ID   CHI_PINMA               Reviewed;         466 AA.
AC   P86955;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Putative chitinase;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase-like protein 3;
DE            Short=Clp3;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 115-129; 179-192; 205-211; 257-266 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:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GT281452; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; GT278709; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT280136; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281452; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281952; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT282837; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420284; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86955; -.
DR   SMR; P86955; -.
DR   PRIDE; P86955; -.
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"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413069"
FT   DOMAIN          20..380
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   COILED          408..442
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"
FT   CONFLICT        135
FT                   /note="G -> C (in Ref. 1; GT282837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="S -> N (in Ref. 1; GT278709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263..264
FT                   /note="FF -> LL (in Ref. 1; GT282837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279..281
FT                   /note="GSP -> RIA (in Ref. 1; GT282837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="A -> S (in Ref. 1; GT281452)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   466 AA;  53984 MW;  C1563E0E9C18068B CRC64;
     MYLTIWLVSI LALGTWGQKF NRFCHYNSWA LSRNPQHGLV PEDIDPFLCT HLILGFAEID
     ESGLRLKDPN HYQQEYLYQR IVRLRRINPR LNMILSVGGW DKSQEGYSKL VSSRENILFF
     TKWIITYLRR HDFDGLDLDW EYPTFKGSPM GDKKKFVDLV ENLAYEFDIE EIPDIKWKLT
     LTWTADPLES VRTSAYDIKG IASKVHNVNL KMYDFHGHWD DPLQVNHHSP LTSPNSPRNV
     NELAKSWVKA GVRIEKLILG IPFFGRSFTL KTANMSVPGS PAVGPGSDFG DGIPIHNLCH
     IIRGGTKELY LPEKKVPYIV SGSEWIGYDN PRSVMEKAQL VFNNALAGVM IYSLDMDDHH
     GTCGRKWPMM MAVIHGLNAY MEYIDSKHKS LELTFNKKIL RARVSLRNYR RRNQQEKVAE
     MEQRIRHLEQ ELQQSMGNMA YERQQAQAML NRGVSLPPIE QQSWSW