CHL_ARATH
ID CHL_ARATH Reviewed; 353 AA.
AC Q9STS7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chloroplastic lipocalin {ECO:0000303|PubMed:19674405};
DE Short=AtCHL {ECO:0000303|PubMed:19674405};
DE Flags: Precursor;
GN Name=CHL {ECO:0000303|PubMed:19674405};
GN OrderedLocusNames=At3g47860 {ECO:0000312|EMBL:AEE78341.1};
GN ORFNames=T23J7.190 {ECO:0000312|EMBL:CAB41869.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP DROUGHT; HIGH LIGHT; PARAQUAT AND ABSCISIC ACID TREATMENTS.
RC STRAIN=cv. Columbia;
RX PubMed=19674405; DOI=10.1111/j.1365-313x.2009.03991.x;
RA Levesque-Tremblay G., Havaux M., Ouellet F.;
RT "The chloroplastic lipocalin AtCHL prevents lipid peroxidation and protects
RT Arabidopsis against oxidative stress.";
RL Plant J. 60:691-702(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE 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).
CC -!- FUNCTION: Lipocalin that prevents thylakoidal membrane lipids
CC peroxidation and confers protection against oxidative stress,
CC especially mediated by singlet oxygen in response to high light and
CC other stress (e.g. heat shocks) (PubMed:19674405, PubMed:23837879).
CC Required for seed longevity by insuring polyunsaturated lipids
CC integrity (PubMed:23837879). {ECO:0000269|PubMed:19674405,
CC ECO:0000269|PubMed:23837879}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:19674405}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves at low levels (at protein
CC levels) (PubMed:23837879). Present in seeds (PubMed:23837879).
CC {ECO:0000269|PubMed:23837879}.
CC -!- INDUCTION: Accumulates in response to drought, high light, paraquat and
CC abscisic acid (ABA) treatments (at protein level).
CC {ECO:0000269|PubMed:19674405}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to photo-oxidative stress
CC induced by drought, high light or paraquat, associated with a rapid
CC accumulation of hydroxy fatty acids mediated by singlet oxygen
CC (PubMed:19674405). When associated with disruption in TIL, highly
CC sensitive to temperature, drought and light stresses than the single
CC mutants, exhibiting intense lipid peroxidation. Seeds of this double
CC mutant are very sensitive to natural and artificial aging, associated
CC with the oxidation of polyunsaturated lipids (PubMed:23837879).
CC {ECO:0000269|PubMed:19674405, ECO:0000269|PubMed:23837879}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AL049746; CAB41869.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78341.1; -; Genomic_DNA.
DR EMBL; AY035165; AAK59669.1; -; mRNA.
DR EMBL; AY044334; AAK73275.1; -; mRNA.
DR EMBL; BT003002; AAO22810.1; -; mRNA.
DR PIR; T07725; T07725.
DR RefSeq; NP_190370.1; NM_114656.4.
DR AlphaFoldDB; Q9STS7; -.
DR SMR; Q9STS7; -.
DR STRING; 3702.AT3G47860.1; -.
DR iPTMnet; Q9STS7; -.
DR PaxDb; Q9STS7; -.
DR PRIDE; Q9STS7; -.
DR ProteomicsDB; 245181; -.
DR EnsemblPlants; AT3G47860.1; AT3G47860.1; AT3G47860.
DR GeneID; 823942; -.
DR Gramene; AT3G47860.1; AT3G47860.1; AT3G47860.
DR KEGG; ath:AT3G47860; -.
DR Araport; AT3G47860; -.
DR TAIR; locus:2100407; AT3G47860.
DR eggNOG; KOG4824; Eukaryota.
DR HOGENOM; CLU_072934_0_0_1; -.
DR InParanoid; Q9STS7; -.
DR OMA; DPGPEFI; -.
DR OrthoDB; 1631943at2759; -.
DR PhylomeDB; Q9STS7; -.
DR PRO; PR:Q9STS7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STS7; baseline and differential.
DR Genevisible; Q9STS7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; IDA:TAIR.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:UniProtKB.
DR GO; GO:0010117; P:photoprotection; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP: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:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:1901562; P:response to paraquat; IEP:UniProtKB.
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; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF08212; Lipocalin_2; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Lipid metabolism; Plastid; Reference proteome;
KW Seed storage protein; Storage protein; Thylakoid; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..353
FT /note="Chloroplastic lipocalin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434133"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 163..299
FT /evidence="ECO:0000250|UniProtKB:P05090"
SQ SEQUENCE 353 AA; 39116 MW; 14A83B0CF1BA8D0D CRC64;
MILLSSSISL SRPVSSQSFS PPAATSTRRS HSSVTVKCCC SSRRLLKNPE LKCSLENLFE
IQALRKCFVS GFAAILLLSQ AGQGIALDLS SGYQNICQLG SAAAVGENKL TLPSDGDSES
MMMMMMRGMT AKNFDPVRYS GRWFEVASLK RGFAGQGQED CHCTQGVYTF DMKESAIRVD
TFCVHGSPDG YITGIRGKVQ CVGAEDLEKS ETDLEKQEMI KEKCFLRFPT IPFIPKLPYD
VIATDYDNYA LVSGAKDKGF VQVYSRTPNP GPEFIAKYKN YLAQFGYDPE KIKDTPQDCE
VTDAELAAMM SMPGMEQTLT NQFPDLGLRK SVQFDPFTSV FETLKKLVPL YFK
