LTI65_ARATH
ID LTI65_ARATH Reviewed; 619 AA.
AC Q04980; Q06737; Q42275; Q8RXF6; Q9FHC9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Low-temperature-induced 65 kDa protein;
DE AltName: Full=Desiccation-responsive protein 29B;
GN Name=LTI65; Synonyms=RD29B; OrderedLocusNames=At5g52300; ORFNames=K24M7.3;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8448363; DOI=10.1007/bf00014547;
RA Nordin K., Vahala T., Palva E.T.;
RT "Differential expression of two related, low-temperature-induced genes in
RT Arabidopsis thaliana (L.) Heynh.";
RL Plant Mol. Biol. 21:641-653(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8310052; DOI=10.1104/pp.101.3.1119;
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Arabidopsis DNA encoding two desiccation-responsive rd29 genes.";
RL Plant Physiol. 101:1119-1120(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8437577; DOI=10.1007/bf00277130;
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of the expression of a desiccation-responsive rd29 gene
RT of Arabidopsis thaliana and analysis of its promoter in transgenic
RT plants.";
RL Mol. Gen. Genet. 236:331-340(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-121.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
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=Q04980-1; Sequence=Displayed;
CC -!- INDUCTION: By low temperature, and mostly by water stress or abscisic
CC acid (ABA). {ECO:0000269|PubMed:8437577}.
CC -!- SIMILARITY: Belongs to the LTI78/LTI65 family. {ECO:0000305}.
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DR EMBL; X67670; CAA47902.1; -; Genomic_DNA.
DR EMBL; D13044; BAA02375.1; -; Genomic_DNA.
DR EMBL; AB019226; BAB10527.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96197.1; -; Genomic_DNA.
DR EMBL; AY081282; AAL91171.1; -; mRNA.
DR EMBL; AY128731; AAM91131.1; -; mRNA.
DR EMBL; Z34014; CAA83975.1; -; mRNA.
DR PIR; S30153; S30153.
DR RefSeq; NP_200043.2; NM_124609.4. [Q04980-1]
DR AlphaFoldDB; Q04980; -.
DR BioGRID; 20551; 1.
DR STRING; 3702.AT5G52300.1; -.
DR iPTMnet; Q04980; -.
DR PaxDb; Q04980; -.
DR PRIDE; Q04980; -.
DR ProteomicsDB; 238806; -. [Q04980-1]
DR EnsemblPlants; AT5G52300.1; AT5G52300.1; AT5G52300. [Q04980-1]
DR GeneID; 835306; -.
DR Gramene; AT5G52300.1; AT5G52300.1; AT5G52300. [Q04980-1]
DR KEGG; ath:AT5G52300; -.
DR Araport; AT5G52300; -.
DR TAIR; locus:2156652; AT5G52300.
DR eggNOG; ENOG502QU29; Eukaryota.
DR HOGENOM; CLU_024021_0_0_1; -.
DR InParanoid; Q04980; -.
DR OMA; HQTPMKT; -.
DR PhylomeDB; Q04980; -.
DR PRO; PR:Q04980; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q04980; baseline and differential.
DR Genevisible; Q04980; AT.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR InterPro; IPR012418; CAP160.
DR InterPro; IPR037491; LTI78/LTI65.
DR PANTHER; PTHR33836; PTHR33836; 1.
DR Pfam; PF07918; CAP160; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..619
FT /note="Low-temperature-induced 65 kDa protein"
FT /id="PRO_0000084510"
FT REPEAT 404..408
FT /note="1"
FT REPEAT 442..446
FT /note="2"
FT REPEAT 460..464
FT /note="3"
FT REPEAT 490..494
FT /note="4"
FT REPEAT 507..511
FT /note="5"
FT REGION 1..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..511
FT /note="5 X 5 AA repeats of [IV]-[AMS]-[EST]-K-L"
FT REGION 408..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06738"
FT CONFLICT 24..43
FT /note="Missing (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..87
FT /note="PVYESSAV -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..83
FT /note="YE -> FD (in Ref. 7; CAA83975)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="Missing (in Ref. 1, 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="N -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="V -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..619
FT /note="TMGFSDSGGSELGGSGGGKGVQDSGN -> KISLVLAVTRNVKILMCVNF
FT (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..619
FT /note="TMGFSDSGGSELGGSGGGKGVQDSGN -> KTPSSLCYT (in Ref. 1;
FT BAA02375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 65971 MW; F2D2DF9C5990A00A CRC64;
MESQLTRPYG HEQAEEPIRI HHPEEEEHHE KGASKVLKKV KEKAKKIKNS LTKHGNGHDH
DVEDDDDEYD EQDPEVHGAP VYESSAVRGG VTGKPKSLSH AGETNVPASE EIVPPGTKVF
PVVSSDHTKP IEPVSLQDTS YGHEALADPV RTTETSDWEA KREAPTHYPL GVSEFSDRGE
SREAHQEPLN TPVSLLSATE DVTRTFAPGG EDDYLGGQRK VNVETPKRLE EDPAAPGGGS
DYLSGVSNYQ SKVTDPTHKG GEAGVPEIAE SLGRMKVTDE SPDQKSRQGR EEDFPTRSHE
FDLKKESDIN KNSPARFGGE SKAGMEEDFP TRGDVKVESG LGRDLPTGTH DQFSPELSRP
KERDDSEETK DESTHETKPS TYTEQLASAT SAITNKAIAA KNVVASKLGY TGENGGGQSE
SPVKDETPRS VTAYGQKVAG TVAEKLTPVY EKVKETGSTV MTKLPLSGGG SGVKETQQGE
EKGVTAKNYI SEKLKPGEED KALSEMIAEK LHFGGGGEKK TTATKEVEVT VEKIPSDQIA
EGKGHGEAVA EEGKGGEGMV GKVKGAVTSW LGGKPKSPRS VEESPQSLGT TVGTMGFSDS
GGSELGGSGG GKGVQDSGN
