HEX_PINMA
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 03-AUG-2022, entry version 37.
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};
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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 PRIDE; 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; -; 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; PTHR22600; 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; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 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; GT281082/GT282050/GT281480/
FT 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
