CHITL_CAEEL
ID CHITL_CAEEL Reviewed; 1067 AA.
AC Q18143;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chitinase-like protein C25A8.4;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=cht-3; ORFNames=C25A8.4;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, 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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47 AND ASN-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47; ASN-216; ASN-475; ASN-710;
RP ASN-933 AND ASN-1010, AND IDENTIFICATION BY MASS 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 -!- FUNCTION: Putative chitinase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 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; FO080398; CCD63429.1; -; Genomic_DNA.
DR PIR; T29806; T29806.
DR RefSeq; NP_501082.2; NM_068681.4.
DR AlphaFoldDB; Q18143; -.
DR SMR; Q18143; -.
DR BioGRID; 42584; 7.
DR STRING; 6239.C25A8.4; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q18143; -.
DR EPD; Q18143; -.
DR PaxDb; Q18143; -.
DR PeptideAtlas; Q18143; -.
DR PRIDE; Q18143; -.
DR EnsemblMetazoa; C25A8.4.1; C25A8.4.1; WBGene00016084.
DR GeneID; 177464; -.
DR KEGG; cel:CELE_C25A8.4; -.
DR UCSC; C25A8.4; c. elegans.
DR CTD; 177464; -.
DR WormBase; C25A8.4; CE32592; WBGene00016084; cht-3.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_288240_0_0_1; -.
DR InParanoid; Q18143; -.
DR OMA; DDYTGIC; -.
DR OrthoDB; 133520at2759; -.
DR PhylomeDB; Q18143; -.
DR PRO; PR:Q18143; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016084; Expressed in germ line (C elegans) and 2 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; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 3.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 3.
DR PROSITE; PS51910; GH18_2; 3.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1067
FT /note="Chitinase-like protein C25A8.4"
FT /id="PRO_0000248518"
FT DOMAIN 26..364
FT /note="GH18 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 372..727
FT /note="GH18 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 743..1067
FT /note="GH18 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 855
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 376..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 747..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 1067 AA; 120199 MW; D1FAE001839BC02C CRC64;
MGIKTLIWLS ILVVGIYCEI SDEDAPVHYC FVNPPPKTRL SPNLLQNITT CTHLVYGSIP
IDRDTGYPQY SVSDVESGYD IDNIRTFMRL RKYHPNAKLL MGVVRTKPFE DAATSVKVAN
GLRSHVKSKR FDGLFVTFNG IHLEYRASTS FLETISKDKK MSLTFGVTGR RVFAFDALRR
LQEINDLVEY IYLDMGELPS NEELARVTHI NPLFYNGSIP FEETIQGTVE ELSKEGILPS
RIVVGLTAGG WKFEIKETQD PLKISHGQYA ENNGKRVSYQ DACRARGAVI YDWQTMNEIT
VYRQTWMSVN LPTIKAMGEK MKWILGQKFA GIGISHALFD DPRGDCGTDP LPAHRLVMEL
IRNTIPANPA KCTRLCYLDP EEVEETFPID NLKSDYCSHI VVPYFALDLS DKMIEEDKAE
DLVKKIDDWR SKIVEVAPRL ILSVGSKQAS TIWQFLLGND FHRKELAEGL VKAINSTNAD
GLEISWTSQP MVSDFDKKNL KSFINDIVAA DTAKMVEIVV ATSQQSAYSD FYDYEHLNKT
ASLIVLHSHR LHSDSLPFTG HPSPLRATSS MTNQKMSWES LLSHWVEKRV LPSKLVLSLS
ASTLSMQSLA DVRSSAATPF GQSAFVSMLR SKKGDIHSQQ EICESLKSGT GVTHWVDGAE
VPYLRRYDQM VAYENTRSAH IKAVWASMEG VGGLALHNMH QDDPSAVCDN RTAFPILNAL
SRAQVCQTCL KQHDFKKCEQ HDFVVSCNFE LKRSTPVFKT DIVPYERCTE VVVEQATLTL
GGNVNFNDVQ QEQVVKNLTS LRSKMVKCGM VLSLSCGDSE KYLNSILGDN MTFAIGNVMN
IMEKYKFSGV QLDCEKVIRR GNHIYFNTFV KKLAQKFESG KASNGCNRTL SARFSHYTQK
PSTYYSVSLL NRLSHIALRM TDKHSVDLPF FFNHTKPEFP STEKFVNIWK NVGLKPDKLV
LELSPFGWQT GKKVGEKKKM TQGVNCVTAG NRAVYEHDYE TLTGMTKHEN GTINMPMIED
FRYKIGYIQR EQLGGIALNV NGDDYTGICG RGSFPILKSV YSSHKCR
