ERLL2_ARATH
ID ERLL2_ARATH Reviewed; 182 AA.
AC Q9SU34;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=pEARLI1-like lipid transfer protein 2;
DE Flags: Precursor;
GN OrderedLocusNames=At4g12490; ORFNames=T1P17.80;
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 FUNCTION, 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 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).
CC -!- FUNCTION: Probable lipid transfer protein (LTP). May improve freezing
CC survival. Seems to control the flowering process and lignin synthesis.
CC Confers resistance to Botrytis cinerea. {ECO:0000269|PubMed:17257167,
CC ECO:0000269|PubMed:17786468, ECO:0000269|PubMed:21815977}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- INDUCTION: Transient accumulation in response to a brief exposures to
CC cold. {ECO:0000269|PubMed:17786468}.
CC -!- DISRUPTION PHENOTYPE: Reduced cutin accumulation due to lower cutin
CC biosynthesis. Early flowering in long-day conditions.
CC {ECO:0000269|PubMed:21815977}.
CC -!- SIMILARITY: Belongs to the plant LTP family. PEARLI1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL049730; CAB41719.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78292.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83139.1; -; Genomic_DNA.
DR EMBL; AY052336; AAK96529.1; -; mRNA.
DR EMBL; AY061906; AAL31233.1; -; mRNA.
DR PIR; T07641; T07641.
DR RefSeq; NP_192986.1; NM_117319.2.
DR AlphaFoldDB; Q9SU34; -.
DR SMR; Q9SU34; -.
DR STRING; 3702.AT4G12490.1; -.
DR PaxDb; Q9SU34; -.
DR PRIDE; Q9SU34; -.
DR ProteomicsDB; 220697; -.
DR EnsemblPlants; AT4G12490.1; AT4G12490.1; AT4G12490.
DR GeneID; 826861; -.
DR Gramene; AT4G12490.1; AT4G12490.1; AT4G12490.
DR KEGG; ath:AT4G12490; -.
DR Araport; AT4G12490; -.
DR TAIR; locus:2135625; AT4G12490.
DR eggNOG; ENOG502RZES; Eukaryota.
DR HOGENOM; CLU_055715_3_2_1; -.
DR InParanoid; Q9SU34; -.
DR OMA; MAYFKIA; -.
DR OrthoDB; 1608612at2759; -.
DR PRO; PR:Q9SU34; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU34; baseline and differential.
DR Genevisible; Q9SU34; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; 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 2: Evidence at transcript level;
KW Cell wall; Plant defense; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..182
FT /note="pEARLI1-like lipid transfer protein 2"
FT /id="PRO_0000425606"
FT REPEAT 42..46
FT /note="1"
FT /evidence="ECO:0000250"
FT REPEAT 47..51
FT /note="2"
FT /evidence="ECO:0000250"
FT REPEAT 52..56
FT /note="3"
FT /evidence="ECO:0000250"
FT REPEAT 62..66
FT /note="4"
FT /evidence="ECO:0000250"
FT REPEAT 67..71
FT /note="5"
FT /evidence="ECO:0000250"
FT REPEAT 72..76
FT /note="6"
FT /evidence="ECO:0000250"
FT REPEAT 77..81
FT /note="7"
FT /evidence="ECO:0000250"
FT REGION 33..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..81
FT /note="7 X 5 AA repeats of P-[KS]-V-P-[ST]"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 18789 MW; 69FCE5B281583E0E CRC64;
MASKNSASLA LFFALNILFF TLTAGTNCRC NPSPKPRPLP NPKVPSPKVP TPSVPSPYVP
TPSVPSPSVP TPSVPSPSVP SPNPTPVIPP RTPGSSGNCP IDALRLGVCA NVLSGLLNVQ
LGQPSPQPCC SLIQGLVDLD AAVCLCTALR ANVLGINLNV PISLSVLLNV CNRRLPSNFQ
CA
