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Database: UniProt
Entry: W5KRD1_ASTMX
LinkDB: W5KRD1_ASTMX
Original site: W5KRD1_ASTMX 
ID   W5KRD1_ASTMX            Unreviewed;       471 AA.
AC   W5KRD1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000010143.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000010143.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000822};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   AlphaFoldDB; W5KRD1; -.
DR   STRING; 7994.ENSAMXP00000010143; -.
DR   Ensembl; ENSAMXT00000010143.2; ENSAMXP00000010143.2; ENSAMXG00000009870.2.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00940000162989; -.
DR   HOGENOM; CLU_002833_3_1_1; -.
DR   InParanoid; W5KRD1; -.
DR   OrthoDB; 1752999at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000009870; Expressed in testis and 3 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR   CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF379; CHITINASE-RELATED; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..471
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017372625"
FT   DOMAIN          22..389
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          421..471
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          395..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  52417 MW;  156C7F8BF6F30007 CRC64;
     MGRLTLLAGL CLVLCHFATS SKQMGCYFTN WSQYRPGIGK YMPANVDPFL CTHLFYAFAM
     INHANELITY EWNDETLYQS FNALKNSNPA LKTLLAVGGW NFGSTQFSIT VSNAANRQKF
     IQSSISFLRT HGFDGMDLDW EYPGSRGSPP EDKQRFTLLC KELLEAYEAE ANATGQPRLL
     LSAAVSAGKG TIDAGYEIAE IAKYLDFINV MTYDFHGTWE RFTGHNSPLY QGSKDEGDLI
     YFNTDYAMRY WRDNGTPVEK LRMGFATYGR TFRLTSAEDG VGAPASGPAS AGTYTREAGF
     WSYYEICGFL EGTKIQWIDD QRVPYATKNS EWVGFDTKES FETKVQYLKD NKFGGAFVWA
     LDLDDFAGQF CGQGNHPLMG HLHNLLDIVV PPRPSTTTPK PGASTIPVTT TPTTTTHKPG
     PGFCNGKPDG LYPHEDPNQF YDCVAGETIV RKCGPGTVFN DDCKCCAWAK H
//
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