ID HEX_PINMA Reviewed; 1130 AA. AC P86956; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 41. DE RecName: Full=Putative beta-hexosaminidase; DE EC=3.2.1.52 {ECO:0000250|UniProtKB:Q04786}; DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000250|UniProtKB:Q04786}; DE AltName: Full=Chitobiase {ECO:0000250|UniProtKB:Q04786}; DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000250|UniProtKB:Q04786}; 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 658-664; 761-767 AND 1005-1016, SUBCELLULAR LOCATION, RP 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=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; CC Evidence={ECO:0000250|UniProtKB:Q04786}; CC -!- PATHWAY: Glycan degradation; chitin degradation. CC {ECO:0000250|UniProtKB:Q04786}. 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 20 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=GT279548; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT280934; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT282050; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT282702; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT282776; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT283781; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=GT284443; Type=Miscellaneous discrepancy; Note=Premature stop codon at position 218.; Evidence={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; GT277795; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278040; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278051; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278127; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278167; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278276; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278283; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278457; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT278599; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279087; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279290; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279353; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279393; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279548; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279589; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279825; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279940; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT279953; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT280934; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT280997; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281082; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281097; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281480; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281527; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281701; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281791; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT281846; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282021; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282046; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282050; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282275; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282639; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282702; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282719; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT282776; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT283348; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT283584; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT283781; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT284045; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GT284443; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; EZ420123; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; EZ420192; -; NOT_ANNOTATED_CDS; mRNA. DR AlphaFoldDB; P86956; -. DR SMR; P86956; -. DR UniPathway; UPA00349; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.40.290; -; 1. DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. DR InterPro; IPR004866; CHB/HEX_N_dom. DR InterPro; IPR015883; Glyco_hydro_20_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR029018; Hex-like_dom2. DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1. DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1. DR Pfam; PF03173; CHB_HEX; 1. DR Pfam; PF00728; Glyco_hydro_20; 1. DR PRINTS; PR00738; GLHYDRLASE20. DR SMART; SM01081; CHB_HEX; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Hydrolase; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..1130 FT /note="Putative beta-hexosaminidase" FT /evidence="ECO:0000255" FT /id="PRO_0000413087" FT REGION 1001..1075 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1102..1130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1013..1031 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1043..1070 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 391 FT /note="E -> Q (in Ref. 1; GT281097)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="D -> S (in Ref. 1; GT279548)" FT /evidence="ECO:0000305" FT CONFLICT 538 FT /note="M -> L (in Ref. 1; GT282050)" FT /evidence="ECO:0000305" FT CONFLICT 614 FT /note="N -> H (in Ref. 1; GT280934)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="V -> M (in Ref. 1; FT GT281082/GT282050/GT281480/GT279953)" FT /evidence="ECO:0000305" FT CONFLICT 653 FT /note="K -> E (in Ref. 1; GT284045)" FT /evidence="ECO:0000305" FT CONFLICT 658 FT /note="F -> V (in Ref. 1; GT279353)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="D -> E (in Ref. 1; GT279548)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="V -> R (in Ref. 1; GT279548)" FT /evidence="ECO:0000305" FT CONFLICT 743 FT /note="D -> N (in Ref. 1; GT278127)" FT /evidence="ECO:0000305" FT CONFLICT 752 FT /note="D -> E (in Ref. 1; GT282050)" FT /evidence="ECO:0000305" FT CONFLICT 806 FT /note="Q -> P (in Ref. 1; GT282702/GT281480)" FT /evidence="ECO:0000305" FT CONFLICT 807 FT /note="E -> G (in Ref. 1; GT282702)" FT /evidence="ECO:0000305" FT CONFLICT 863..865 FT /note="VNG -> PSW (in Ref. 1; GT284045)" FT /evidence="ECO:0000305" FT CONFLICT 866..876 FT /note="NPWTDNVKVLD -> SP (in Ref. 1; GT283781)" FT /evidence="ECO:0000305" FT CONFLICT 870..871 FT /note="DN -> GH (in Ref. 1; GT284045)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="D -> N (in Ref. 1; GT279087)" FT /evidence="ECO:0000305" FT CONFLICT 964 FT /note="A -> T (in Ref. 1; GT279087)" FT /evidence="ECO:0000305" FT CONFLICT 1104 FT /note="R -> K (in Ref. 1; GT283348)" FT /evidence="ECO:0000305" SQ SEQUENCE 1130 AA; 126718 MW; 9F180107C5016EA5 CRC64; MKWVKSGVGI LGILLIICHA VTSQRRILDI TDNLKITFKT ISNFGPRAQS IQNVTIENVG IKDIPDFGWR CYFCHDQLLF PGTFNLARSQ YFLRPILDNY VVLSDGFLLE FIKGCMYRIT PIPRNAPIKT RDKREFTLLA EQFSVSKYDS FPNWYCETIS GGNTEVANIR STENLKYVED FDSSYNWFRI PHDFRSVPLQ PQDRYSANHK ASSVEECKYK VIPTPVKASV RKVQRNFGTT VYYGTTDTSI RGKLFKVAEK LALKHKLGLV EMTPGQPVNN GISLVVTGNY IERNIPSPDE AYRLSVSADL ISIEAPALPG LINGIETMHS LSAWDMALPY GGVKDFPRFP FRGIFLDIAS NFPGYNYMMK FLTVMAQYKL NKLVLPLYNN EGFRLELNDS PGYEFQALHL VGGNRCHDLK EENCLFSQLG SFAGNSDGYL TKGDMVDLIK TADLLNIEII MSLNIGESAR GAIVPLKTSK HNRLLYDPED TDFVDRFYPQ KDSSMNPCRE ETMIFYDHML KQLKAIYKAA SVPLKTIMIG SKVNFDQVLN SKYCYPKNLN STQRLMEREN LERNINGFKL NFTKRLVKTA HDNGINEVMA IDDVFTTEFD AAGNTPNTVY DTVDSETNKT RFNATVTAVH SRYDTVRDER LWKRGDRFAE LGYKVIISPP ILDFNYAVEP DPDRPGDYDS VIRNISFSKL FRFVPDSHCC NIPNAIQHDC ALESDCTTAG PPDSYIGTLG KLDTRKLRSL KDWNELLFPR LLIFAERSWH KSSWEDSFEP HRVRMNNITR QIITNYTVPN WNDIIQEESK VLGCISRKEK LRLMHEDGLK PYVEPPGARL LGGNTMRIAA STTEDSFWVQ ASVNGNPWTD NVKVLDVNPT DSVRLRTVHP AKAELRSKEV KLNLTSLPTP REQFRKIAQD ALSRRIGIDI QRARMPPMPV NPTYRPPVPL PSFDPADDRA PDLAAIAAAH PPPLPPGMPP HMMPNMPFPP RPPFVPPLLP PGQMRALGQQ AGQALRGQGQ QTGQQTLPAQ PRGPMGLTGQ AAGTGVAGQS GQQPSAAGQG TQQGLPGQQR TGVVPGQWPF FPGMPAAQFP PMFNPQMQRA LQMRGQGQIP QTQGAVAGAG QSRVPQQQAG //