TIL_ARATH
ID TIL_ARATH Reviewed; 186 AA.
AC Q9FGT8; Q8LE12;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Temperature-induced lipocalin-1 {ECO:0000303|PubMed:18671872};
DE Short=AtTIL1 {ECO:0000303|PubMed:18671872};
GN Name=TIL {ECO:0000303|PubMed:18671872};
GN OrderedLocusNames=At5g58070 {ECO:0000312|EMBL:AED96994.1};
GN ORFNames=K21L19.6 {ECO:0000312|EMBL:AAL32867.1};
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|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
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 [4]
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 [5]
RP INDUCTION BY DROUGHT AND HEAT.
RX PubMed=15047901; DOI=10.1104/pp.103.033431;
RA Rizhsky L., Liang H., Shuman J., Shulaev V., Davletova S., Mittler R.;
RT "When defense pathways collide. The response of Arabidopsis to a
RT combination of drought and heat stress.";
RL Plant Physiol. 134:1683-1696(2004).
RN [6]
RP INDUCTION BY YARIV PHENYLGLYCOSIDE.
RX PubMed=15235117; DOI=10.1104/pp.104.039370;
RA Guan Y., Nothnagel E.A.;
RT "Binding of arabinogalactan proteins by Yariv phenylglycoside triggers
RT wound-like responses in Arabidopsis cell cultures.";
RL Plant Physiol. 135:1346-1366(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18671872; DOI=10.1186/1471-2229-8-86;
RA Charron J.-B.F., Ouellet F., Houde M., Sarhan F.;
RT "The plant Apolipoprotein D ortholog protects Arabidopsis against oxidative
RT stress.";
RL BMC Plant Biol. 8:86-86(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=19302169; DOI=10.1111/j.1365-3040.2009.01972.x;
RA Chi W.T., Fung R.W., Liu H.C., Hsu C.C., Charng Y.Y.;
RT "Temperature-induced lipocalin is required for basal and acquired
RT thermotolerance in Arabidopsis.";
RL Plant Cell Environ. 32:917-927(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20959419; DOI=10.1104/pp.110.164152;
RA Brinker M., Brosche M., Vinocur B., Abo-Ogiala A., Fayyaz P., Janz D.,
RA Ottow E.A., Cullmann A.D., Saborowski J., Kangasjarvi J., Altman A.,
RA Polle A.;
RT "Linking the salt transcriptome with physiological responses of a salt-
RT resistant Populus species as a strategy to identify genes important for
RT stress acclimation.";
RL Plant Physiol. 154:1697-1709(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24028869; DOI=10.1016/j.jplph.2013.08.003;
RA Abo-Ogiala A., Carsjens C., Diekmann H., Fayyaz P., Herrfurth C.,
RA Feussner I., Polle A.;
RT "Temperature-induced lipocalin (TIL) is translocated under salt stress and
RT protects chloroplasts from ion toxicity.";
RL J. Plant Physiol. 171:250-259(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23837879; DOI=10.1111/pce.12159;
RA Boca S., Koestler F., Ksas B., Chevalier A., Leymarie J., Fekete A.,
RA Mueller M.J., Havaux M.;
RT "Arabidopsis lipocalins AtCHL and AtTIL have distinct but overlapping
RT functions essential for lipid protection and seed longevity.";
RL Plant Cell Environ. 37:368-381(2014).
RN [12]
RP SUBCELLULAR LOCATION, HPR MOTIF, DOMAIN, AND MUTAGENESIS OF PRO-90; PRO-91;
RP 92-PHE--ILE-96; PRO-94 AND PRO-97.
RX PubMed=25957952; DOI=10.1007/s11103-015-0326-x;
RA Hernandez-Gras F., Boronat A.;
RT "A hydrophobic proline-rich motif is involved in the intracellular
RT targeting of temperature-induced lipocalin.";
RL Plant Mol. Biol. 88:301-311(2015).
CC -!- FUNCTION: Involved in basal (BT) and acquired thermotolerance (AT),
CC probably by preventing plasma membrane lipids peroxidation induced by
CC severe heat-shock (HS) (PubMed:19302169, PubMed:23837879). Lipocalin
CC that confers protection against oxidative stress caused by heat,
CC freezing, paraquat and light (PubMed:18671872, PubMed:19302169).
CC Confers resistance to high salt (NaCl) levels, probably by protecting
CC chloroplasts from ion toxicity via ion homeostasis maintenance
CC (PubMed:20959419, PubMed:24028869). Required for seed longevity by
CC insuring polyunsaturated lipids integrity (PubMed:23837879).
CC {ECO:0000269|PubMed:18671872, ECO:0000269|PubMed:19302169,
CC ECO:0000269|PubMed:20959419, ECO:0000269|PubMed:23837879,
CC ECO:0000269|PubMed:24028869}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19302169,
CC ECO:0000269|PubMed:23837879, ECO:0000269|PubMed:24028869,
CC ECO:0000269|PubMed:25957952}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:24028869,
CC ECO:0000269|PubMed:25957952}; Cytoplasmic side
CC {ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:24028869}. Cytoplasm
CC {ECO:0000269|PubMed:24028869}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:24028869}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24028869}; Cytoplasmic side
CC {ECO:0000269|PubMed:24028869}. Note=Translocates from cell membrane to
CC cytoplasm upon salinity stress. A small fraction is associated with the
CC chloroplast envelope. {ECO:0000269|PubMed:24028869}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at similar levels, except in
CC dry seeds (at protein level) (PubMed:18671872, PubMed:19302169).
CC Present in seeds (PubMed:23837879). {ECO:0000269|PubMed:18671872,
CC ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:23837879}.
CC -!- INDUCTION: By drought and heat combination stress (PubMed:15047901).
CC Accumulates upon treatment with 50 mM (beta-D -Glc)(3), a Yariv
CC phenylglycoside that aggregates arabinogalactan-proteins (AGPs)
CC (PubMed:15235117). {ECO:0000269|PubMed:15047901,
CC ECO:0000269|PubMed:15235117}.
CC -!- DOMAIN: The HPR motif (90-97) is required for intracellular targeting
CC at membranes. {ECO:0000269|PubMed:25957952}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to sudden drops in
CC temperature and paraquat treatment. Dark-grown plants die shortly after
CC transfer to light. These phenotypes are associated with an accumulation
CC of hydrogen peroxide and other ROS, which causes an oxidative stress
CC that leads to a reduction in hypocotyl growth and sensitivity to light
CC (PubMed:18671872). Severe defects in basal (BT) and acquired
CC thermotolerance (AT) leading to death within 7 days. Stronger
CC sensitivity to tert-butyl hydroperoxide, a reagent that induces lipid
CC peroxidation (PubMed:19302169). Stronger sensitivity to high salt
CC levels (NaCl) associated with membrane injury, chlorophyll b
CC degradation and accumulation of chloride and sodium in chloroplasts
CC (PubMed:20959419, PubMed:24028869). When associated with disruption in
CC CHL, highly sensitive to temperature, drought and light stresses than
CC the single mutants, exhibiting intense lipid peroxidation. Seeds of
CC this double mutant are very sensitive to natural and artificial aging,
CC associated with the oxidation of polyunsaturated lipids
CC (PubMed:23837879). {ECO:0000269|PubMed:18671872,
CC ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:20959419,
CC ECO:0000269|PubMed:23837879, ECO:0000269|PubMed:24028869}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62904.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB024029; BAB10998.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96994.1; -; Genomic_DNA.
DR EMBL; AY062789; AAL32867.1; -; mRNA.
DR EMBL; AY081612; AAM10174.1; -; mRNA.
DR EMBL; AY085685; AAM62904.1; ALT_INIT; mRNA.
DR RefSeq; NP_200615.1; NM_125192.4.
DR AlphaFoldDB; Q9FGT8; -.
DR SMR; Q9FGT8; -.
DR STRING; 3702.AT5G58070.1; -.
DR MetOSite; Q9FGT8; -.
DR PaxDb; Q9FGT8; -.
DR PRIDE; Q9FGT8; -.
DR ProMEX; Q9FGT8; -.
DR ProteomicsDB; 234374; -.
DR EnsemblPlants; AT5G58070.1; AT5G58070.1; AT5G58070.
DR GeneID; 835919; -.
DR Gramene; AT5G58070.1; AT5G58070.1; AT5G58070.
DR KEGG; ath:AT5G58070; -.
DR Araport; AT5G58070; -.
DR TAIR; locus:2155831; AT5G58070.
DR eggNOG; KOG4824; Eukaryota.
DR HOGENOM; CLU_068449_3_1_1; -.
DR OMA; SQFYKDK; -.
DR OrthoDB; 1631943at2759; -.
DR PhylomeDB; Q9FGT8; -.
DR PRO; PR:Q9FGT8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGT8; baseline and differential.
DR Genevisible; Q9FGT8; AT.
DR GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:1901562; P:response to paraquat; IMP:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IMP:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR002446; Lipocalin_bac.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF08212; Lipocalin_2; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR01171; BCTLIPOCALIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloroplast; Cytoplasm; Lipid metabolism; Lipoprotein;
KW Membrane; Plastid; Reference proteome; Seed storage protein;
KW Storage protein.
FT CHAIN 1..186
FT /note="Temperature-induced lipocalin-1"
FT /id="PRO_0000434134"
FT REGION 154..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 90..97
FT /note="HPR (Hydrophobic proline-rich)"
FT /evidence="ECO:0000305|PubMed:25957952"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 90
FT /note="P->V: Partially altered subcellular localization."
FT /evidence="ECO:0000269|PubMed:25957952"
FT MUTAGEN 91
FT /note="P->V: Partially altered subcellular localization."
FT /evidence="ECO:0000269|PubMed:25957952"
FT MUTAGEN 92..96
FT /note="FLPII->SAPAR: Impaired subcellular localization."
FT /evidence="ECO:0000269|PubMed:25957952"
FT MUTAGEN 94
FT /note="P->V: Impaired subcellular localization."
FT /evidence="ECO:0000269|PubMed:25957952"
FT MUTAGEN 97
FT /note="P->V: Partially altered subcellular localization."
FT /evidence="ECO:0000269|PubMed:25957952"
SQ SEQUENCE 186 AA; 21434 MW; 408EF049B4B0325E CRC64;
MTEKKEMEVV KGLNVERYMG RWYEIASFPS RFQPKNGVDT RATYTLNPDG TIHVLNETWS
NGKRGFIEGS AYKADPKSDE AKLKVKFYVP PFLPIIPVTG DYWVLYIDPD YQHALIGQPS
RSYLWILSRT AQMEEETYKQ LVEKAVEEGY DISKLHKTPQ SDTPPESNTA PEDSKGVWWF
KSLFGK
