ID   CHI1_PINMG              Reviewed;         468 AA.
AC   H2A0L4;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative chitinase 1 {ECO:0000250|UniProtKB:P86955};
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase-like protein 1;
DE            Short=Clp1;
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 68-82; 117-148; 158-166; 206-213 AND 259-268,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
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:0000255};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the outer
CC       epithelium of the mantle edge and lower level in the mantle pallium.
CC       {ECO:0000269|PubMed:23213212}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000255}.
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; HE610381; CCE46155.1; -; mRNA.
DR   AlphaFoldDB; H2A0L4; -.
DR   SMR; H2A0L4; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PRIDE; H2A0L4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Disulfide bond; Glycosidase;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..468
FT                   /note="Putative chitinase 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417975"
FT   DOMAIN          22..381
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   COILED          386..440
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         73..74
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         100..103
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         144
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         213..216
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         353
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        26..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   468 AA;  53559 MW;  8C335D39F157F3A0 CRC64;
     MDFYSSLLPF LILIYLEFCS GFNRVCYYNG WALYRDSEHA LKPENIDAFL CTHLVFAFGA
     IDETGTRIYV PEVFEDMHLF ERMNELRHRN EDLNLVLSVG GWDMGSEAWS EVLASKDNMQ
     TFVKEAIVYL RLHDFDGIDL DWEYPTFRGS KPIDREKFTQ LIEIFRHEMD IEETPDDKWD
     LCLSVAVDPS EYMSSSSYEI DKITKNIDFY NLKMYDFHGH WNDPVLVKHH SALTSSSSLP
     SVNELAKMWV QRGVPKRKIN IGIPFFGRSY RTAQPNATIG DPALGPGSDG GIGIPVSNIC
     HLIRGGTKEH YLKEENVPFI VNGDEWVGFD NPRSVREKAA LVRNNRLGGI MVWAIDMDDH
     SGWCGEKFPL MMSIIHGLGE YVDYMSDTLE AEREMINKKI RKAAREISYY SDKGNSTMAK
     KMEDKLNQLK DHLSAVQAHQ SVQWANVQYS AGLGGKPLPS KDTPSWSW