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H2A0L6 (HEX_PINMG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 12. 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 margaritifera (Black-lipped pearl oyster)
Taxonomic identifier102329 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Protein attributes

Sequence length1135 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.

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 – 11351112Putative beta-hexosaminidase
PRO_0000418019

Regions

Compositional bias937 – 100468Pro-rich
Compositional bias1006 – 1133128Gln-rich

Sequences

Sequence LengthMass (Da)Tools
H2A0L6 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 208E25A2E93AA61E

FASTA1,135126,661
        10         20         30         40         50         60 
MKWVKSGVGI LGILLTICHA VTSQGHILDI TDSLKITFKT LSNFGPRAQS IQNVTIENVG 

        70         80         90        100        110        120 
IKDIPDSGWR CYFCHDQLLF PGTFNLARNQ YFLRPILDNY VVLSDGFLLE FIKGCMYRIT 

       130        140        150        160        170        180 
PIPRNAPIKT RDKREFTLLA EQFSVSKYDS FPKWYCETIS GGNTEVGIIR NTENLKYVED 

       190        200        210        220        230        240 
FDSSYNWFRI PHDFRSVPLQ PQDRFSANHK ASSVDECKYK VIPTPVKASV SKVQRNFGTT 

       250        260        270        280        290        300 
VYYGTTDTSI RGREKLFKVA EQLALKHNLG LVEITPGLTV NNGISLVVTG NYVERNIPSP 

       310        320        330        340        350        360 
DEAYSLTVTA DLISIEAPAL PGLINGIETI HSLSAWDMAL PYGGIKDFPR FPFRGIFLDI 

       370        380        390        400        410        420 
ASNFPGYNYI KKFLTVMAQY KLNKLVLPMY NNEGFRLQLN DSPRYEFQAL HMIGGKRCHD 

       430        440        450        460        470        480 
LKEEKCLFSQ LGSGPDSSGG YLTKAQMTDL IKTADLLNIE IIMSMNIGES ARGAIVPLKQ 

       490        500        510        520        530        540 
SPHSRLLYDP DDTDFVDRFY PQKDTSMNPC REETTYFYDH MLKQLKDIYN AASVPLKTIM 

       550        560        570        580        590        600 
IGSKVNFDQV LNSKYCYASN LNSTQRLMAR GNLERNINGF KLNFTKRLVK TAHDNGIKEV 

       610        620        630        640        650        660 
MAIDDVFTTE FDAEGNTPNT VYDTKNSDNS TRFNATVTAV HSRYDTVRDE RLWKRGDRFA 

       670        680        690        700        710        720 
ELGYKVILSP PILDFNYAVE PDPDRPGDYD SVIRNISFSK LFRFVPDSRC CNIPNAIQHD 

       730        740        750        760        770        780 
CALESDCTTA GAKDSYIGTL GKLDTRKLRS LKDWNELLFP RLLIFAERSW HKSSWEDSFG 

       790        800        810        820        830        840 
PHRASVNNIT RQLITNYTVP NWNDINNEES KVLGCISRKE KLRLMHEDGL KPYVEPPGAR 

       850        860        870        880        890        900 
LLGGNTMRIA ASTTEDSFWV QASVNGNPWT DNVKILDVNP TDSVRLRTVH PAKAELRSKE 

       910        920        930        940        950        960 
VKLNLTSLPT PRERFRKIAQ DALSRRIGID IQRARMPPMP VNPAYRPPVP LPSFDPADDR 

       970        980        990       1000       1010       1020 
APDLAAIAAA HPPPLPPGMP SHMMPNMPPP FPPRPPFGPP MLPPGQMRAL GQQAGQALRG 

      1030       1040       1050       1060       1070       1080 
QGTALGPQTG QQPMPAQPRG PLTGQAAGTG VAGQTGQQPS TAGQGTQQGL PGQQRGGVLP 

      1090       1100       1110       1120       1130 
GQWPFFPGMP AAQFPPMFNP QMQRALQMRG QGQIPQRTQG AAAGAGQSRI PQQAG 

« Hide

References

[1]"Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization."
Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F., Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.
BMC Genomics 11:613-613(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 259-266, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Shell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE610383 mRNA. Translation: CCE46157.1.

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.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
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.
ProtoNetSearch...

Entry information

Entry nameHEX_PINMG
AccessionPrimary (citable) accession number: H2A0L6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: March 21, 2012
Last modified: October 16, 2013
This is version 12 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