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ERLL1_ARATH
ID   ERLL1_ARATH             Reviewed;         161 AA.
AC   Q9SU35;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=pEARLI1-like lipid transfer protein 1;
DE   AltName: Full=Protein AZELAIC ACID INDUCED 1;
DE   Flags: Precursor;
GN   Name=AZI1; OrderedLocusNames=At4g12470; ORFNames=T1P17.60;
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 [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   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=17257167; DOI=10.1111/j.1365-313x.2006.03017.x;
RA   Chassot C., Nawrath C., Metraux J.-P.;
RT   "Cuticular defects lead to full immunity to a major plant pathogen.";
RL   Plant J. 49:972-980(2007).
RN   [5]
RP   INDUCTION BY COLD, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17786468; DOI=10.1007/s00425-007-0611-2;
RA   Zhang Y., Schlappi M.;
RT   "Cold responsive EARLI1 type HyPRPs improve freezing survival of yeast
RT   cells and form higher order complexes in plants.";
RL   Planta 227:233-243(2007).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY AZELAIC ACID.
RX   PubMed=19342588; DOI=10.1126/science.1170025;
RA   Jung H.W., Tschaplinski T.J., Wang L., Glazebrook J., Greenberg J.T.;
RT   "Priming in systemic plant immunity.";
RL   Science 324:89-91(2009).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY COLD.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija;
RX   PubMed=21492954; DOI=10.1016/j.jplph.2011.01.023;
RA   Xu Z.Y., Zhang X., Schlappi M., Xu Z.Q.;
RT   "Cold-inducible expression of AZI1 and its function in improvement of
RT   freezing tolerance of Arabidopsis thaliana and Saccharomyces cerevisiae.";
RL   J. Plant Physiol. 168:1576-1587(2011).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=21815977; DOI=10.1111/j.1438-8677.2010.00428.x;
RA   Shi Y., Zhang X., Xu Z.Y., Li L., Zhang C., Schlappi M., Xu Z.Q.;
RT   "Influence of EARLI1-like genes on flowering time and lignin synthesis of
RT   Arabidopsis thaliana.";
RL   Plant Biol. 13:731-739(2011).
RN   [9]
RP   FUNCTION, AND INDUCTION BY PSEUDOMONAS FLUORESCENS.
RX   PubMed=22375709; DOI=10.1094/mpmi-09-11-0253;
RA   Weston D.J., Pelletier D.A., Morrell-Falvey J.L., Tschaplinski T.J.,
RA   Jawdy S.S., Lu T.Y., Allen S.M., Melton S.J., Martin M.Z., Schadt C.W.,
RA   Karve A.A., Chen J.G., Yang X., Doktycz M.J., Tuskan G.A.;
RT   "Pseudomonas fluorescens induces strain-dependent and strain-independent
RT   host plant responses in defense networks, primary metabolism,
RT   photosynthesis, and fitness.";
RL   Mol. Plant Microbe Interact. 25:765-778(2012).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLYCEROL-3-PHOSPHATE,
RP   SUBCELLULAR LOCATION, INTERACTION WITH DIR1, AND SUBUNIT.
RC   STRAIN=cv. Columbia;
RX   PubMed=23602565; DOI=10.1016/j.celrep.2013.03.030;
RA   Yu K., Soares J.M., Mandal M.K., Wang C., Chanda B., Gifford A.N.,
RA   Fowler J.S., Navarre D., Kachroo A., Kachroo P.;
RT   "A feedback regulatory loop between G3P and lipid transfer proteins DIR1
RT   and AZI1 mediates azelaic-acid-induced systemic immunity.";
RL   Cell Rep. 3:1266-1278(2013).
RN   [11]
RP   INTERACTION WITH PDLP1, AND SUBCELLULAR LOCATION.
RX   PubMed=27078071; DOI=10.1016/j.chom.2016.03.006;
RA   Lim G.H., Shine M.B., de Lorenzo L., Yu K., Cui W., Navarre D., Hunt A.G.,
RA   Lee J.Y., Kachroo A., Kachroo P.;
RT   "Plasmodesmata localizing proteins regulate transport and signaling during
RT   systemic acquired immunity in plants.";
RL   Cell Host Microbe 19:541-549(2016).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27337039; DOI=10.1016/j.plaphy.2016.06.016;
RA   Wang X.Y., Li D.Z., Li Q., Ma Y.Q., Yao J.W., Huang X., Xu Z.Q.;
RT   "Metabolomic analysis reveals the relationship between AZI1 and sugar
RT   signaling in systemic acquired resistance of Arabidopsis.";
RL   Plant Physiol. Biochem. 107:273-287(2016).
CC   -!- FUNCTION: Probable lipid transfer protein (LTP). Seems to control the
CC       flowering process and lignin synthesis. Together with DIR1, required
CC       for glycerol-3-phosphate- (G3P) and azelaic acid- (AA) induced systemic
CC       acquired resistance (SAR). Component of plant systemic immunity
CC       involved in priming defenses in a AA-dependent manner, by modulating
CC       production and/or translocation of a mobile signal(s) during SAR.
CC       Confers resistance to Botrytis cinerea and Pseudomonas syringae pv.
CC       tomato DC3000 and PmaDG3. May be involved in induced systemic
CC       resistance (ISR) mediated by non-pathogenic bacteria (e.g. P.
CC       fluorescens GM30). Prevents electrolyte leakage during freezing damage.
CC       {ECO:0000269|PubMed:17257167, ECO:0000269|PubMed:19342588,
CC       ECO:0000269|PubMed:21492954, ECO:0000269|PubMed:21815977,
CC       ECO:0000269|PubMed:22375709, ECO:0000269|PubMed:23602565,
CC       ECO:0000269|PubMed:27337039}.
CC   -!- SUBUNIT: Self-interacts and binds to DIR1 (PubMed:23602565). Interacts
CC       with PDLP1 (PubMed:27078071). {ECO:0000269|PubMed:23602565,
CC       ECO:0000269|PubMed:27078071}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Endoplasmic
CC       reticulum {ECO:0000269|PubMed:23602565, ECO:0000269|PubMed:27078071}.
CC       Cell junction, plasmodesma {ECO:0000269|PubMed:23602565}. Plastid,
CC       chloroplast {ECO:0000269|PubMed:27078071}. Note=Chloroplast location is
CC       observed in the absence of PLDP1 or PDLP5.
CC       {ECO:0000269|PubMed:27078071}.
CC   -!- INDUCTION: Transient accumulation in response to a brief exposures to
CC       cold. Induced by glycerol-3-phosphate (G3P) and azelaic acid (AA)
CC       during systemic acquired resistance (SAR) and Pseudomonas fluorescens
CC       GM30 strain during induced systemic resistance (ISR).
CC       {ECO:0000269|PubMed:17786468, ECO:0000269|PubMed:19342588,
CC       ECO:0000269|PubMed:21492954, ECO:0000269|PubMed:22375709,
CC       ECO:0000269|PubMed:23602565}.
CC   -!- DISRUPTION PHENOTYPE: Reduced cutin accumulation due to lower cutin
CC       biosynthesis. Early flowering in long-day conditions. Compromised
CC       pathogen-induced (e.g. Pseudomonas syringae pv. tomato DC3000 and
CC       PmaDG3) glycerol-3-phosphate- (G3P) and azelaic acid-(AA) dependent
CC       systemic acquired resistance (SAR). Increased tendencies in cellular
CC       damage after freezing treatment. {ECO:0000269|PubMed:19342588,
CC       ECO:0000269|PubMed:21492954, ECO:0000269|PubMed:21815977,
CC       ECO:0000269|PubMed:23602565, ECO:0000269|PubMed:27337039}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. PEARLI1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL049730; CAB41717.1; -; Genomic_DNA.
DR   EMBL; AL161534; CAB78290.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83137.1; -; Genomic_DNA.
DR   EMBL; AY093032; AAM13031.1; -; mRNA.
DR   EMBL; BT000404; AAN15723.1; -; mRNA.
DR   PIR; T07639; T07639.
DR   RefSeq; NP_192984.1; NM_117317.4.
DR   AlphaFoldDB; Q9SU35; -.
DR   SMR; Q9SU35; -.
DR   BioGRID; 12157; 2.
DR   STRING; 3702.AT4G12470.1; -.
DR   iPTMnet; Q9SU35; -.
DR   PaxDb; Q9SU35; -.
DR   ProteomicsDB; 220696; -.
DR   EnsemblPlants; AT4G12470.1; AT4G12470.1; AT4G12470.
DR   GeneID; 826859; -.
DR   Gramene; AT4G12470.1; AT4G12470.1; AT4G12470.
DR   KEGG; ath:AT4G12470; -.
DR   Araport; AT4G12470; -.
DR   TAIR; locus:2135595; AT4G12470.
DR   eggNOG; ENOG502S36E; Eukaryota.
DR   HOGENOM; CLU_055715_3_2_1; -.
DR   InParanoid; Q9SU35; -.
DR   OMA; SERIPMG; -.
DR   OrthoDB; 1608612at2759; -.
DR   PhylomeDB; Q9SU35; -.
DR   PRO; PR:Q9SU35; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SU35; baseline and differential.
DR   Genevisible; Q9SU35; AT.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
DR   GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR   GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR   CDD; cd01958; HPS_like; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR027923; Hydrophob_seed_dom.
DR   Pfam; PF14547; Hydrophob_seed; 1.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell wall; Chloroplast; Endoplasmic reticulum;
KW   Hypersensitive response; Plant defense; Plastid; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..161
FT                   /note="pEARLI1-like lipid transfer protein 1"
FT                   /id="PRO_0000425605"
FT   REPEAT          32..39
FT                   /note="A-1"
FT                   /evidence="ECO:0000250"
FT   REPEAT          40..47
FT                   /note="A-2"
FT                   /evidence="ECO:0000250"
FT   REGION          32..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..49
FT                   /note="2 X 8 AA tandem repeats A of P-S-P-K-P-K-P-V"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        33..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   161 AA;  16766 MW;  E65581673BC641F7 CRC64;
     MASKNSASLA LFFALNILFF TLTVATNCNC KPSPKPKPVP SPKPKPVQCP PPPRPSVPSP
     NPRPVTPPRT PGSSGNSCPI DALKLGVCAN VLSSLLNIQL GQPSSQQCCS LIQGLVDVDA
     AICLCTALRA NVLGINLNVP ISLSVLLNVC NRKLPSGFQC A
 
 
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