CRL_ARATH
ID CRL_ARATH Reviewed; 269 AA.
AC Q9FI46; Q8LCJ3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chromophore lyase CRL, chloroplastic;
DE EC=4.-.-.-;
DE AltName: Full=Protein CONSTITUTIVE ACTIVATOR OF AAA-ATPase 33;
DE AltName: Full=Protein CRUMPLED LEAF;
GN Name=CRL; Synonyms=CAA33; OrderedLocusNames=At5g51020; ORFNames=K3K7.20;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15086805; DOI=10.1111/j.1365-313x.2004.02057.x;
RA Asano T., Yoshioka Y., Kurei S., Sakamoto W., Sodmergen X., Machida Y.;
RT "A mutation of the CRUMPLED LEAF gene that encodes a protein localized in
RT the outer envelope membrane of plastids affects the pattern of cell
RT division, cell differentiation, and plastid division in Arabidopsis.";
RL Plant J. 38:448-459(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19318374; DOI=10.1093/pcp/pcp047;
RA Chen Y., Asano T., Fujiwara M.T., Yoshida S., Machida Y., Yoshioka Y.;
RT "Plant cells without detectable plastids are generated in the crumpled leaf
RT mutant of Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:956-969(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CABBAGE LEAF CURL VIRUS.
RC STRAIN=cv. Columbia;
RX PubMed=19840398; DOI=10.1186/1743-422x-6-169;
RA Trejo-Saavedra D.L., Vielle-Calzada J.P., Rivera-Bustamante R.F.;
RT "The infective cycle of Cabbage leaf curl virus (CaLCuV) is affected by
RT CRUMPLED LEAF (CRL) gene in Arabidopsis thaliana.";
RL Virol. J. 6:169-169(2009).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-31.
RC STRAIN=cv. Columbia;
RX PubMed=22014227; DOI=10.1111/j.1365-313x.2011.04825.x;
RA Simkova K., Kim C., Gacek K., Baruah A., Laloi C., Apel K.;
RT "The chloroplast division mutant caa33 of Arabidopsis thaliana reveals the
RT crucial impact of chloroplast homeostasis on stress acclimation and
RT retrograde plastid-to-nucleus signaling.";
RL Plant J. 69:701-712(2012).
CC -!- FUNCTION: Covalently attaches a chromophore to Cys residue(s) of
CC phycobiliproteins (By similarity). Required for plastid division, and
CC involved in cell differentiation and regulation of the cell division
CC plane. Maintenance of plastid homeostasis controls plant
CC preconditioning to stress and stress acclimation. {ECO:0000250,
CC ECO:0000269|PubMed:15086805, ECO:0000269|PubMed:19318374,
CC ECO:0000269|PubMed:19840398, ECO:0000269|PubMed:22014227}.
CC -!- FUNCTION: Confers sensitivity to cabbage leaf curl virus (CaLCuV),
CC probably by supporting viral movement.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:15086805}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15086805}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in shoot apices, to a lower
CC extent, in leaves, inflorescence stems, buds and cotyledons, and, at
CC low levels, in roots and siliques. {ECO:0000269|PubMed:15086805}.
CC -!- INDUCTION: Transient strong induction in response to cabbage leaf curl
CC virus (CaLCuV) infection at an early stage.
CC {ECO:0000269|PubMed:19840398}.
CC -!- DISRUPTION PHENOTYPE: Abnormal organ morphology (e.g. pale green,
CC reduced stature, crumpled and irregular margins in leaves and floral
CC organs, and shorter roots) due to altered pattern of cell division and
CC differentiation. Impaired plastid division leading to enlarged
CC chloroplasts and the formation of cells lacking plastids. Reduced
CC susceptibility to viral infection by cabbage leaf curl virus (CaLCuV).
CC {ECO:0000269|PubMed:15086805, ECO:0000269|PubMed:19318374,
CC ECO:0000269|PubMed:19840398}.
CC -!- SIMILARITY: Belongs to the CpcT/CpeT biliprotein lyase family.
CC {ECO:0000305}.
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DR EMBL; AB120415; BAD12566.1; -; mRNA.
DR EMBL; AB017063; BAB08748.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96022.1; -; Genomic_DNA.
DR EMBL; AF370196; AAK44011.1; -; mRNA.
DR EMBL; AY113932; AAM44980.1; -; mRNA.
DR EMBL; AY086572; AAM63635.1; -; mRNA.
DR RefSeq; NP_199915.1; NM_124481.4.
DR PDB; 6LIX; X-ray; 2.38 A; A/B=1-269.
DR PDB; 6LIY; X-ray; 1.76 A; A/B=1-269.
DR PDBsum; 6LIX; -.
DR PDBsum; 6LIY; -.
DR AlphaFoldDB; Q9FI46; -.
DR SMR; Q9FI46; -.
DR BioGRID; 20420; 2.
DR STRING; 3702.AT5G51020.1; -.
DR PaxDb; Q9FI46; -.
DR PRIDE; Q9FI46; -.
DR ProteomicsDB; 224531; -.
DR EnsemblPlants; AT5G51020.1; AT5G51020.1; AT5G51020.
DR GeneID; 835175; -.
DR Gramene; AT5G51020.1; AT5G51020.1; AT5G51020.
DR KEGG; ath:AT5G51020; -.
DR Araport; AT5G51020; -.
DR TAIR; locus:2157398; AT5G51020.
DR eggNOG; ENOG502QU5I; Eukaryota.
DR HOGENOM; CLU_077016_0_0_1; -.
DR InParanoid; Q9FI46; -.
DR OMA; YMSKCER; -.
DR OrthoDB; 1048268at2759; -.
DR PhylomeDB; Q9FI46; -.
DR PRO; PR:Q9FI46; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI46; baseline and differential.
DR Genevisible; Q9FI46; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043572; P:plastid fission; IMP:TAIR.
DR GO; GO:0017009; P:protein-phycocyanobilin linkage; IEA:InterPro.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
DR GO; GO:0046741; P:transport of virus in host, tissue to tissue; IMP:UniProtKB.
DR CDD; cd16338; CpcT; 1.
DR Gene3D; 2.40.128.590; -; 1.
DR InterPro; IPR010404; CpcT/CpeT.
DR InterPro; IPR038672; CpcT/CpeT_sf.
DR PANTHER; PTHR35137; PTHR35137; 1.
DR Pfam; PF06206; CpeT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chloroplast;
KW Developmental protein; Lyase; Membrane; Plant defense; Plastid;
KW Plastid outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..269
FT /note="Chromophore lyase CRL, chloroplastic"
FT /id="PRO_0000429739"
FT TRANSMEM 19..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 31
FT /note="G->D: In crl-2; impeded plastid division leading to
FT enlarged chloroplasts in mesophyll cells and abnormal
FT plastid homeostasis, thus resulting in preconditioning
FT plants by activating the expression of stress genes,
FT enhancing pathogen resistance (e.g. Pseudomonas syringae
FT DC3000) and attenuating the capacity to respond to plastid
FT signals. Spontaneous light intensity-dependent cell death
FT formation associated with O(2) production."
FT /evidence="ECO:0000269|PubMed:22014227"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6LIY"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:6LIY"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6LIY"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6LIY"
SQ SEQUENCE 269 AA; 30330 MW; 80F14DF12E717E98 CRC64;
MGTESGSDPE SSSNGWSRAR GLVVKTLVLI GGALLIKRLT KSTTRRDHAR VVSRSLTGEK
FTREQASRDP DNYFNIRMLS CPAAEMVDGS EVLYLEQAFW RTPQKPFRQR LYMVKPCPKE
LKCDVEVSSY AIRDAEEYKN FCDRPKDQRP LPEEVIGDIG EHLTTIHLNC CDRGKRCLYE
GSTSPGGFPN SWNGASYCTS DLAVLKNNEI HLWDRGFDEN RNQVWGPKEG PYEFKPATSS
SINENLSALN ILYQSSIDKP IQGSLILQD
