LEA31_ARATH
ID LEA31_ARATH Reviewed; 262 AA.
AC Q9LJ97; Q39137; Q42234;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Late embryogenesis abundant protein 31 {ECO:0000303|PubMed:18318901};
DE Short=LEA 31 {ECO:0000303|PubMed:18318901};
DE AltName: Full=Protein RESPONSIVE TO ABSCISIC ACID 28 {ECO:0000303|PubMed:10412913};
DE Short=AtRAB28 {ECO:0000303|PubMed:10412913};
GN Name=RAB28 {ECO:0000303|PubMed:10412913};
GN OrderedLocusNames=At3g22490 {ECO:0000312|Araport:AT3G22490};
GN ORFNames=F16J14.5 {ECO:0000312|EMBL:BAB01464.1};
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 {ECO:0000312|EMBL:BAB01464.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Raynal M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [MRNA] OF 163-262.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, INDUCTION BY ABI3, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=10412913; DOI=10.1023/a:1006219315562;
RA Arenas-Mena C., Raynal M., Borrell A., Varoquaux F., Cutanda M.C.,
RA Stacy R.A.P., Pages M., Delseny M., Culianez-Macia F.A.;
RT "Expression and cellular localization of Atrab28 during arabidopsis
RT embryogenesis.";
RL Plant Mol. Biol. 40:355-363(1999).
RN [7]
RP FUNCTION, MUTAGENESIS OF 8-LYS-ARG-9, SUBCELLULAR LOCATION, AND NUCLEAR
RP LOCALIZATION SIGNAL.
RC STRAIN=cv. Columbia;
RX PubMed=12175017; DOI=10.1023/a:1016084615014;
RA Borrell A., Cutanda M.C., Lumbreras V., Pujal J., Goday A.,
RA Culianez-Macia F.A., Pages M.;
RT "Arabidopsis thaliana atrab28: a nuclear targeted protein related to
RT germination and toxic cation tolerance.";
RL Plant Mol. Biol. 50:249-259(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18318901; DOI=10.1186/1471-2164-9-118;
RA Hundertmark M., Hincha D.K.;
RT "LEA (late embryogenesis abundant) proteins and their encoding genes in
RT Arabidopsis thaliana.";
RL BMC Genomics 9:118-118(2008).
RN [9]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=25005920; DOI=10.1105/tpc.114.127316;
RA Candat A., Paszkiewicz G., Neveu M., Gautier R., Logan D.C.,
RA Avelange-Macherel M.-H., Macherel D.;
RT "The ubiquitous distribution of late embryogenesis abundant proteins across
RT cell compartments in Arabidopsis offers tailored protection against abiotic
RT stress.";
RL Plant Cell 26:3148-3166(2014).
CC -!- FUNCTION: LEA proteins are late embryonic proteins abundant in higher
CC plant seed embryos. The function of those proteins is not known
CC (Probable). Promotes germination rate. Enhances cation toxicity (e.g.
CC lithium ion) and osmotic stress (e.g. NaCl and sorbitol) tolerance
CC during germination and in seedlings (PubMed:12175017).
CC {ECO:0000269|PubMed:12175017, ECO:0000305}.
CC -!- INTERACTION:
CC Q9LJ97; O04492: DRB1; NbExp=3; IntAct=EBI-25520978, EBI-632620;
CC Q9LJ97; Q9FIF5: SAG113; NbExp=3; IntAct=EBI-25520978, EBI-2363373;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12175017}.
CC Nucleus {ECO:0000269|PubMed:12175017, ECO:0000269|PubMed:25005920}.
CC Cytoplasm {ECO:0000269|PubMed:25005920}. Note=Present in the nucleus
CC and nucleolus of mature embryos cells. {ECO:0000269|PubMed:12175017}.
CC -!- TISSUE SPECIFICITY: Embryo specific, only in dry mature seeds.
CC {ECO:0000269|PubMed:10412913}.
CC -!- DEVELOPMENTAL STAGE: In mature embryos, restricted to provascular
CC tissues. Also present in the seed coat outer tegument and silique
CC epidermis. Levels decrease during seed imbibition and germination.
CC {ECO:0000269|PubMed:10412913}.
CC -!- INDUCTION: Stimulated in embryos by the transcriptional activator ABI3.
CC Not induced in vegetative tissues by abscisic acid (ABA), osmotic
CC stress or dehydration. {ECO:0000269|PubMed:10412913}.
CC -!- SIMILARITY: Belongs to the LEA type SMP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63085.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X92115; CAA63085.1; ALT_FRAME; mRNA.
DR EMBL; AP000731; BAB01464.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76646.1; -; Genomic_DNA.
DR EMBL; BT002907; AAO22723.1; -; mRNA.
DR EMBL; BT004425; AAO42419.1; -; mRNA.
DR EMBL; Z29875; CAA82828.1; -; mRNA.
DR PIR; S71260; S71260.
DR RefSeq; NP_188888.1; NM_113148.1.
DR AlphaFoldDB; Q9LJ97; -.
DR IntAct; Q9LJ97; 2.
DR STRING; 3702.AT3G22490.1; -.
DR PaxDb; Q9LJ97; -.
DR PRIDE; Q9LJ97; -.
DR ProMEX; Q9LJ97; -.
DR ProteomicsDB; 230197; -.
DR EnsemblPlants; AT3G22490.1; AT3G22490.1; AT3G22490.
DR GeneID; 821820; -.
DR Gramene; AT3G22490.1; AT3G22490.1; AT3G22490.
DR KEGG; ath:AT3G22490; -.
DR Araport; AT3G22490; -.
DR TAIR; locus:2077081; AT3G22490.
DR eggNOG; ENOG502QPSX; Eukaryota.
DR HOGENOM; CLU_075678_0_0_1; -.
DR InParanoid; Q9LJ97; -.
DR OMA; MMQMAEN; -.
DR OrthoDB; 1200778at2759; -.
DR PhylomeDB; Q9LJ97; -.
DR PRO; PR:Q9LJ97; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJ97; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:UniProtKB.
DR InterPro; IPR042971; LEA_SMP.
DR InterPro; IPR007011; LEA_SMP_dom.
DR PANTHER; PTHR31174; PTHR31174; 1.
DR Pfam; PF04927; SMP; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..262
FT /note="Late embryogenesis abundant protein 31"
FT /id="PRO_0000436059"
FT DOMAIN 14..68
FT /note="SMP 1"
FT /evidence="ECO:0000255"
FT DOMAIN 136..192
FT /note="SMP 2"
FT /evidence="ECO:0000255"
FT DOMAIN 201..260
FT /note="SMP 3"
FT /evidence="ECO:0000255"
FT MOTIF 6..10
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000269|PubMed:12175017"
FT MUTAGEN 8..9
FT /note="KR->TL: Reduced targeting to nucleus leading to both
FT cytoplasmic and nuclear localization."
FT /evidence="ECO:0000269|PubMed:12175017"
FT CONFLICT 122..127
FT /note="AMEAEV -> VYGKQKL (in Ref. 1; CAA63085)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="A -> S (in Ref. 5; CAA82828)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="S -> I (in Ref. 5; CAA82828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 26744 MW; 368176E81574E795 CRC64;
MSQEEQPKRP QEPVTYGDVF EVSGELADKP IAPEDANMMQ AAETRVFGHT QKGGAAAVMQ
SAATANKRGG FVHPGDTTDL AAERGVTVAQ TDVPGARVTT EFVGGQVVGQ YVEPRPVATA
AAMEAEVVGL SLQSAITIGE ALEATVQTAG NKPVDQSDAA AIQAAEVRAC GTNVIAPGGI
AASAQSAANH NATIDRDEDK IKLIDVLAGA TGKLAADKAV TRQDAEGVVS AELRNNPNLS
THPGGVAASI TAAARLNERA DI
