CLP_ORYSJ
ID CLP_ORYSJ Reviewed; 424 AA.
AC Q8S1V1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chitinase CLP {ECO:0000303|PubMed:23331415};
DE Short=OsCLP {ECO:0000303|PubMed:23331415};
DE EC=3.2.1.14 {ECO:0000269|PubMed:23331415};
DE AltName: Full=Chitinase-like protein {ECO:0000303|PubMed:23331415};
DE Flags: Precursor;
GN Name=CLP {ECO:0000303|PubMed:23331415};
GN OrderedLocusNames=Os01g0937050 {ECO:0000312|EMBL:BAH91462.1},
GN LOC_Os01g71080 {ECO:0000305};
GN ORFNames=P0504E02.9 {ECO:0000312|EMBL:BAB89707.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=23331415; DOI=10.1186/1472-6750-13-4;
RA Wu J., Wang Y., Kim S.T., Kim S.G., Kang K.Y.;
RT "Characterization of a newly identified rice chitinase-like protein (OsCLP)
RT homologous to xylanase inhibitor.";
RL BMC Biotechnol. 13:4-4(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28401568; DOI=10.1111/ppl.12579;
RA Wu J., Wang Y., Kim S.G., Jung K.H., Gupta R., Kim J., Park Y., Kang K.Y.,
RA Kim S.T.;
RT "A secreted chitinase-like protein (OsCLP) supports root growth through
RT calcium signaling in Oryza sativa.";
RL Physiol. Plantarum 161:273-284(2017).
CC -!- FUNCTION: Chitinase that possesses antifungal activity
CC (PubMed:23331415). Inhibits the growth of the fungal pathogen
CC Rhizoctonia solani by degrading the fungal cell wall (PubMed:23331415).
CC Does not possess inhibiting activity against fungal endo-1,4-beta-D-
CC xylanases belonging to glycoside hydrolase family 10 (GH10) and family
CC 11 (GH11) (PubMed:23331415). Involved in the regulation of plant growth
CC by regulating the intracellular calcium ion concentration in roots
CC (PubMed:28401568). {ECO:0000269|PubMed:23331415,
CC ECO:0000269|PubMed:28401568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000269|PubMed:23331415};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:28401568}.
CC -!- TISSUE SPECIFICITY: Expressed in roots (PubMed:28401568). Expressed at
CC low levels in leaf sheaths, stems and flowers (PubMed:28401568).
CC {ECO:0000269|PubMed:28401568}.
CC -!- INDUCTION: Induced by infection with an incompatible race of the fungal
CC pathogen Magnaporthe oryzae. {ECO:0000269|PubMed:23331415}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth of roots and shoots.
CC {ECO:0000269|PubMed:28401568}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103, ECO:0000305}.
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DR EMBL; AP003269; BAB89707.1; -; Genomic_DNA.
DR EMBL; AP008207; BAH91462.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS76113.1; -; Genomic_DNA.
DR RefSeq; XP_015632157.1; XM_015776671.1.
DR AlphaFoldDB; Q8S1V1; -.
DR SMR; Q8S1V1; -.
DR STRING; 4530.OS01T0937050-00; -.
DR MEROPS; A01.974; -.
DR PaxDb; Q8S1V1; -.
DR PRIDE; Q8S1V1; -.
DR EnsemblPlants; Os01t0937050-01; Os01t0937050-01; Os01g0937050.
DR GeneID; 9267890; -.
DR Gramene; Os01t0937050-01; Os01t0937050-01; Os01g0937050.
DR KEGG; osa:9267890; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_032185_1_0_1; -.
DR InParanoid; Q8S1V1; -.
DR OMA; YAVPQVD; -.
DR OrthoDB; 1055542at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0048367; P:shoot system development; IMP:UniProtKB.
DR CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Apoplast; Carbohydrate metabolism; Chitin degradation; Glycoprotein;
KW Glycosidase; Growth regulation; Hydrolase; Plant defense;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..424
FT /note="Chitinase CLP"
FT /id="PRO_5013535939"
FT DOMAIN 43..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 424 AA; 44620 MW; 0DACD5CAC8852C34 CRC64;
MSLHLLLAVS LCVALASSLP WAAASANGNG NGKPLVAAIT KDAATSLYTV PIKDGRPLVL
DLAGALVWMS CAAAHPTLEC HHHFCMHAHS YHPPGCPHNG YGRADVEDPF RCKCTAHPYN
PFSGESATAD LTRTRLSANA TDGKNPLYPV SFAAVTSCAP DSLLAKLPAG AVGVAGLART
RLALQAQVAR SQKVANKFAL CLPSGGGGDG VAIFGGGPLF LLPPGRPDVA ATLAGETPLH
RNKDLPGYFI SATKIAVNQE QVQLYTQEPL VVELCTRIPY TALRPDVYRA VVDAFARATA
GRKRVTPPPP PAAPFELCYD SRDLGSTRLG YAVPQIDLVL EGGKNWTVFG GNSMAQVSDN
TACLAVVKVK GEKGSPPPPA AIIGGFQMEN NLVVFDEEKQ RLGFSGLLWG RQTTCSNFNF
TLAA
