Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P86956 (HEX_PINMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative beta-hexosaminidase

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
Chitobiase
N-acetyl-beta-glucosaminidase
OrganismPinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster)
Taxonomic identifier104660 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Protein attributes

Sequence length1130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. UniProtKB Q04786

Pathway

Glycan degradation; chitin degradation. UniProtKB Q04786

Subcellular location

Secreted Ref.2.

Tissue specificity

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. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Sequence caution

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.

The sequence GT284443 differs from that shown. Reason: Premature stop codon at position 218.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

chitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 11301107Putative beta-hexosaminidase
PRO_0000413087

Regions

Compositional bias936 – 100166Pro-rich
Compositional bias1003 – 1128126Gln-rich

Experimental info

Sequence conflict3911E → Q in GT281097. Ref.1
Sequence conflict4871D → S in GT279548. Ref.1
Sequence conflict5381M → L in GT282050. Ref.1
Sequence conflict6141N → H in GT280934. Ref.1
Sequence conflict6231V → M in GT281082. Ref.1
Sequence conflict6231V → M in GT282050. Ref.1
Sequence conflict6231V → M in GT281480. Ref.1
Sequence conflict6231V → M in GT279953. Ref.1
Sequence conflict6531K → E in GT284045. Ref.1
Sequence conflict6581F → V in GT279353. Ref.1
Sequence conflict6871D → E in GT279548. Ref.1
Sequence conflict6911V → R in GT279548. Ref.1
Sequence conflict7431D → N in GT278127. Ref.1
Sequence conflict7521D → E in GT282050. Ref.1
Sequence conflict8061Q → P in GT282702. Ref.1
Sequence conflict8061Q → P in GT281480. Ref.1
Sequence conflict8071E → G in GT282702. Ref.1
Sequence conflict863 – 8653VNG → PSW in GT284045. Ref.1
Sequence conflict866 – 87611NPWTDNVKVLD → SP in GT283781. Ref.1
Sequence conflict870 – 8712DN → GH in GT284045. Ref.1
Sequence conflict9571D → N in GT279087. Ref.1
Sequence conflict9641A → T in GT279087. Ref.1
Sequence conflict11041R → K in GT283348. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P86956 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 9F180107C5016EA5

FASTA1,130126,718
        10         20         30         40         50         60 
MKWVKSGVGI LGILLIICHA VTSQRRILDI TDNLKITFKT ISNFGPRAQS IQNVTIENVG 

        70         80         90        100        110        120 
IKDIPDFGWR CYFCHDQLLF PGTFNLARSQ YFLRPILDNY VVLSDGFLLE FIKGCMYRIT 

       130        140        150        160        170        180 
PIPRNAPIKT RDKREFTLLA EQFSVSKYDS FPNWYCETIS GGNTEVANIR STENLKYVED 

       190        200        210        220        230        240 
FDSSYNWFRI PHDFRSVPLQ PQDRYSANHK ASSVEECKYK VIPTPVKASV RKVQRNFGTT 

       250        260        270        280        290        300 
VYYGTTDTSI RGKLFKVAEK LALKHKLGLV EMTPGQPVNN GISLVVTGNY IERNIPSPDE 

       310        320        330        340        350        360 
AYRLSVSADL ISIEAPALPG LINGIETMHS LSAWDMALPY GGVKDFPRFP FRGIFLDIAS 

       370        380        390        400        410        420 
NFPGYNYMMK FLTVMAQYKL NKLVLPLYNN EGFRLELNDS PGYEFQALHL VGGNRCHDLK 

       430        440        450        460        470        480 
EENCLFSQLG SFAGNSDGYL TKGDMVDLIK TADLLNIEII MSLNIGESAR GAIVPLKTSK 

       490        500        510        520        530        540 
HNRLLYDPED TDFVDRFYPQ KDSSMNPCRE ETMIFYDHML KQLKAIYKAA SVPLKTIMIG 

       550        560        570        580        590        600 
SKVNFDQVLN SKYCYPKNLN STQRLMEREN LERNINGFKL NFTKRLVKTA HDNGINEVMA 

       610        620        630        640        650        660 
IDDVFTTEFD AAGNTPNTVY DTVDSETNKT RFNATVTAVH SRYDTVRDER LWKRGDRFAE 

       670        680        690        700        710        720 
LGYKVIISPP ILDFNYAVEP DPDRPGDYDS VIRNISFSKL FRFVPDSHCC NIPNAIQHDC 

       730        740        750        760        770        780 
ALESDCTTAG PPDSYIGTLG KLDTRKLRSL KDWNELLFPR LLIFAERSWH KSSWEDSFEP 

       790        800        810        820        830        840 
HRVRMNNITR QIITNYTVPN WNDIIQEESK VLGCISRKEK LRLMHEDGLK PYVEPPGARL 

       850        860        870        880        890        900 
LGGNTMRIAA STTEDSFWVQ ASVNGNPWTD NVKVLDVNPT DSVRLRTVHP AKAELRSKEV 

       910        920        930        940        950        960 
KLNLTSLPTP REQFRKIAQD ALSRRIGIDI QRARMPPMPV NPTYRPPVPL PSFDPADDRA 

       970        980        990       1000       1010       1020 
PDLAAIAAAH PPPLPPGMPP HMMPNMPFPP RPPFVPPLLP PGQMRALGQQ AGQALRGQGQ 

      1030       1040       1050       1060       1070       1080 
QTGQQTLPAQ PRGPMGLTGQ AAGTGVAGQS GQQPSAAGQG TQQGLPGQQR TGVVPGQWPF 

      1090       1100       1110       1120       1130 
FPGMPAAQFP PMFNPQMQRA LQMRGQGQIP QTQGAVAGAG QSRVPQQQAG 

« Hide

References

[1]"Parallel evolution of nacre building gene sets in molluscs."
Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M., Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D., Degnan B.M.
Mol. Biol. Evol. 27:591-608(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION.
Tissue: Mantle.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00349.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProIPR025705. 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]
PfamPF03173. CHB_HEX. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF55545. SSF55545. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEX_PINMA
AccessionPrimary (citable) accession number: P86956
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries