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O35632 (HYAL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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:
Hyaluronidase-2

Short name=Hyal-2
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-2
Gene names
Name:Hyal2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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-anchor By 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.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
Receptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cartilage development

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to UV-B

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to fibroblast growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to transforming growth factor beta stimulus

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from direct assay PubMed 16191204. Source: UniProtKB

fusion of virus membrane with host plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

glycosaminoglycan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic progenitor cell differentiation

Inferred from mutant phenotype PubMed 18772348. Source: MGI

hyaluronan catabolic process

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

monocyte activation

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

multicellular organismal aging

Inferred from mutant phenotype PubMed 18772348. Source: MGI

multicellular organismal iron ion homeostasis

Inferred from mutant phenotype PubMed 18772348. Source: MGI

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 19366691. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

positive regulation of interleukin-6 secretion

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

positive regulation of interleukin-8 secretion

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

positive regulation of protein import into nucleus

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

positive regulation of urine volume

Inferred from sequence or structural similarity. Source: UniProtKB

renal water absorption

Inferred from sequence or structural similarity. Source: UniProtKB

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to reactive oxygen species

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from direct assay Ref.2. Source: UniProtKB

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 18772348. Source: MGI

transformation of host cell by virus

Inferred from sequence or structural similarity. Source: UniProtKB

viral entry into host cell

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from sequence or structural similarity PubMed 21740893. Source: UniProtKB

anchored component of plasma membrane

Inferred from direct assay PubMed 21740893. Source: UniProtKB

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 21740893. Source: UniProtKB

microvillus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 19366691. Source: BHF-UCL

hyaluronic acid binding

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

hyaluronoglucuronidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from sequence or structural similarity PubMed 19443707. Source: UniProtKB

receptor signaling protein tyrosine kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta binding

Inferred from physical interaction PubMed 19366691. Source: BHF-UCL

virus receptor activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

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; alternate Potential
Glycosylation741N-linked (GlcNAc...) Ref.5
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Ref.5
Glycosylation4481N-linked (GlcNAc...); alternate 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. Ref.1
Sequence conflict26 – 272TA → KP in 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. Ref.1
Sequence conflict3831A → V in CAA03889. Ref.1
Sequence conflict416 – 4227ADLNYLQ → RDRQLPE in CAA03888. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35632 [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

« Hide 'large scale' 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-390.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. NM_010489.2.
XP_006511706.1. XM_006511643.1.
XP_006511707.1. XM_006511644.1.
XP_006511708.1. XM_006511645.1.
UniGeneMm.440982.
Mm.4834.

3D structure databases

ProteinModelPortalO35632.
SMRO35632. Positions 29-440.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PRIDEO35632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010191; ENSMUSP00000010191; ENSMUSG00000010047.
GeneID15587.
KEGGmmu:15587.
UCSCuc009rlu.1. mouse.

Organism-specific databases

CTD8692.
MGIMGI:1196334. Hyal2.

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidO35632.
KOK01197.
OMAGWGGEQC.
OrthoDBEOG74J97S.
PhylomeDBO35632.
TreeFamTF321598.

Gene expression databases

ArrayExpressO35632.
BgeeO35632.
CleanExMM_HYAL2.
GenevestigatorO35632.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288580.
PROO35632.
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: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries