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ERLI1_ARATH
ID   ERLI1_ARATH             Reviewed;         168 AA.
AC   Q39176;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Lipid transfer protein EARLI 1;
DE   AltName: Full=Protein EARLY ARABIDOPSIS ALUMINUM INDUCED 1;
DE            Short=pEARLI1;
DE   Flags: Precursor;
GN   Name=EARLI1; OrderedLocusNames=At4g12480; ORFNames=T1P17.70;
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], INDUCTION BY ALUMINUM, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RA   Richards K.D., Gardner R.C.;
RT   "pEARLI 1: an Arabidopsis member of a conserved gene family.";
RL   (er) Plant Gene Register PGR95-099(1995).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. No-0;
RX   PubMed=11202439; DOI=10.1023/a:1026536724779;
RA   Wilkosz R., Schlaeppi M.;
RT   "A gene expression screen identifies EARLI1 as a novel vernalization-
RT   responsive gene in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 44:777-787(2000).
RN   [7]
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   [8]
RP   FUNCTION, INDUCTION BY COLD, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   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   [9]
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   [10]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY COLD AND SALT.
RC   STRAIN=cv. Columbia;
RX   PubMed=21556912; DOI=10.1007/s00425-011-1425-9;
RA   Xu D., Huang X., Xu Z.Q., Schlappi M.;
RT   "The HyPRP gene EARLI1 has an auxiliary role for germinability and early
RT   seedling development under low temperature and salt stress conditions in
RT   Arabidopsis thaliana.";
RL   Planta 234:565-577(2011).
RN   [11]
RP   FUNCTION AS ANTI-FUNGAL PROTEIN.
RC   STRAIN=cv. Columbia;
RX   PubMed=22759515; DOI=10.1016/j.gene.2012.06.070;
RA   Li L., Zhang C., Xu D., Schlappi M., Xu Z.Q.;
RT   "Expression of recombinant EARLI1, a hybrid proline-rich protein of
RT   Arabidopsis, in Escherichia coli and its inhibition effect to the growth of
RT   fungal pathogens and Saccharomyces cerevisiae.";
RL   Gene 506:50-61(2012).
CC   -!- FUNCTION: Probable lipid transfer protein (LTP). May improve freezing
CC       survival. Seems to control the flowering process and lignin synthesis.
CC       Has an auxiliary role for germinability and early seedling development
CC       under low temperature and salt stress conditions, probably in an
CC       abscisic acid- (ABA) dependent manner. Confers resistance to Botrytis
CC       cinerea and exhibits anti-fungal activity, at least against
CC       S.cerevisiae, B. cinerea and Fusarium oxysporum, probably by increasing
CC       their membrane permeability. {ECO:0000269|PubMed:17257167,
CC       ECO:0000269|PubMed:17786468, ECO:0000269|PubMed:21556912,
CC       ECO:0000269|PubMed:21815977, ECO:0000269|PubMed:22759515}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:17786468}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in aerial part of seedlings, and,
CC       to a lower extent, in roots. Higher basal levels in early-flowering
CC       ecotypes. {ECO:0000269|PubMed:11202439, ECO:0000269|Ref.1}.
CC   -!- DEVELOPMENTAL STAGE: Induced during germination in embryonic tissues,
CC       and strongly expressed in certain parts of young seedlings, in the tips
CC       of cotyledons and to a certain degree in developing leaves and roots.
CC       {ECO:0000269|PubMed:21556912}.
CC   -!- INDUCTION: Transient accumulation in response to toxic levels of
CC       aluminum (Al). Stably activated by vernalization; vernalization and
CC       subsequent growth in long-day photoperiods have an additive or
CC       synergistic effect on this activation. Induced by both cold and salt.
CC       {ECO:0000269|PubMed:11202439, ECO:0000269|PubMed:17786468,
CC       ECO:0000269|PubMed:21556912, ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: Increased tendency for freezing-induced cellular
CC       damage. Reduced cutin accumulation due to lower cutin biosynthesis.
CC       Early flowering in long-day conditions. {ECO:0000269|PubMed:17786468,
CC       ECO:0000269|PubMed:21815977}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. PEARLI1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L43080; AAC37471.1; -; mRNA.
DR   EMBL; AL049730; CAB41718.1; -; Genomic_DNA.
DR   EMBL; AL161534; CAB78291.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83138.1; -; Genomic_DNA.
DR   EMBL; AF412111; AAL06564.1; -; mRNA.
DR   EMBL; AY133654; AAM91484.1; -; mRNA.
DR   EMBL; AK230253; BAF02055.1; -; mRNA.
DR   PIR; T07640; T07640.
DR   RefSeq; NP_192985.1; NM_117318.3.
DR   AlphaFoldDB; Q39176; -.
DR   SMR; Q39176; -.
DR   STRING; 3702.AT4G12480.1; -.
DR   PaxDb; Q39176; -.
DR   PRIDE; Q39176; -.
DR   ProteomicsDB; 220695; -.
DR   EnsemblPlants; AT4G12480.1; AT4G12480.1; AT4G12480.
DR   GeneID; 826860; -.
DR   Gramene; AT4G12480.1; AT4G12480.1; AT4G12480.
DR   KEGG; ath:AT4G12480; -.
DR   Araport; AT4G12480; -.
DR   TAIR; locus:2135610; AT4G12480.
DR   eggNOG; ENOG502S36E; Eukaryota.
DR   HOGENOM; CLU_055715_3_2_1; -.
DR   InParanoid; Q39176; -.
DR   OMA; NVCNRKV; -.
DR   OrthoDB; 1608612at2759; -.
DR   PhylomeDB; Q39176; -.
DR   PRO; PR:Q39176; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q39176; baseline and differential.
DR   Genevisible; Q39176; 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:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; 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 wall; Plant defense; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..168
FT                   /note="Lipid transfer protein EARLI 1"
FT                   /id="PRO_0000425604"
FT   REPEAT          34..41
FT                   /note="A-1"
FT   REPEAT          42..49
FT                   /note="A-2"
FT   REPEAT          50..57
FT                   /note="A-3"
FT   REPEAT          58..62
FT                   /note="B-1"
FT   REPEAT          63..67
FT                   /note="B-2"
FT   REGION          32..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..57
FT                   /note="3 X 8 AA repeats A of P-K-[HP]-K-P-V-P-S"
FT   REGION          58..67
FT                   /note="2 X 58 AA tandem repeats B of P-S-V-P-S"
FT   COMPBIAS        35..79
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  17308 MW;  752368B34493D9B7 CRC64;
     MASKNSASIA LFFALNIIFF TLTAATDCGC NPSPKHKPVP SPKPKPVPSP KPKPVPSPSV
     PSPSVPSPNP RPVTPPRTPG SSGNCPIDAL RLGVCANVLS SLLNIQLGQP SAQPCCSLIQ
     GLVDLDAAIC LCTALRANVL GINLNVPISL SVLLNVCNRK VPSGFQCA
 
 
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