CTL2_ARATH
ID CTL2_ARATH Reviewed; 333 AA.
AC Q9LSP9; F4J3Y0;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Chitinase-like protein 2;
DE Short=AtCTL2;
DE Flags: Precursor;
GN Name=CTL2; OrderedLocusNames=At3g16920; ORFNames=K14A17.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 (By similarity). Required for proper
CC cell wall biosynthesis in etiolated seedlings. Prevents lignin
CC accumulation in hypocotyls. {ECO:0000250, ECO:0000269|PubMed:20056293}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, especially in xylem and
CC interfascicular fibers. {ECO:0000269|PubMed:20056293}.
CC -!- DISRUPTION PHENOTYPE: Ectopic accumulation of lignin in etiolated
CC hypocotyls. {ECO:0000269|PubMed:20056293}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026636; BAA94976.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75884.2; -; Genomic_DNA.
DR EMBL; AF412071; AAL06524.1; -; mRNA.
DR EMBL; AY090261; AAL90922.1; -; mRNA.
DR EMBL; AK226317; BAE98469.1; -; mRNA.
DR RefSeq; NP_001319573.1; NM_001338267.1.
DR AlphaFoldDB; Q9LSP9; -.
DR SMR; Q9LSP9; -.
DR STRING; 3702.AT3G16920.1; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q9LSP9; -.
DR ProteomicsDB; 222633; -.
DR EnsemblPlants; AT3G16920.1; AT3G16920.1; AT3G16920.
DR GeneID; 820947; -.
DR Gramene; AT3G16920.1; AT3G16920.1; AT3G16920.
DR KEGG; ath:AT3G16920; -.
DR Araport; AT3G16920; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_2_0_1; -.
DR OMA; MTPPEKH; -.
DR PhylomeDB; Q9LSP9; -.
DR PRO; PR:Q9LSP9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSP9; baseline and differential.
DR Genevisible; Q9LSP9; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..333
FT /note="Chitinase-like protein 2"
FT /id="PRO_0000394284"
FT REGION 307..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..56
FT /evidence="ECO:0000250"
FT DISULFID 165..175
FT /evidence="ECO:0000250"
FT DISULFID 275..313
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 36699 MW; 1AA719D98ED97824 CRC64;
MVSKPLFSLL LLTVALVVFQ TGTLVNAEDS EPSSSTRKPL VKIVKGKKLC DKGWECKGWS
EYCCNHTISD FFETYQFENL FSKRNSPVAH AVGFWDYRSF ITAAAEYQPL GFGTAGEKLQ
GMKEVAAFLG HVGSKTSCGY GVATGGPLAW GLCYNKEMSP DQLYCDDYYK LTYPCTPGVS
YHGRGALPVY WNYNYGQTGE ALKVDLLSHP EYLENNATLA FQAAIWRWMT PPKKHLPSAH
DVFVGKWKPT KNDTAAKRTP GFGATINVLY GDQICNSGFD NDEMNNIVSH YLYYLDLIGV
GREEAGPHEK LSCADQEPFS SSSSAPPSSG SSS
