ERD10_ARATH
ID ERD10_ARATH Reviewed; 260 AA.
AC P42759; Q8H7D3; Q94AF8; Q94KJ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Dehydrin ERD10;
DE AltName: Full=Low-temperature-induced protein LTI45;
GN Name=ERD10; Synonyms=LTI29, LTI45; OrderedLocusNames=At1g20450;
GN ORFNames=F5M15.21, F5M15_20;
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=7579189; DOI=10.1007/bf00043662;
RA Welin B.V., Olson A., Palva E.T.;
RT "Structure and organization of two closely related low-temperature-induced
RT dhn/lea/rab-like genes in Arabidopsis thaliana L. Heynh.";
RL Plant Mol. Biol. 29:391-395(1995).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-260.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=7948863; DOI=10.1007/bf00039526;
RA Welin B.V., Olson A., Nylander M., Palva E.T.;
RT "Characterization and differential expression of dhn/lea/rab-like genes
RT during cold acclimation and drought stress in Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:131-144(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-183.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42759-1; Sequence=Displayed;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK82471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D17714; BAA04568.1; -; mRNA.
DR EMBL; X90958; CAA62448.1; -; Genomic_DNA.
DR EMBL; AC027665; AAF79613.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29973.1; -; Genomic_DNA.
DR EMBL; AF360351; AAK38607.1; -; mRNA.
DR EMBL; AY136407; AAM97073.1; -; mRNA.
DR EMBL; AY142491; AAN13042.1; -; mRNA.
DR EMBL; BT002131; AAN72142.1; -; mRNA.
DR EMBL; AY048208; AAK82471.1; ALT_INIT; mRNA.
DR EMBL; X77614; CAA54705.1; -; mRNA.
DR EMBL; AF083731; AAN60289.1; -; mRNA.
DR PIR; S60480; S60480.
DR RefSeq; NP_850947.1; NM_180616.3. [P42759-1]
DR AlphaFoldDB; P42759; -.
DR BioGRID; 23872; 2.
DR IntAct; P42759; 1.
DR STRING; 3702.AT1G20450.1; -.
DR iPTMnet; P42759; -.
DR MetOSite; P42759; -.
DR PaxDb; P42759; -.
DR PRIDE; P42759; -.
DR ProteomicsDB; 220621; -. [P42759-1]
DR EnsemblPlants; AT1G20450.1; AT1G20450.1; AT1G20450. [P42759-1]
DR GeneID; 838633; -.
DR Gramene; AT1G20450.1; AT1G20450.1; AT1G20450. [P42759-1]
DR KEGG; ath:AT1G20450; -.
DR Araport; AT1G20450; -.
DR TAIR; locus:2034369; AT1G20450.
DR eggNOG; ENOG502SRR2; Eukaryota.
DR HOGENOM; CLU_081104_0_0_1; -.
DR InParanoid; P42759; -.
DR OrthoDB; 1490579at2759; -.
DR PhylomeDB; P42759; -.
DR PRO; PR:P42759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42759; baseline and differential.
DR Genevisible; P42759; AT.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003779; F:actin binding; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IDA:CAFA.
DR GO; GO:0016151; F:nickel cation binding; IDA:CAFA.
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; IGI:TAIR.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
DR GO; GO:0090559; P:regulation of membrane permeability; IDA:CAFA.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR DisProt; DP00606; -.
DR InterPro; IPR000167; Dehydrin.
DR InterPro; IPR030513; Dehydrin_CS.
DR PANTHER; PTHR33346; PTHR33346; 1.
DR Pfam; PF00257; Dehydrin; 2.
DR PROSITE; PS00315; DEHYDRIN_1; 1.
DR PROSITE; PS00823; DEHYDRIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..260
FT /note="Dehydrin ERD10"
FT /id="PRO_0000100036"
FT REPEAT 184..204
FT /note="1"
FT REPEAT 227..247
FT /note="2"
FT REGION 1..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..247
FT /note="2 X 21 AA repeats, Lys-rich"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42763"
FT CONFLICT 12
FT /note="Q -> H (in Ref. 7; AAN60289)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="H -> G (in Ref. 3; CAA54705)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="G -> D (in Ref. 5; AAK38607)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Q -> E (in Ref. 3; CAA54705)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 5; AAK38607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29548 MW; 318B6FC6B4A1AE5A CRC64;
MAEEYKNTVP EQETPKVATE ESSAPEIKER GMFDFLKKKE EVKPQETTTL ASEFEHKTQI
SEPESFVAKH EEEEHKPTLL EQLHQKHEEE EENKPSLLDK LHRSNSSSSS SSDEEGEDGE
KKKKEKKKKI VEGDHVKTVE EENQGVMDRI KEKFPLGEKP GGDDVPVVTT MPAPHSVEDH
KPEEEEKKGF MDKIKEKLPG HSKKPEDSQV VNTTPLVETA TPIADIPEEK KGFMDKIKEK
LPGYHAKTTG EEEKKEKVSD
