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   24-JAN-2024, entry version 147.
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 ensuring 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.Q9STS7; -.
DR   iPTMnet; Q9STS7; -.
DR   PaxDb; 3702-AT3G47860-1; -.
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; AT3G47860; CHL.
DR   eggNOG; KOG4824; Eukaryota.
DR   HOGENOM; CLU_072934_0_0_1; -.
DR   InParanoid; Q9STS7; -.
DR   OMA; MPGMEQT; -.
DR   OrthoDB; 5342507at2759; -.
DR   PhylomeDB; Q9STS7; -.
DR   PRO; PR:Q9STS7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STS7; baseline and differential.
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:SF32; CHLOROPLASTIC LIPOCALIN; 1.
DR   PANTHER; PTHR11430; LIPOCALIN; 1.
DR   Pfam; PF08212; Lipocalin_2; 1.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
DR   Genevisible; Q9STS7; AT.
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
//