CHIT_CAEEL
ID CHIT_CAEEL Reviewed; 617 AA.
AC Q11174; O17321;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Probable endochitinase;
DE EC=3.2.1.14;
GN Name=cht-1; ORFNames=C04F6.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-178.
RX PubMed=9662472; DOI=10.1111/j.1365-2583.1998.00065.x;
RA de la Vega H., Specht C.A., Liu Y., Robbins P.W.;
RT "Chitinases are a multi-gene family in Aedes, Anopheles and Drosophila.";
RL Insect Mol. Biol. 7:233-239(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-310, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-310, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; FO080344; CCD63028.1; -; Genomic_DNA.
DR EMBL; AF026152; AAB81847.1; -; Genomic_DNA.
DR PIR; T15408; T15408.
DR PIR; T37249; T37249.
DR RefSeq; NP_508588.1; NM_076187.4.
DR PDB; 6LDU; X-ray; 1.70 A; A=52-433.
DR PDB; 6LE7; X-ray; 1.86 A; A=53-433.
DR PDB; 6LE8; X-ray; 1.40 A; A=52-431.
DR PDBsum; 6LDU; -.
DR PDBsum; 6LE7; -.
DR PDBsum; 6LE8; -.
DR AlphaFoldDB; Q11174; -.
DR SMR; Q11174; -.
DR BioGRID; 45569; 3.
DR STRING; 6239.C04F6.3; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q11174; -.
DR EPD; Q11174; -.
DR PaxDb; Q11174; -.
DR PeptideAtlas; Q11174; -.
DR EnsemblMetazoa; C04F6.3.1; C04F6.3.1; WBGene00000503.
DR GeneID; 180628; -.
DR KEGG; cel:CELE_C04F6.3; -.
DR UCSC; C04F6.3.1; c. elegans.
DR CTD; 180628; -.
DR WormBase; C04F6.3; CE03923; WBGene00000503; cht-1.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000168919; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q11174; -.
DR OMA; NPMTYDF; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; Q11174; -.
DR PRO; PR:Q11174; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000503; Expressed in embryo and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IDA:WormBase.
DR GO; GO:0006032; P:chitin catabolic process; IDA:WormBase.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009620; P:response to fungus; IEP:WormBase.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00494; ChtBD2; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57625; SSF57625; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat.
FT CHAIN 1..617
FT /note="Probable endochitinase"
FT /id="PRO_0000077049"
FT DOMAIN 53..426
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 478..534
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 563..617
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 109..110
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 136..139
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 180
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 245..248
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 394
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 57..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 511..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 594..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CONFLICT 138
FT /note="W -> C (in Ref. 2; AAB81847)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..165
FT /note="ITF -> TTS (in Ref. 2; AAB81847)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="I -> L (in Ref. 2; AAB81847)"
FT /evidence="ECO:0000305"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6LE8"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6LE8"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 184..208
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 295..310
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6LE8"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6LE8"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:6LE8"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:6LE8"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6LDU"
SQ SEQUENCE 617 AA; 66857 MW; DDA1D2AAAC0E54DA CRC64;
MLLGKFLLVA SFILPIAYTW TGATIRNHPA DVVAARNKIT SRSVARSEPT NSYIRPCYFT
NWAQYRQGRA KFVPEDYTPG LCTHILFAFG WMNADYTVRA YDPADLPNDW AGEGMYRRVN
KLKVTDTQLK TLLSFGGWSF GTALFQGMAA SSASRKVFID SAITFVRTWG FDGIDIDWEY
PSGATDMANY VALVKELKAA CESEAGSTGK DRLLVTAAVA AGPATIDAGY DIPNLAPNFD
FILLMSYDFF GAWASLVGFN SPLYATTELP AEWNGWNVDS SARYWNQKGM PKEKIIVGMP
TYGRGWTLNN ASAINPGTSG SPAKITQYVQ EAGVGAYFEF CEMLANGATR YWDSQSQVPY
LVQGNQWWSY DDEESFANKM AYVKREGYGG AFVWTLDFDD FNAGCSNSNG QLYPLISVIA
KELGGVIIPK KGGVTTAPTT VATTVTTGRP PMTSAVTTTT AATTTTTRAA TTTTASNTNV
CSGKSDGFYP NSNNCGLFVL CLSSKSYSMS CPSGLQYSAS LKYCTTSTAS GCSVTTTRAP
TTTTKSAPTV TTTTRAPTTT TPAFKCTKDG FFGVPSDCLK FIRCVNGISY NFECPNGLSF
HADTMMCDRP DPSKCAK
