impacts on
RT oviposition and involvement of the jasmonic acid pathway.";
RL Oecologia 149:81-90(2006).
RN [25]
RP FUNCTION AS JASMONATES ADENYLASE.
RX PubMed=17291501; DOI=10.1016/j.febslet.2007.01.049;
RA Guranowski A., Miersch O., Staswick P.E., Suza W., Wasternack C.;
RT "Substrate specificity and products of side-reactions catalyzed by
RT jasmonate:amino acid synthetase (JAR1).";
RL FEBS Lett. 581:815-820(2007).
RN [26]
RP FUNCTION IN INDUCED SYSTEMIC RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17601164; DOI=10.1094/mpmi-20-7-0759;
RA Ahn I.-P., Lee S.-W., Suh S.-C.;
RT "Rhizobacteria-induced priming in Arabidopsis is dependent on ethylene,
RT jasmonic acid, and NPR1.";
RL Mol. Plant Microbe Interact. 20:759-768(2007).
RN [27]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GSTU20/FIP1.
RX PubMed=17220357; DOI=10.1104/pp.106.094185;
RA Chen I.-C., Huang I.-C., Liu M.-J., Wang Z.-G., Chung S.-S., Hsieh H.-L.;
RT "Glutathione S-transferase interacting with far-red insensitive 219 is
RT involved in phytochrome A-mediated signaling in Arabidopsis.";
RL Plant Physiol. 143:1189-1202(2007).
RN [28]
RP FUNCTION AS JASMONATES ADENYLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION BY WOUNDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18247047; DOI=10.1007/s00425-008-0694-4;
RA Suza W.P., Staswick P.E.;
RT "The role of JAR1 in Jasmonoyl-L: -isoleucine production during Arabidopsis
RT wound response.";
RL Planta 227:1221-1232(2008).
RN [29]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19304739; DOI=10.1093/pcp/pcp044;
RA Kawamura Y., Takenaka S., Hase S., Kubota M., Ichinose Y., Kanayama Y.,
RA Nakaho K., Klessig D.F., Takahashi H.;
RT "Enhanced defense responses in Arabidopsis induced by the cell wall protein
RT fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and JAR1.";
RL Plant Cell Physiol. 50:924-934(2009).
RN [30]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=19473329; DOI=10.1111/j.1365-313x.2009.03924.x;
RA Koo A.J.K., Gao X., Jones A.D., Howe G.A.;
RT "A rapid wound signal activates the systemic synthesis of bioactive
RT jasmonates in Arabidopsis.";
RL Plant J. 59:974-986(2009).
RN [31]
RP FUNCTION IN FAR-RED LIGHT SIGNALING, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19251652; DOI=10.1073/pnas.0900701106;
RA Moreno J.E., Tao Y., Chory J., Ballare C.L.;
RT "Ecological modulation of plant defense via phytochrome control of
RT jasmonate sensitivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4935-4940(2009).
RN [32]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20521949; DOI=10.1094/mpmi-23-7-0861;
RA Makandar R., Nalam V., Chaturvedi R., Jeannotte R., Sparks A.A., Shah J.;
RT "Involvement of salicylate and jasmonate signaling pathways in Arabidopsis
RT interaction with Fusarium graminearum.";
RL Mol. Plant Microbe Interact. 23:861-870(2010).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH
RP JASMONOYL-ISOLEUCINE.
RX PubMed=22628555; DOI=10.1126/science.1221863;
RA Westfall C.S., Zubieta C., Herrmann J., Kapp U., Nanao M.H., Jez J.M.;
RT "Structural basis for prereceptor modulation of plant hormones by GH3
RT proteins.";
RL Science 336:1708-1711(2012).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH GSTU20/FIP1; ATP;
RP L-ISOLEUCINE; L-LEUCINE; L-METHIONINE; L-VALINE AND JASMONOYL-ISOLEUCINE,
RP FUNCTION, MUTAGENESIS OF SER-101, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=28223489; DOI=10.1073/pnas.1609980114;
RA Chen C.-Y., Ho S.-S., Kuo T.-Y., Hsieh H.-L., Cheng Y.-S.;
RT "Structural basis of jasmonate-amido synthetase FIN219 in complex with
RT glutathione S-transferase FIP1 during the JA signal regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1815-E1824(2017).
CC -!- FUNCTION: Catalyzes the synthesis of jasmonates-amino acid conjugates
CC by adenylation; can use Ile and, in vitro at least, Val, Leu and Phe as
CC conjugating amino acids on jasmonic acid (JA) and 9,10-dihydro-JA
CC substrates, and to a lower extent, on 3-oxo-2-(2Z-pentenyl)-
CC cyclopentane-1-butyric acid (OPC-4) and 12-hydroxy-JA (12-OH-JA). Can
CC synthesize adenosine 5-tetraphosphate in vitro. Required for the JA-
CC mediated signaling pathway that regulates many developmental and
CC defense mechanisms, including growth root inhibition, vegetative
CC storage proteins (VSPs) accumulation, induced systemic resistance
CC (ISR), response to wounding and herbivores, tolerance to ozone O(3)
CC (probably having a role in lesion containment). Plays an important role
CC in the accumulation of JA-Ile in response to wounding, both locally and
CC systemically; promotes JA responding genes especially in distal part of
CC wounded plants, via the JA-Ile-stimulated degradation of JAZ repressor
CC proteins by the SCF(COI)E3 ubiquitin-protein ligase pathway. Involved
CC in the apoptosis-like programmed cell death (PCD) induced by fungal
CC toxin fumonisin B1-mediated (FB1). Required for volatile compounds (C6-
CC aldehydes and allo-ocimene)-mediated defense activation. Involved in
CC the non-pathogenic rhizobacterium-mediated ISR (defense priming) by
CC P.fluorescens (strains CHAOr and WCS417r) and P.putida LSW17S against
CC infection leaf pathogens such as P.syringae pv. tomato and
CC H.parasitica. Required for the JA-dependent resistance to fungi such as
CC P.irregulare, U.vignae and U.appendiculatus. Necessary to induce
CC systemic resistance against R.solanaceraum and P.syringae pv. tomato
CC with P.oligandrum (a non-pathogenic biocontrol agent) cell wall protein
CC fraction (CWP). Mediates PGIP2 accumulation in response to B.cinerea
CC infection and thus contributes to resistance against this pathogen.
CC Modulates the UV-B alteration of leaves attractiveness to diamondback
CC moths P.xylostella leading to insect oviposition. Involved in the
CC regulation of far-red light influence on development, being an actor of
CC the interplay between light and JA signaling (PubMed:28223489). Seems
CC necessary for the salicylic acid (SA)-mediated, NPR1-independent
CC resistance pathway. May contribute to the chitin-elicited pathway.
CC Contributes to the sensitivity toward F.graminearum.
CC {ECO:0000269|PubMed:10921909, ECO:0000269|PubMed:11006337,
CC ECO:0000269|PubMed:11041879, ECO:0000269|PubMed:11041881,
CC ECO:0000269|PubMed:11090217, ECO:0000269|PubMed:11607311,
CC ECO:0000269|PubMed:12084835, ECO:0000269|PubMed:12236603,
CC ECO:0000269|PubMed:12376653, ECO:0000269|PubMed:12509524,
CC ECO:0000269|PubMed:12744510, ECO:0000269|PubMed:12848825,
CC ECO:0000269|PubMed:14558686, ECO:0000269|PubMed:15258265,
CC ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:16639567,
CC ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:17291501,
CC ECO:0000269|PubMed:17601164, ECO:0000269|PubMed:18247047,
CC ECO:0000269|PubMed:19251652, ECO:0000269|PubMed:19304739,
CC ECO:0000269|PubMed:19473329, ECO:0000269|PubMed:20521949,
CC ECO:0000269|PubMed:28223489, ECO:0000269|PubMed:9724702,
CC ECO:0000269|PubMed:9807813}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a jasmonate + an L-alpha-amino acid + ATP = a jasmonyl-L-amino
CC acid + AMP + diphosphate + H(+); Xref=Rhea:RHEA:55772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:136183, ChEBI:CHEBI:136184,
CC ChEBI:CHEBI:456215; EC=6.3.2.52;
CC Evidence={ECO:0000269|PubMed:18247047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-7-isojasmonate + ATP + L-isoleucine = AMP + diphosphate +
CC H(+) + L-isoleucine-(+)-7-isojasmonate; Xref=Rhea:RHEA:54812,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:136179, ChEBI:CHEBI:136180,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15258265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54813;
CC Evidence={ECO:0000269|PubMed:15258265};
CC -!- ACTIVITY REGULATION: Activated by GSTU20/FIP1.
CC {ECO:0000269|PubMed:28223489}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for Ile {ECO:0000269|PubMed:18247047};
CC KM=1.93 mM for Leu {ECO:0000269|PubMed:18247047};
CC KM=1.84 mM for Phe {ECO:0000269|PubMed:18247047};
CC KM=2.49 mM for Val {ECO:0000269|PubMed:18247047};
CC KM=0.19 mM for (-)-JA {ECO:0000269|PubMed:18247047};
CC Vmax=92.4 nmol/min/mg enzyme with Ile as substrate
CC {ECO:0000269|PubMed:18247047};
CC Vmax=196.9 nmol/min/mg enzyme with Leu as substrate
CC {ECO:0000269|PubMed:18247047};
CC Vmax=68.1 nmol/min/mg enzyme with Phe as substrate
CC {ECO:0000269|PubMed:18247047};
CC Vmax=326.1 nmol/min/mg enzyme with Val as substrate
CC {ECO:0000269|PubMed:18247047};
CC Vmax=68.8 nmol/min/mg enzyme with (-)-JA as substrate
CC {ECO:0000269|PubMed:18247047};
CC Vmax=25.38 umol/min/mg enzyme with ATP as substrate (in the presence
CC of JA) {ECO:0000269|PubMed:28223489};
CC Vmax=59.17 umol/min/mg enzyme with ATP as substrate (in the presence
CC of JA and when in complex with GSTU20/FIP1)
CC {ECO:0000269|PubMed:28223489};
CC Note=All results obtained at pH 8.6 and 25 degrees Celsius
CC (PubMed:18247047). kcat is 2.72 sec(-1) with ATP as substrate (in the
CC presence of JA). kcat is 6.32 sec(-1) with ATP as substrate (in the
CC presence of JA and when in complex with GSTU20/FIP1)
CC (PubMed:28223489). {ECO:0000269|PubMed:18247047,
CC ECO:0000269|PubMed:28223489};
CC -!- SUBUNIT: Interacts with GSTU20/FIP1 under continuous far red (cFR)
CC light; this binding increases its activity and determines the priority
CC of substrate binding. {ECO:0000269|PubMed:17220357,
CC ECO:0000269|PubMed:28223489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10921909}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SKE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SKE2-2; Sequence=VSP_040469;
CC Name=3;
CC IsoId=Q9SKE2-3; Sequence=VSP_040468;
CC -!- INDUCTION: Rapidly induced by auxin. Accumulates locally in response to
CC wounding. {ECO:0000269|PubMed:10921909, ECO:0000269|PubMed:18247047}.
CC -!- DISRUPTION PHENOTYPE: Long hypocotyl phenotype under continuous far red
CC (cFR) light. Suppression of COP1 disruption. Decreased sensitivity to
CC jasmonic acid (JA) and methyl-jasmonate (MeJA) inhibition of root
CC elongation, but increased sensitivity to abscisic acid during seed
CC germination. Reduced induced systemic resistance (ISR) mediated by
CC P.fluorescens (CHAOr and WCS417r) and P.putida LSW17S in roots toward
CC H.parasitica and P.syringae pv. tomato in leaves. Increased
CC susceptibility to the fungi P.irregulare, U.vignae and
CC U.appendiculatus. Enhanced sensitivity to ozone O(3). Reduced fungal
CC toxin fumonisin B1-mediated (FB1) induced apoptosis-like programmed
CC cell death (PCD). Impaired SA-mediated, NPR1-independent resistance
CC pathway. Reduced gene induction in resposne to chitin. Reduced PGIP2
CC accumulation upon B.cinerea infection leading to enhanced sensitivity.
CC Altered defense activation by volatile compounds such as C6-aldehydes.
CC Disrupted UV-B alteration of leaves attractiveness to diamondback moths
CC P.xylostella, accompanied with reduced levels of UV-absorbing phenolic
CC compounds. Reduced accumulation of JA-Ile conjugates in response to
CC wounding, both locally and systemically. Compromised P.oligandrum cell
CC wall protein fraction (CWP) induce systemic resistance against
CC R.solanaceraum and P.syringae pv. tomato. Enhanced resistance to
CC F.graminearum. {ECO:0000269|PubMed:10921909,
CC ECO:0000269|PubMed:11006337, ECO:0000269|PubMed:11041879,
CC ECO:0000269|PubMed:11041881, ECO:0000269|PubMed:11090217,
CC ECO:0000269|PubMed:11607311, ECO:0000269|PubMed:12084835,
CC ECO:0000269|PubMed:12236603, ECO:0000269|PubMed:12376653,
CC ECO:0000269|PubMed:12509524, ECO:0000269|PubMed:12744510,
CC ECO:0000269|PubMed:12848825, ECO:0000269|PubMed:14558686,
CC ECO:0000269|PubMed:15879447, ECO:0000269|PubMed:16639567,
CC ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:17601164,
CC ECO:0000269|PubMed:18247047, ECO:0000269|PubMed:19251652,
CC ECO:0000269|PubMed:19304739, ECO:0000269|PubMed:19473329,
CC ECO:0000269|PubMed:20521949, ECO:0000269|PubMed:9724702,
CC ECO:0000269|PubMed:9807813}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF279129; AAF86349.1; -; Genomic_DNA.
DR EMBL; AC006526; AAD23040.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10683.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10684.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10685.1; -; Genomic_DNA.
DR EMBL; AY050861; AAK92798.1; -; mRNA.
DR EMBL; AY150437; AAN12979.1; -; mRNA.
DR EMBL; AK316746; BAH19469.1; -; mRNA.
DR EMBL; AK319095; BAH57210.1; -; mRNA.
DR EMBL; Z26804; CAA81417.1; -; mRNA.
DR EMBL; AK221189; BAD95281.1; -; mRNA.
DR PIR; A84902; A84902.
DR RefSeq; NP_001078069.1; NM_001084600.1. [Q9SKE2-3]
DR RefSeq; NP_566071.1; NM_130200.2. [Q9SKE2-1]
DR RefSeq; NP_850453.1; NM_180122.4. [Q9SKE2-1]
DR PDB; 4EPL; X-ray; 2.01 A; A=1-575.
DR PDB; 5ECH; X-ray; 2.14 A; A/D=1-575.
DR PDB; 5ECI; X-ray; 1.56 A; A/D=1-575.
DR PDB; 5ECK; X-ray; 1.54 A; A/D=1-575.
DR PDB; 5ECL; X-ray; 1.85 A; A/D=1-575.
DR PDB; 5ECM; X-ray; 1.60 A; A/D=1-575.
DR PDB; 5ECN; X-ray; 1.72 A; A/D=1-575.
DR PDB; 5ECO; X-ray; 1.80 A; A/D=1-575.
DR PDB; 5ECP; X-ray; 2.25 A; A/D=1-575.
DR PDB; 5ECQ; X-ray; 1.66 A; A/D=1-575.
DR PDB; 5ECR; X-ray; 1.72 A; A/D=1-575.
DR PDB; 5GZZ; X-ray; 2.39 A; A=1-575.
DR PDBsum; 4EPL; -.
DR PDBsum; 5ECH; -.
DR PDBsum; 5ECI; -.
DR PDBsum; 5ECK; -.
DR PDBsum; 5ECL; -.
DR PDBsum; 5ECM; -.
DR PDBsum; 5ECN; -.
DR PDBsum; 5ECO; -.
DR PDBsum; 5ECP; -.
DR PDBsum; 5ECQ; -.
DR PDBsum; 5ECR; -.
DR PDBsum; 5GZZ; -.
DR AlphaFoldDB; Q9SKE2; -.
DR SMR; Q9SKE2; -.
DR BioGRID; 4579; 3.
DR STRING; 3702.AT2G46370.4; -.
DR SwissLipids; SLP:000001772; -.
DR PaxDb; Q9SKE2; -.
DR PRIDE; Q9SKE2; -.
DR ProteomicsDB; 232263; -. [Q9SKE2-1]
DR EnsemblPlants; AT2G46370.1; AT2G46370.1; AT2G46370. [Q9SKE2-1]
DR EnsemblPlants; AT2G46370.2; AT2G46370.2; AT2G46370. [Q9SKE2-1]
DR EnsemblPlants; AT2G46370.3; AT2G46370.3; AT2G46370. [Q9SKE2-3]
DR GeneID; 819244; -.
DR Gramene; AT2G46370.1; AT2G46370.1; AT2G46370. [Q9SKE2-1]
DR Gramene; AT2G46370.2; AT2G46370.2; AT2G46370. [Q9SKE2-1]
DR Gramene; AT2G46370.3; AT2G46370.3; AT2G46370. [Q9SKE2-3]
DR KEGG; ath:AT2G46370; -.
DR Araport; AT2G46370; -.
DR eggNOG; ENOG502QPMW; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9SKE2; -.
DR OMA; DEKIMID; -.
DR PhylomeDB; Q9SKE2; -.
DR BioCyc; ARA:AT2G46370-MON; -.
DR BRENDA; 6.3.2.52; 399.
DR PRO; PR:Q9SKE2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKE2; baseline and differential.
DR Genevisible; Q9SKE2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0102058; F:jasmonoyl-leucine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0102057; F:jasmonoyl-valine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0070728; F:leucine binding; IDA:UniProtKB.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IEP:UniProtKB.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR GO; GO:2000030; P:regulation of response to red or far red light; IMP:UniProtKB.
DR GO; GO:0010046; P:response to mycotoxin; IMP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IMP:UniProtKB.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Immunity; Innate immunity; Jasmonic acid signaling pathway; Ligase;
KW Nucleotide-binding; Plant defense; Reference proteome.
FT CHAIN 1..575
FT /note="Jasmonoyl--L-amino acid synthetase JAR1"
FT /id="PRO_0000403931"
FT COILED 10..30
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 101
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0007744|PDB:4EPL"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 166..170
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL,
FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 328..331
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:22628555,
FT ECO:0000269|PubMed:28223489, ECO:0007744|PDB:4EPL,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL,
FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP,
FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR,
FT ECO:0007744|PDB:5GZZ"
FT BINDING 331..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT BINDING 530..534
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECL, ECO:0007744|PDB:5ECM,
FT ECO:0007744|PDB:5ECN, ECO:0007744|PDB:5ECP,
FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28223489,
FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI,
FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECN,
FT ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040468"
FT VAR_SEQ 13..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040469"
FT MUTAGEN 101
FT /note="S->F: In jar1-1; insensitivity to jasmonate,
FT Strongly reduced adenylation activity."
FT /evidence="ECO:0000269|PubMed:12084835,
FT ECO:0000269|PubMed:28223489"
FT MUTAGEN 303
FT /note="G->R: In jar1-5; insensitivity to jasmonate."
FT /evidence="ECO:0000269|PubMed:12084835"
FT MUTAGEN 334
FT /note="E->K: In jar1-3; insensitivity to jasmonate."
FT /evidence="ECO:0000269|PubMed:12084835"
FT CONFLICT 475
FT /note="Y -> N (in Ref. 4; AAK92798)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="T -> A (in Ref. 7; BAD95281)"
FT /evidence="ECO:0000305"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5ECH"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:5ECM"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5ECM"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5ECL"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5ECR"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:5ECI"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:5ECM"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5ECI"
FT STRAND 399..413
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:4EPL"
FT HELIX 438..453
FT /evidence="ECO:0007829|PDB:5ECK"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 504..512
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 527..536
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:5ECK"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:5ECK"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:5ECK"
SQ SEQUENCE 575 AA; 64350 MW; 2E4304B03DA6DE59 CRC64;
MLEKVETFDM NRVIDEFDEM TRNAHQVQKQ TLKEILLKNQ SAIYLQNCGL NGNATDPEEA
FKSMVPLVTD VELEPYIKRM VDGDTSPILT GHPVPAISLS SGTSQGRPKF IPFTDELMEN
TLQLFRTAFA FRNRDFPIDD NGKALQFIFS SKQYISTGGV PVGTATTNVY RNPNFKAGMK
SITSPSCSPD EVIFSPDVHQ ALYCHLLSGI LFRDQVQYVF AVFAHGLVHA FRTFEQVWEE
IVTDIKDGVL SNRITVPSVR TAMSKLLTPN PELAETIRTK CMSLSNWYGL IPALFPNAKY
VYGIMTGSME PYVPKLRHYA GDLPLVSHDY GSSEGWIAAN VTPRLSPEEA TFAVIPNLGY
FEFLPVSETG EGEEKPVGLT QVKIGEEYEV VITNYAGLYR YRLGDVVKVI GFYNNTPQLK
FICRRNLILS INIDKNTERD LQLSVESAAK RLSEEKIEVI DFSSYIDVST DPGHYAIFWE
ISGETNEDVL QDCCNCLDRA FIDAGYVSSR KCKTIGALEL RVVAKGTFRK IQEHFLGLGS
SAGQFKMPRC VKPSNAKVLQ ILCENVVSSY FSTAF
