CR15B_ARATH
ID CR15B_ARATH Reviewed; 141 AA.
AC Q9SIN5; Q39058;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein COLD-REGULATED 15B, chloroplastic {ECO:0000303|PubMed:8260628};
DE Short=AtCOR15B {ECO:0000303|PubMed:8260628};
DE Flags: Precursor;
GN Name=COR15B {ECO:0000303|PubMed:8260628};
GN OrderedLocusNames=At2g42530 {ECO:0000312|Araport:AT2G42530};
GN ORFNames=F14N22 {ECO:0000312|EMBL:AAD23000.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Martin-Cuadrado A.-B., Rodriguez-Valera F., Moreira D., Alba J.-C.,
RA Ivars-Martinez E., Henn M.R., Talla E., Lopez-Garcia P.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY COLD AND ABA.
RX PubMed=8260628; DOI=10.1007/bf00021822;
RA Wilhelm K.S., Thomashow M.F.;
RT "Arabidopsis thaliana cor15b, an apparent homologue of cor15a, is strongly
RT responsive to cold and ABA, but not drought.";
RL Plant Mol. Biol. 23:1073-1077(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
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 [7]
RP INDUCTION BY COLD.
RX PubMed=12481097; DOI=10.1104/pp.008532;
RA Kreps J.A., Wu Y., Chang H.S., Zhu T., Wang X., Harper J.F.;
RT "Transcriptome changes for Arabidopsis in response to salt, osmotic, and
RT cold stress.";
RL Plant Physiol. 130:2129-2141(2002).
RN [8]
RP INDUCTION BY COLD ACCLIMATION.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=15144380; DOI=10.1111/j.1365-313x.2004.02080.x;
RA Rohde P., Hincha D.K., Heyer A.G.;
RT "Heterosis in the freezing tolerance of crosses between two Arabidopsis
RT thaliana accessions (Columbia-0 and C24) that show differences in non-
RT acclimated and acclimated freezing tolerance.";
RL Plant J. 38:790-799(2004).
RN [9]
RP INDUCTION BY COLD.
RX PubMed=18808718; DOI=10.1186/1471-2164-9-434;
RA Robinson S.J., Parkin I.A.;
RT "Differential SAGE analysis in Arabidopsis uncovers increased transcriptome
RT complexity in response to low temperature.";
RL BMC Genomics 9:434-434(2008).
RN [10]
RP INDUCTION BY COMPATIBLE INTERACTION.
RX PubMed=19656045; DOI=10.1094/mpmi-22-9-1104;
RA Huibers R.P., de Jong M., Dekter R.W., Van den Ackerveken G.;
RT "Disease-specific expression of host genes during downy mildew infection of
RT Arabidopsis.";
RL Mol. Plant Microbe Interact. 22:1104-1115(2009).
RN [11]
RP FUNCTION, MISCELLANEOUS, AND SUBUNIT.
RX PubMed=20510170; DOI=10.1016/j.bbamem.2010.05.015;
RA Thalhammer A., Hundertmark M., Popova A.V., Seckler R., Hincha D.K.;
RT "Interaction of two intrinsically disordered plant stress proteins (COR15A
RT and COR15B) with lipid membranes in the dry state.";
RL Biochim. Biophys. Acta 1798:1812-1820(2010).
RN [12]
RP INVOLVEMENT IN SENESCENCE, AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=21673078; DOI=10.1105/tpc.111.084913;
RA Yang S.-D., Seo P.J., Yoon H.-K., Park C.-M.;
RT "The Arabidopsis NAC transcription factor VNI2 integrates abscisic acid
RT signals into leaf senescence via the COR/RD genes.";
RL Plant Cell 23:2155-2168(2011).
CC -!- FUNCTION: Exhibits cryoprotective activity toward stromal substrates in
CC chloroplasts and in protoplasts and confers freezing tolerance to
CC plants in a CBF-dependent manner. Protectant against various stresses
CC (e.g. cold, drought and heat stress) by preventing protein aggregation
CC and attenuating enzyme inactivation. Influences the intrinsic curvature
CC of the inner membrane of the chloroplast envelope, and modulates the
CC freeze-induced lamellar-to-hexagonal II phase transitions that occur in
CC regions where the plasma membrane is brought into close apposition with
CC the chloroplast envelope during freeze-induced osmotic contraction (By
CC similarity). Mediates a shift in the melting curves of phospholipids-
CC containing membranes to lower temperatures (PubMed:20510170). Involved
CC in the regulation of leaf senescence by abscisic acid (ABA) in a VNI2-
CC dependent manner (PubMed:21673078). {ECO:0000250|UniProtKB:Q42512,
CC ECO:0000269|PubMed:20510170, ECO:0000269|PubMed:21673078}.
CC -!- SUBUNIT: Forms homooligomers which interact with potential stromal
CC substrates in the stroma of chloroplasts (By similarity). Interacts
CC with the galactose headgroup of the chloroplast lipid
CC monogalactosyldiacylglycerol (MGDG) (PubMed:20510170).
CC {ECO:0000250|UniProtKB:Q42512, ECO:0000269|PubMed:20510170}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q42512}.
CC -!- INDUCTION: Strongly induced by cold (PubMed:8260628, PubMed:15144380,
CC PubMed:12481097, PubMed:18808718). Accumulates in response to abscisic
CC acid (ABA) (PubMed:8260628, PubMed:21673078). Accumulates during
CC compatible but not during incompatible interactions with the downy
CC mildew pathogen Hyaloperonospora arabidopsidis, and thus belongs to
CC compatible specific (CS) proteins (PubMed:19656045).
CC {ECO:0000269|PubMed:12481097, ECO:0000269|PubMed:15144380,
CC ECO:0000269|PubMed:18808718, ECO:0000269|PubMed:19656045,
CC ECO:0000269|PubMed:21673078, ECO:0000269|PubMed:8260628}.
CC -!- MISCELLANEOUS: Predominantly unstructured in solution and mainly alpha-
CC helical after drying. {ECO:0000269|PubMed:20510170}.
CC -!- SIMILARITY: Belongs to the COR15 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32774.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ156734; ACH95801.1; -; mRNA.
DR EMBL; L24070; AAA32774.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC007087; AAD23000.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10134.1; -; Genomic_DNA.
DR EMBL; AY045809; AAK76483.1; -; mRNA.
DR EMBL; AY091440; AAM14379.1; -; mRNA.
DR EMBL; AY085876; AAM63089.1; -; mRNA.
DR PIR; S43320; S43320.
DR RefSeq; NP_181781.1; NM_129814.3.
DR AlphaFoldDB; Q9SIN5; -.
DR SMR; Q9SIN5; -.
DR STRING; 3702.AT2G42530.1; -.
DR iPTMnet; Q9SIN5; -.
DR PaxDb; Q9SIN5; -.
DR PRIDE; Q9SIN5; -.
DR ProteomicsDB; 222725; -.
DR EnsemblPlants; AT2G42530.1; AT2G42530.1; AT2G42530.
DR GeneID; 818853; -.
DR Gramene; AT2G42530.1; AT2G42530.1; AT2G42530.
DR KEGG; ath:AT2G42530; -.
DR Araport; AT2G42530; -.
DR TAIR; locus:2041534; AT2G42530.
DR HOGENOM; CLU_1951822_0_0_1; -.
DR InParanoid; Q9SIN5; -.
DR OMA; HNVGAKQ; -.
DR OrthoDB; 1517058at2759; -.
DR PhylomeDB; Q9SIN5; -.
DR PRO; PR:Q9SIN5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIN5; baseline and differential.
DR Genevisible; Q9SIN5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:TAIR.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR DisProt; DP01058; -.
PE 1: Evidence at protein level;
KW Chloroplast; Glycoprotein; Lipid-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..141
FT /note="Protein COLD-REGULATED 15B, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432648"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 141 AA; 14961 MW; 72F09F3A224FFCCD CRC64;
MAMSLSGAVL SGMGSSFHNV GAKQSGVGTV RVGRKSELVV VAQRKKSLIY AVKSDGNILD
DLNEATKKAS DFVTDKTKEA LADGEKTKDY IVEKTIEANE TATEEAKKAL DYVTEKGKEA
GNKAAEFVEG KAEEAKNATK S
