CTL1_ARATH
ID CTL1_ARATH Reviewed; 321 AA.
AC Q9MA41; C0SUT2; Q42042;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Chitinase-like protein 1;
DE Short=AtCTL1;
DE AltName: Full=Protein ANION ALTERED ROOT MORPHOLOGY;
DE AltName: Full=Protein ECTOPIC DEPOSITION OF LIGNIN IN PITH 1;
DE AltName: Full=Protein ECTOPIC ROOT HAIR 2;
DE AltName: Full=Protein POM-POM1;
DE AltName: Full=Protein SENSITIVE TO HOT TEMPERATURES 2;
DE Flags: Precursor;
GN Name=CTL1; Synonyms=ARM, ELP1, ERH2, HOT2, POM1;
GN OrderedLocusNames=At1g05850; ORFNames=T20M3.12;
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING AND ETHYLENE.
RX PubMed=11826306; DOI=10.1105/tpc.010278;
RA Zhong R., Kays S.J., Schroeder B.P., Ye Z.H.;
RT "Mutation of a chitinase-like gene causes ectopic deposition of lignin,
RT aberrant cell shapes, and overproduction of ethylene.";
RL Plant Cell 14:165-179(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-166.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Hofte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7743935; DOI=10.1242/dev.121.4.1237;
RA Hauser M.-T., Morikami A., Benfey P.N.;
RT "Conditional root expansion mutants of Arabidopsis.";
RL Development 121:1237-1252(1995).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9165126; DOI=10.1242/dev.124.9.1789;
RA Schneider K., Wells B., Dolan L., Roberts K.;
RT "Structural and genetic analysis of epidermal cell differentiation in
RT Arabidopsis primary roots.";
RL Development 124:1789-1798(1997).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10760305; DOI=10.1073/pnas.97.8.4392;
RA Hong S.-W., Vierling E.;
RT "Mutants of Arabidopsis thaliana defective in the acquisition of tolerance
RT to high temperature stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4392-4397(2000).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10806225; DOI=10.1104/pp.123.1.59;
RA Zhong R., Ripperger A., Ye Z.-H.;
RT "Ectopic deposition of lignin in the pith of stems of two Arabidopsis
RT mutants.";
RL Plant Physiol. 123:59-70(2000).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12805605; DOI=10.1104/pp.102.017145;
RA Hong S.-W., Lee U., Vierling E.;
RT "Arabidopsis hot mutants define multiple functions required for acclimation
RT to high temperatures.";
RL Plant Physiol. 132:757-767(2003).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15908600; DOI=10.1104/pp.105.059774;
RA Yuen C.Y., Sedbrook J.C., Perrin R.M., Carroll K.L., Masson P.H.;
RT "Loss-of-function mutations of ROOT HAIR DEFECTIVE3 suppress root waving,
RT skewing, and epidermal cell file rotation in Arabidopsis.";
RL Plant Physiol. 138:701-714(2005).
RN [13]
RP FUNCTION, MUTAGENESIS OF GLY-188, AND DISRUPTION PHENOTYPE.
RX PubMed=17156413; DOI=10.1111/j.1365-313x.2006.02950.x;
RA Kwon Y., Kim S.-H., Jung M.-S., Kim M.-S., Oh J.-E., Ju H.-W., Kim K.-I.,
RA Vierling E., Lee H., Hong S.-W.;
RT "Arabidopsis hot2 encodes an endochitinase-like protein that is essential
RT for tolerance to heat, salt and drought stresses.";
RL Plant J. 49:184-193(2007).
RN [14]
RP FUNCTION, MUTAGENESIS OF SER-168, AND TISSUE SPECIFICITY.
RX PubMed=20007445; DOI=10.1104/pp.109.149849;
RA Hermans C., Porco S., Verbruggen N., Bush D.R.;
RT "Chitinase-like protein CTL1 plays a role in altering root system
RT architecture in response to multiple environmental conditions.";
RL Plant Physiol. 152:904-917(2010).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20056293; DOI=10.1016/j.jplph.2009.12.001;
RA Hossain M.A., Noh H.N., Kim K.I., Koh E.J., Wi S.G., Bae H.J., Lee H.,
RA Hong S.W.;
RT "Mutation of the chitinase-like protein-encoding AtCTL2 gene enhances
RT lignin accumulation in dark-grown Arabidopsis seedlings.";
RL J. Plant Physiol. 167:650-658(2010).
CC -!- FUNCTION: No chitinase activity. Essential for normal plant growth and
CC development. Regulates cell expansion extent and differentiation at
CC least in roots and hypocotyls. Prevents lignin accumulation in the
CC pith. May modulate ethylene-mediated regulation during development.
CC Probably required to establish thermotolerance acclimation. Plays a
CC role for controlled anisotropic cell expansion in the regulation of
CC waving during root gravitropism and thigmotropism. Involved in the root
CC system architecture adaptation to multiple environmental conditions
CC such as nitrate. Contributes to salt tolerance and possibly to drought
CC by preventing the overaccumulation of sodium ions.
CC {ECO:0000269|PubMed:10760305, ECO:0000269|PubMed:10806225,
CC ECO:0000269|PubMed:11826306, ECO:0000269|PubMed:12805605,
CC ECO:0000269|PubMed:15908600, ECO:0000269|PubMed:17156413,
CC ECO:0000269|PubMed:20007445, ECO:0000269|PubMed:20056293,
CC ECO:0000269|PubMed:7743935, ECO:0000269|PubMed:9165126}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings shoots and roots,
CC stems, and flowers, and, to a lower extent, in flowers, mature leaves
CC and roots. {ECO:0000269|PubMed:11826306, ECO:0000269|PubMed:20007445,
CC ECO:0000269|PubMed:20056293}.
CC -!- INDUCTION: Repressed after wounding or treatment with ethylene.
CC {ECO:0000269|PubMed:11826306}.
CC -!- DISRUPTION PHENOTYPE: Abnormal root expansion with ectopic root-hairs,
CC reduced growth, excess lateral stems and smaller leaves. Loss of
CC regulation of the extent of root epidermal and cortex cell expansion.
CC Ectopic deposition of lignin and aberrant shapes of cells with
CC incomplete cell walls in the pith of inflorescence stems. Exaggerated
CC hook curvature, reduced length and increased diameter of hypocotyls in
CC dark-grown seedlings, and reduced root length and increased number of
CC root hairs in light-grown seedlings. Increased ethylene production.
CC Exhibit also thermotolerance defect. Lacks the lefthanded root
CC epidermal cell file rotation (CFR) and enhanced root skewing in
CC response to low doses of propyzamide. Aberrant reduced tolerance to
CC salt and drought stresses, with accumulated of sodium ions.
CC {ECO:0000269|PubMed:10760305, ECO:0000269|PubMed:10806225,
CC ECO:0000269|PubMed:11826306, ECO:0000269|PubMed:12805605,
CC ECO:0000269|PubMed:15908600, ECO:0000269|PubMed:17156413,
CC ECO:0000269|PubMed:7743935, ECO:0000269|PubMed:9165126}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. {ECO:0000305}.
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DR EMBL; AF422178; AAL37736.1; -; mRNA.
DR EMBL; AF422179; AAL37737.1; -; Genomic_DNA.
DR EMBL; AC009999; AAF29391.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27904.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59031.1; -; Genomic_DNA.
DR EMBL; AF332458; AAG48821.1; -; mRNA.
DR EMBL; AY034935; AAK59442.1; -; mRNA.
DR EMBL; AY113925; AAM44973.1; -; mRNA.
DR EMBL; AB493435; BAH30273.1; -; mRNA.
DR EMBL; Z25683; CAA81011.1; -; mRNA.
DR PIR; C86193; C86193.
DR RefSeq; NP_001321426.1; NM_001331589.1.
DR RefSeq; NP_172076.1; NM_100466.5.
DR AlphaFoldDB; Q9MA41; -.
DR SMR; Q9MA41; -.
DR STRING; 3702.AT1G05850.1; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q9MA41; -.
DR PRIDE; Q9MA41; -.
DR ProteomicsDB; 220318; -.
DR EnsemblPlants; AT1G05850.1; AT1G05850.1; AT1G05850.
DR EnsemblPlants; AT1G05850.2; AT1G05850.2; AT1G05850.
DR GeneID; 837095; -.
DR Gramene; AT1G05850.1; AT1G05850.1; AT1G05850.
DR Gramene; AT1G05850.2; AT1G05850.2; AT1G05850.
DR KEGG; ath:AT1G05850; -.
DR Araport; AT1G05850; -.
DR TAIR; locus:2198688; AT1G05850.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_2_0_1; -.
DR InParanoid; Q9MA41; -.
DR OMA; TMENRVP; -.
DR OrthoDB; 803707at2759; -.
DR PhylomeDB; Q9MA41; -.
DR PRO; PR:Q9MA41; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA41; baseline and differential.
DR Genevisible; Q9MA41; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0030247; F:polysaccharide binding; IDA:TAIR.
DR GO; GO:0001708; P:cell fate specification; IMP:TAIR.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0010167; P:response to nitrate; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Ethylene signaling pathway;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..321
FT /note="Chitinase-like protein 1"
FT /id="PRO_0000394283"
FT REGION 297..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..55
FT /evidence="ECO:0000250"
FT DISULFID 157..167
FT /evidence="ECO:0000250"
FT DISULFID 267..304
FT /evidence="ECO:0000250"
FT MUTAGEN 168
FT /note="S->I: In arm; abnormal root architecture in
FT responses to high nitrate."
FT /evidence="ECO:0000269|PubMed:20007445"
FT MUTAGEN 188
FT /note="G->R: In hot2-1; reduced tolerance to abiotic
FT stresses such as salt, drought and heat."
FT /evidence="ECO:0000269|PubMed:17156413"
FT CONFLICT 149
FT /note="E -> A (in Ref. 6; CAA81011)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="M -> L (in Ref. 6; CAA81011)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="N -> K (in Ref. 5; BAH30273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35579 MW; 35B2822474CEA31F CRC64;
MVTIRSGSIV ILVLLAVSFL ALVANGEDKT IKVKKVRGNK VCTQGWECSW WSKYCCNQTI
SDYFQVYQFE QLFSKRNTPI AHAVGFWDYQ SFITAAALFE PLGFGTTGGK LMGQKEMAAF
LGHVASKTSC GYGVATGGPL AWGLCYNREM SPMQSYCDES WKFKYPCSPG AEYYGRGALP
IYWNFNYGAA GEALKADLLN HPEYIEQNAT LAFQAAIWRW MTPIKRAQPS AHDIFVGNWK
PTKNDTLSKR GPTFGSTMNV LYGEYTCGQG SIDPMNNIIS HYLYFLDLMG IGREDAGPND
ELSCAEQKPF NPSTVPSSSS S
