ID   CHI2_PINMG              Reviewed;         466 AA.
AC   H2A0L5;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Putative chitinase 2 {ECO:0000250|UniProtKB:P86955};
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase-like protein 3 {ECO:0000250|UniProtKB:P86955};
DE            Short=Clp3;
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 179-192; 205-211; 257-266; 390-397 AND 444-452,
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 mantle edge
CC       and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000255}.
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DR   EMBL; HE610382; CCE46156.1; -; mRNA.
DR   AlphaFoldDB; H2A0L5; -.
DR   SMR; H2A0L5; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PRIDE; H2A0L5; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..466
FT                   /note="Putative chitinase 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417976"
FT   DOMAIN          20..380
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   COILED          395..447
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        24..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   466 AA;  53985 MW;  F8AE0ABB4571A13E CRC64;
     MYLTIWLVPL LAVGTWGQKF NRFCHYNSWA LSRNPQHGLV PEDIDPFLCT HMILGFAEID
     ESGLRLKDPN HYQQQYLYQR IVRLRRINPR LNMILSVGGW DKSQEGYSKL VSSRENIIFF
     TKWIITYLRR HDFDGLDLDW EYPTFKGSPM VDKKKFVDLV ENLAYEFDIE EIPDIKWKLT
     LTWTADPLES VRTSAYDIKG IASKVHYVNL KMYDFHGHWD DPLRVNHHSP LTSSNSPRNV
     NELAKTWVKA GVRIEKLILG IPFFGRSFTL KTANMSAPGS PAVGPGSDFG DGIPIHNLCH
     IIRGGTKELY LPEKKVPYIV SGSEWIGYDN PRSVMEKAQL VFNNALAGVM IYSLDMDDHH
     GTCGKKWPMM MAVIHGLNAY MEYIDSKHKS LELTYNKKIL RARVSLRNYR RRNQQGKVAE
     MEQRIRNLEQ ELQQSMGNMA YERQQAQAML NRGVSLPPIE QQSWSW