ERD14_ARATH
ID ERD14_ARATH Reviewed; 185 AA.
AC P42763; Q0WV63; Q9C5R5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Dehydrin ERD14;
GN Name=ERD14; OrderedLocusNames=At1g76180; ORFNames=T23E18.12, T23E18_36;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8069491;
RA Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of two cDNAs (ERD10 and ERD14) corresponding to genes
RT that respond rapidly to dehydration stress in Arabidopsis thaliana.";
RL Plant Cell Physiol. 35:225-231(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=18359842; DOI=10.1104/pp.108.118208;
RA Kovacs D., Kalmar E., Torok Z., Tompa P.;
RT "Chaperone activity of ERD10 and ERD14, two disordered stress-related plant
RT proteins.";
RL Plant Physiol. 147:381-390(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Intrinsically disordered protein acting as a chaperone.
CC Prevents heat-induced aggregation and/or inactivation of various
CC substrates. Binds to acidic phospholipid vesicles without affecting
CC membrane fluidity. {ECO:0000269|PubMed:18359842}.
CC -!- TISSUE SPECIFICITY: In stems, cauline leaves, roots and flowers. Low
CC levels found in maturing seeds. Absent in dry seeds.
CC -!- INDUCTION: By dehydration, cold stress and abscisic acid (ABA).
CC Induction by dehydration occurs after 1 hour and increases to a maximum
CC after 10 hours. Cold stress induction peaks at 1 hour and 5 hours after
CC start of cold exposure.
CC -!- SIMILARITY: Belongs to the plant dehydrin family. {ECO:0000305}.
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DR EMBL; D17715; BAA04569.1; -; mRNA.
DR EMBL; AC009978; AAF17644.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35806.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35807.1; -; Genomic_DNA.
DR EMBL; AF324699; AAG40050.2; -; mRNA.
DR EMBL; AF326904; AAG41486.1; -; mRNA.
DR EMBL; AF339722; AAK00404.1; -; mRNA.
DR EMBL; AF428362; AAL16292.1; -; mRNA.
DR EMBL; AY039594; AAK62649.1; -; mRNA.
DR EMBL; AY054151; AAL06812.1; -; mRNA.
DR EMBL; AY054233; AAL06893.1; -; mRNA.
DR EMBL; AY086997; AAM64558.1; -; mRNA.
DR EMBL; AK226910; BAE98985.1; -; mRNA.
DR PIR; F96789; F96789.
DR RefSeq; NP_001185408.1; NM_001198479.1.
DR RefSeq; NP_177745.1; NM_106267.4.
DR AlphaFoldDB; P42763; -.
DR BMRB; P42763; -.
DR BioGRID; 29169; 8.
DR STRING; 3702.AT1G76180.1; -.
DR iPTMnet; P42763; -.
DR PaxDb; P42763; -.
DR PRIDE; P42763; -.
DR ProteomicsDB; 221864; -.
DR EnsemblPlants; AT1G76180.1; AT1G76180.1; AT1G76180.
DR EnsemblPlants; AT1G76180.2; AT1G76180.2; AT1G76180.
DR GeneID; 843950; -.
DR Gramene; AT1G76180.1; AT1G76180.1; AT1G76180.
DR Gramene; AT1G76180.2; AT1G76180.2; AT1G76180.
DR KEGG; ath:AT1G76180; -.
DR Araport; AT1G76180; -.
DR TAIR; locus:2199757; AT1G76180.
DR eggNOG; ENOG502SRR2; Eukaryota.
DR HOGENOM; CLU_081104_1_0_1; -.
DR InParanoid; P42763; -.
DR OMA; YHPKTVE; -.
DR OrthoDB; 1490579at2759; -.
DR PRO; PR:P42763; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42763; baseline and differential.
DR Genevisible; P42763; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:CAFA.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:CAFA.
DR GO; GO:0009631; P:cold acclimation; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
DR GO; GO:0090559; P:regulation of membrane permeability; IDA:CAFA.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IBA:GO_Central.
DR DisProt; DP00667; -.
DR InterPro; IPR000167; Dehydrin.
DR InterPro; IPR030513; Dehydrin_CS.
DR PANTHER; PTHR33346; PTHR33346; 3.
DR Pfam; PF00257; Dehydrin; 1.
DR PROSITE; PS00315; DEHYDRIN_1; 1.
DR PROSITE; PS00823; DEHYDRIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Phosphoprotein; Reference proteome; Repeat;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P42759"
FT CHAIN 2..185
FT /note="Dehydrin ERD14"
FT /id="PRO_0000100037"
FT REPEAT 112..132
FT /note="1"
FT REPEAT 154..174
FT /note="2"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..174
FT /note="2 X 21 AA repeats, Lys-rich"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P42759"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 176
FT /note="T -> P (in Ref. 4; AAG40050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20786 MW; FEDE94706C87F5EE CRC64;
MAEEIKNVPE QEVPKVATEE SSAEVTDRGL FDFLGKKKDE TKPEETPIAS EFEQKVHISE
PEPEVKHESL LEKLHRSDSS SSSSSEEEGS DGEKRKKKKE KKKPTTEVEV KEEEKKGFME
KLKEKLPGHK KPEDGSAVAA APVVVPPPVE EAHPVEKKGI LEKIKEKLPG YHPKTTVEEE
KKDKE
