Putative beta-hexosaminidase precursor - Pinctada maxima (Silver-lipped pearl oyster)

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P86956 (HEX_PINMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 11. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Putative beta-hexosaminidase EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase Chitobiase N-acetyl-beta-glucosaminidase
Organism	Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster)
Taxonomic identifier	104660 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Pteriomorphia › Pterioida › Pterioidea › Pteriidae › Pinctada

Protein attributes

Sequence length	1130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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). 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 component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Chain

24 – 1130

1107

Putative beta-hexosaminidase

PRO_0000413087

Regions

Compositional bias

936 – 1001

Pro-rich

Compositional bias

1003 – 1128

126

Gln-rich

Experimental info

Sequence conflict

391

E → Q in GT281097. Ref.1

Sequence conflict

487

D → S in GT279548. Ref.1

Sequence conflict

538

M → L in GT282050. Ref.1

Sequence conflict

614

N → H in GT280934. Ref.1

Sequence conflict

623

V → M in GT281082. Ref.1

Sequence conflict

623

V → M in GT282050. Ref.1

Sequence conflict

623

V → M in GT281480. Ref.1

Sequence conflict

623

V → M in GT279953. Ref.1

Sequence conflict

653

K → E in GT284045. Ref.1

Sequence conflict

658

F → V in GT279353. Ref.1

Sequence conflict

687

D → E in GT279548. Ref.1

Sequence conflict

691

V → R in GT279548. Ref.1

Sequence conflict

743

D → N in GT278127. Ref.1

Sequence conflict

752

D → E in GT282050. Ref.1

Sequence conflict

806

Q → P in GT282702. Ref.1

Sequence conflict

806

Q → P in GT281480. Ref.1

Sequence conflict

807

E → G in GT282702. Ref.1

Sequence conflict

863 – 865

VNG → PSW in GT284045. Ref.1

Sequence conflict

866 – 876

NPWTDNVKVLD → SP in GT283781. Ref.1

Sequence conflict

870 – 871

DN → GH in GT284045. Ref.1

Sequence conflict

957

D → N in GT279087. Ref.1

Sequence conflict

964

A → T in GT279087. Ref.1

Sequence conflict

1104

R → K in GT283348. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P86956 [UniParc].

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

FASTA

1,130

126,718

        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

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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]	"Dissimilar protein secretions control the deposition of nacreous and prismatic shell layers by the pearl oyster mantle epithelia." Marie B., Joubert C., Marin F., Gueguen Y., Montagnani C. Submitted (JUN-2011) to UniProtKB 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
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00349.
Family and domain databases
Gene3D	2.60.40.290. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR025705. 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]
Pfam	PF03173. CHB_HEX. 1 hit. PF00728. Glyco_hydro_20. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEX_PINMA

Accession

Primary (citable) accession number: P86956

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	October 19, 2011
Last modified:	May 1, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents