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Q9Z2Q3 (HYAL2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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-anchor By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

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 sequence or structural similarity. 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

hyaluronan catabolic process

Inferred from direct assay PubMed 19635555. Source: UniProtKB

kidney development

Inferred from expression pattern PubMed 17706761. Source: UniProtKB

monocyte activation

Inferred from sequence or structural similarity. Source: UniProtKB

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 inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-6 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of urine volume

Inferred from expression pattern PubMed 19635555. Source: UniProtKB

renal water absorption

Inferred from expression pattern PubMed 19635555. Source: UniProtKB

response to reactive oxygen species

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from sequence or structural similarity. Source: UniProtKB

transformation of host cell by virus

Inferred from direct assay PubMed 12584308. Source: RGD

viral entry into host cell

Inferred from direct assay PubMed 12584308. Source: RGD

   Cellular_componentGolgi membrane

Inferred from direct assay 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

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_functionhyaluronic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronoglucuronidase activity

Inferred from direct assay PubMed 19635555. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein tyrosine kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

virus receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 448428Hyaluronidase-2
PRO_0000012103
Propeptide449 – 47325Removed in mature form Potential
PRO_0000012104

Regions

Domain361 – 43979EGF-like

Sites

Active site1351Proton donor By similarity

Amino acid modifications

Lipidation4481GPI-anchor amidated aspartate Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation3571N-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

Sequences

Sequence LengthMass (Da)Tools
Q9Z2Q3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 46B90A2F260B0CE4

FASTA47353,999
        10         20         30         40         50         60 
MRAGLGPIIT LALVLEVAWA SELKPTAPPI FTGRPFVVAW NVPTQECAPR HKVPLDLRAF 

        70         80         90        100        110        120 
DVEATPNEGF FNQNITTFYY DRLGLYPRFD AAGMSVHGGV PQNGSLCAHL PMLKEAVERY 

       130        140        150        160        170        180 
IQTQEPAGLA VIDWEEWRPV WVRNWQEKDV YRQSSRQLVA SRHPDWPSDR IVKQAQYEFE 

       190        200        210        220        230        240 
FAARQFMLNT LRYVKAVRPQ HLWGFYLFPD CYNHDYVQNW DSYTGRCPDV EVAQNDQLAW 

       250        260        270        280        290        300 
LWAENTALFP SVYLDKTLAS SKHSRNFVSF RVQEALRVAH THHANHALPV YVFTRPTYTR 

       310        320        330        340        350        360 
RLTELNQMDL ISTIGESAAL GSAGVIFWGD SVYASSMENC QNLKKYLTQT LVPYIVNVSW 

       370        380        390        400        410        420 
ATQYCSWTQC HGHGRCVRRN PSASTFLHLS PSSFRLVPGR TPSEPQLRPE GELSEDDLSY 

       430        440        450        460        470 
LQMHFRCHCY LGWGGEQCQW NHKRAAGDAS RAWAGAHLAS LLGLVAMTLT WTL 

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References

[1]"Cloning and expression of the cDNA for a rat hyaluronidase."
Boel P., Mertens-Strijthagen J., Flamion B.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF034218 mRNA. Translation: AAD01980.1.
UniGeneRn.8278.

3D structure databases

ProteinModelPortalQ9Z2Q3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PaxDbQ9Z2Q3.
PRIDEQ9Z2Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:620321. rat.

Organism-specific databases

RGD620321. Hyal2.

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidQ9Z2Q3.
PhylomeDBQ9Z2Q3.

Gene expression databases

GenevestigatorQ9Z2Q3.

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

PROQ9Z2Q3.

Entry information

Entry nameHYAL2_RAT
AccessionPrimary (citable) accession number: Q9Z2Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 99 of the entry and version 1 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries