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P86956

- HEX_PINMA

UniProt

P86956 - HEX_PINMA

Protein

Putative beta-hexosaminidase

Gene
N/A
Organism
Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 15 (01 Oct 2014)
      Sequence version 1 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.By similarity

    Pathwayi

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC
    2. polysaccharide binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    UniPathwayiUPA00349.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative beta-hexosaminidase (EC:3.2.1.52By similarity)
    Alternative name(s):
    Beta-N-acetylhexosaminidaseBy similarity
    ChitobiaseBy similarity
    N-acetyl-beta-glucosaminidaseBy similarity
    OrganismiPinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster)
    Taxonomic identifieri104660 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 11301107Putative beta-hexosaminidaseSequence AnalysisPRO_0000413087Add
    BLAST

    Expressioni

    Tissue specificityi

    Prismatic layer of shell (at protein level). Expressed primarily in the mantle with highest level in the mantle edge and lower level in the mantle pallium.1 Publication

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi936 – 100166Pro-richSequence AnalysisAdd
    BLAST
    Compositional biasi1003 – 1128126Gln-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR004866. CHB/HEX_N_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF03173. CHB_HEX. 1 hit.
    PF00728. Glyco_hydro_20. 1 hit.
    [Graphical view]
    PRINTSiPR00738. GLHYDRLASE20.
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF55545. SSF55545. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P86956-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKWVKSGVGI LGILLIICHA VTSQRRILDI TDNLKITFKT ISNFGPRAQS     50
    IQNVTIENVG IKDIPDFGWR CYFCHDQLLF PGTFNLARSQ YFLRPILDNY 100
    VVLSDGFLLE FIKGCMYRIT PIPRNAPIKT RDKREFTLLA EQFSVSKYDS 150
    FPNWYCETIS GGNTEVANIR STENLKYVED FDSSYNWFRI PHDFRSVPLQ 200
    PQDRYSANHK ASSVEECKYK VIPTPVKASV RKVQRNFGTT VYYGTTDTSI 250
    RGKLFKVAEK LALKHKLGLV EMTPGQPVNN GISLVVTGNY IERNIPSPDE 300
    AYRLSVSADL ISIEAPALPG LINGIETMHS LSAWDMALPY GGVKDFPRFP 350
    FRGIFLDIAS NFPGYNYMMK FLTVMAQYKL NKLVLPLYNN EGFRLELNDS 400
    PGYEFQALHL VGGNRCHDLK EENCLFSQLG SFAGNSDGYL TKGDMVDLIK 450
    TADLLNIEII MSLNIGESAR GAIVPLKTSK HNRLLYDPED TDFVDRFYPQ 500
    KDSSMNPCRE ETMIFYDHML KQLKAIYKAA SVPLKTIMIG SKVNFDQVLN 550
    SKYCYPKNLN STQRLMEREN LERNINGFKL NFTKRLVKTA HDNGINEVMA 600
    IDDVFTTEFD AAGNTPNTVY DTVDSETNKT RFNATVTAVH SRYDTVRDER 650
    LWKRGDRFAE LGYKVIISPP ILDFNYAVEP DPDRPGDYDS VIRNISFSKL 700
    FRFVPDSHCC NIPNAIQHDC ALESDCTTAG PPDSYIGTLG KLDTRKLRSL 750
    KDWNELLFPR LLIFAERSWH KSSWEDSFEP HRVRMNNITR QIITNYTVPN 800
    WNDIIQEESK VLGCISRKEK LRLMHEDGLK PYVEPPGARL LGGNTMRIAA 850
    STTEDSFWVQ ASVNGNPWTD NVKVLDVNPT DSVRLRTVHP AKAELRSKEV 900
    KLNLTSLPTP REQFRKIAQD ALSRRIGIDI QRARMPPMPV NPTYRPPVPL 950
    PSFDPADDRA PDLAAIAAAH PPPLPPGMPP HMMPNMPFPP RPPFVPPLLP 1000
    PGQMRALGQQ AGQALRGQGQ QTGQQTLPAQ PRGPMGLTGQ AAGTGVAGQS 1050
    GQQPSAAGQG TQQGLPGQQR TGVVPGQWPF FPGMPAAQFP PMFNPQMQRA 1100
    LQMRGQGQIP QTQGAVAGAG QSRVPQQQAG 1130
    Length:1,130
    Mass (Da):126,718
    Last modified:October 19, 2011 - v1
    Checksum:i9F180107C5016EA5
    GO

    Sequence cautioni

    The sequence GT284443 differs from that shown. Reason: Premature stop codon at position 218.
    The sequence GT279548 differs from that shown. Reason: Frameshift at position 694.
    The sequence GT280934 differs from that shown. Reason: Frameshift at position 615.
    The sequence GT282050 differs from that shown. Reason: Frameshift at position 756.
    The sequence GT282702 differs from that shown. Reason: Frameshift at position 812.
    The sequence GT282776 differs from that shown. Reason: Frameshift at positions 675, 684, 687 and 690.
    The sequence GT283781 differs from that shown. Reason: Frameshift at position 1069.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti391 – 3911E → Q in GT281097. (PubMed:19915030)Curated
    Sequence conflicti487 – 4871D → S in GT279548. (PubMed:19915030)Curated
    Sequence conflicti538 – 5381M → L in GT282050. (PubMed:19915030)Curated
    Sequence conflicti614 – 6141N → H in GT280934. (PubMed:19915030)Curated
    Sequence conflicti623 – 6231V → M in GT281082. (PubMed:19915030)Curated
    Sequence conflicti623 – 6231V → M in GT282050. (PubMed:19915030)Curated
    Sequence conflicti623 – 6231V → M in GT281480. (PubMed:19915030)Curated
    Sequence conflicti623 – 6231V → M in GT279953. (PubMed:19915030)Curated
    Sequence conflicti653 – 6531K → E in GT284045. (PubMed:19915030)Curated
    Sequence conflicti658 – 6581F → V in GT279353. (PubMed:19915030)Curated
    Sequence conflicti687 – 6871D → E in GT279548. (PubMed:19915030)Curated
    Sequence conflicti691 – 6911V → R in GT279548. (PubMed:19915030)Curated
    Sequence conflicti743 – 7431D → N in GT278127. (PubMed:19915030)Curated
    Sequence conflicti752 – 7521D → E in GT282050. (PubMed:19915030)Curated
    Sequence conflicti806 – 8061Q → P in GT282702. (PubMed:19915030)Curated
    Sequence conflicti806 – 8061Q → P in GT281480. (PubMed:19915030)Curated
    Sequence conflicti807 – 8071E → G in GT282702. (PubMed:19915030)Curated
    Sequence conflicti863 – 8653VNG → PSW in GT284045. (PubMed:19915030)Curated
    Sequence conflicti866 – 87611NPWTDNVKVLD → SP in GT283781. (PubMed:19915030)CuratedAdd
    BLAST
    Sequence conflicti870 – 8712DN → GH in GT284045. (PubMed:19915030)Curated
    Sequence conflicti957 – 9571D → N in GT279087. (PubMed:19915030)Curated
    Sequence conflicti964 – 9641A → T in GT279087. (PubMed:19915030)Curated
    Sequence conflicti1104 – 11041R → K in GT283348. (PubMed:19915030)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GT277795 mRNA. No translation available.
    GT278040 mRNA. No translation available.
    GT278051 mRNA. No translation available.
    GT278127 mRNA. No translation available.
    GT278167 mRNA. No translation available.
    GT278276 mRNA. No translation available.
    GT278283 mRNA. No translation available.
    GT278457 mRNA. No translation available.
    GT278599 mRNA. No translation available.
    GT279087 mRNA. No translation available.
    GT279290 mRNA. No translation available.
    GT279353 mRNA. No translation available.
    GT279393 mRNA. No translation available.
    GT279548 mRNA. No translation available.
    GT279589 mRNA. No translation available.
    GT279825 mRNA. No translation available.
    GT279940 mRNA. No translation available.
    GT279953 mRNA. No translation available.
    GT280934 mRNA. No translation available.
    GT280997 mRNA. No translation available.
    GT281082 mRNA. No translation available.
    GT281097 mRNA. No translation available.
    GT281480 mRNA. No translation available.
    GT281527 mRNA. No translation available.
    GT281701 mRNA. No translation available.
    GT281791 mRNA. No translation available.
    GT281846 mRNA. No translation available.
    GT282021 mRNA. No translation available.
    GT282046 mRNA. No translation available.
    GT282050 mRNA. No translation available.
    GT282275 mRNA. No translation available.
    GT282639 mRNA. No translation available.
    GT282702 mRNA. No translation available.
    GT282719 mRNA. No translation available.
    GT282776 mRNA. No translation available.
    GT283348 mRNA. No translation available.
    GT283584 mRNA. No translation available.
    GT283781 mRNA. No translation available.
    GT284045 mRNA. No translation available.
    GT284443 mRNA. No translation available.
    EZ420123 mRNA. No translation available.
    EZ420192 mRNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GT277795 mRNA. No translation available.
    GT278040 mRNA. No translation available.
    GT278051 mRNA. No translation available.
    GT278127 mRNA. No translation available.
    GT278167 mRNA. No translation available.
    GT278276 mRNA. No translation available.
    GT278283 mRNA. No translation available.
    GT278457 mRNA. No translation available.
    GT278599 mRNA. No translation available.
    GT279087 mRNA. No translation available.
    GT279290 mRNA. No translation available.
    GT279353 mRNA. No translation available.
    GT279393 mRNA. No translation available.
    GT279548 mRNA. No translation available.
    GT279589 mRNA. No translation available.
    GT279825 mRNA. No translation available.
    GT279940 mRNA. No translation available.
    GT279953 mRNA. No translation available.
    GT280934 mRNA. No translation available.
    GT280997 mRNA. No translation available.
    GT281082 mRNA. No translation available.
    GT281097 mRNA. No translation available.
    GT281480 mRNA. No translation available.
    GT281527 mRNA. No translation available.
    GT281701 mRNA. No translation available.
    GT281791 mRNA. No translation available.
    GT281846 mRNA. No translation available.
    GT282021 mRNA. No translation available.
    GT282046 mRNA. No translation available.
    GT282050 mRNA. No translation available.
    GT282275 mRNA. No translation available.
    GT282639 mRNA. No translation available.
    GT282702 mRNA. No translation available.
    GT282719 mRNA. No translation available.
    GT282776 mRNA. No translation available.
    GT283348 mRNA. No translation available.
    GT283584 mRNA. No translation available.
    GT283781 mRNA. No translation available.
    GT284045 mRNA. No translation available.
    GT284443 mRNA. No translation available.
    EZ420123 mRNA. No translation available.
    EZ420192 mRNA. No translation available.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00349 .

    Family and domain databases

    Gene3Di 2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR004866. CHB/HEX_N_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF03173. CHB_HEX. 1 hit.
    PF00728. Glyco_hydro_20. 1 hit.
    [Graphical view ]
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 2 hits.
    SSF55545. SSF55545. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION.
      Tissue: Mantle1 Publication.
    2. "Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell."
      Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C., Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.
      Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 658-664; 761-767 AND 1005-1016, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Shell.

    Entry informationi

    Entry nameiHEX_PINMA
    AccessioniPrimary (citable) accession number: P86956
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 15 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3