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Reviewed, UniProtKB/Swiss-Prot O35632 (HYAL2_MOUSE)

Last modified November 25, 2008. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hyaluronidase-2
      Short name=Hyal-2
    EC=3.2.1.35
Alternative name(s):
    Hyaluronoglucosaminidase-2
      Short name=LUCA-2
Gene names
Name: Hyal2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R By similarity.

Catalytic activity

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Subunit structure

Interacts with MST1R By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchorBy similarity.

Tissue specificity

Widely expressed. In the brain, expressed during embryonic stages but expression decreases after birth and is barely detectable in adult brain. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Caution

Was originally thought to be lysosomal.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 448428Hyaluronidase-2
PRO_0000012101
Propeptide449 – 47325Removed in mature form Potential
PRO_0000012102

Regions

Domain361 – 43979EGF-like

Sites

Active site1351Proton donor By similarity

Amino acid modifications

Lipidation4481GPI-anchor amidated asparagine Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation4481N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 340 By similarity
Disulfide bond211 ↔ 227 By similarity
Disulfide bond365 ↔ 376 By similarity
Disulfide bond370 ↔ 427 By similarity
Disulfide bond429 ↔ 438 By similarity

Experimental info

Sequence conflict26 – 272TA → KP in CAA03888 and CAA03889. Ref.1
Sequence conflict193 – 1997YVKAVRP → LRQGSQT in CAA03888. Ref.1
Sequence conflict2501Missing in CAA03888. Ref.1
Sequence conflict269 – 2724SFRV → RFGG in CAA03888. Ref.1
Sequence conflict3551I → V in AAK28481. Ref.2
Sequence conflict3831A → V in CAA03888 and CAA03889. Ref.1
Sequence conflict416 – 4227ADLNYLQ → RDRQLPE in CAA03888. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35632-1 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: DD433C9FFCF8147C

FASTA47353,618
        10         20         30         40         50         60 
MRAGLGPIIT LALVLEVAWA GELKPTAPPI FTGRPFVVAW NVPTQECAPR HKVPLDLRAF 

        70         80         90        100        110        120 
DVKATPNEGF FNQNITTFYY DRLGLYPRFD AAGTSVHGGV PQNGSLCAHL PMLKESVERY 

       130        140        150        160        170        180 
IQTQEPGGLA VIDWEEWRPV WVRNWQEKDV YRQSSRQLVA SRHPDWPSDR VMKQAQYEFE 

       190        200        210        220        230        240 
FAARQFMLNT LRYVKAVRPQ HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW 

       250        260        270        280        290        300 
LWAESTALFP SVYLDETLAS SVHSRNFVSF RVREALRVAH THHANHALPV YVFTRPTYTR 

       310        320        330        340        350        360 
GLTGLSQVDL ISTIGESAAL GSAGVIFWGD SEDASSMETC QYLKNYLTQL LVPYIVNVSW 

       370        380        390        400        410        420 
ATQYCSWTQC HGHGRCVRRN PSANTFLHLN ASSFRLVPGH TPSEPQLRPE GQLSEADLNY 

       430        440        450        460        470 
LQKHFRCQCY LGWGGEQCQR NYKGAAGNAS RAWAGSHLTS LLGLVAVALT WTL 

« Hide

References

[1]"Structural organization and chromosomal localization of Hyal2, a gene encoding a lysosomal hyaluronidase."
Strobl B., Wechselberger C., Beier D., Lepperdinger G.
Genomics 53:214-219(1998) [PubMed: 9790770] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Strain: 129/SvJ.
[2]"Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation."
Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A., Lerman M.I., Miller A.D.
Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001) [PubMed: 11296287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H and Czech II.
[3]"Transforming growth factor-beta1 blocks the enhancement of tumor necrosis factor cytotoxicity by hyaluronidase Hyal-2 in L929 fibroblasts."
Chang N.-S.
BMC Cell Biol. 3:8-8(2002) [PubMed: 11960552] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Czech II.
[4]"Hyal2 -- less active, but more versatile?"
Lepperdinger G., Mullegger J., Kreil G.
Matrix Biol. 20:509-514(2001) [PubMed: 11731268] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ000059 mRNA. Translation: CAA03888.1.
AJ000060 Genomic DNA. Translation: CAA03889.1.
AF302843 mRNA. Translation: AAK28481.1.
AF302844 mRNA. Translation: AAK28482.1.
AF422177 mRNA. Translation: AAL17823.1.
RefSeqNP_034619.2.
UniGeneMm.465277
Mm.4834

3D structure databases

HSSPHSSP built from PDB template 1FCQ based on UniProtKB Q08169.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000010047. Mus musculus. [Contig view]
GeneID15587.
KEGGmmu:15587.

Organism-specific databases

MGIMGI:1196334. Hyal2.

Phylogenomic databases

HOGENOMO35632.
HOVERGENO35632.

Gene expression databases

ArrayExpressO35632.
CleanExMM_HYAL2.
GermOnlineENSMUSG00000010047. Mus musculus.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR006210. EGF.
IPR000742. EGF_3.
IPR013032. EGF_like_reg_CS.
IPR001968. Glyco_hydro_56.
IPR017430. Glyco_hydro_56_Hyaluronidase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11769. Glyco_hydro_56. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
ProDomPD003549. Glyco_hydro_56. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00181. EGF. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio288580.
SOURCESearch...

Entry information

Entry nameHYAL2_MOUSE
AccessionPrimary (citable) accession number: O35632
Secondary accession number(s): O35631, Q99MS9, Q99MT0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents