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Q6RHW4 (HYAL1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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-1

Short name=Hyal-1
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-1
Gene names
Name:HYAL1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity. Lysosome By similarity.

Tissue specificity

Highly expressed in spleen, kidney, and lung. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   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 interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to pH

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to platelet-derived growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of hyaluranon cable assembly

Inferred from sequence or structural similarity. Source: UniProtKB

response to antibiotic

Inferred from sequence or structural similarity. 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

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluranon cable

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionhyaluronan synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 435414Hyaluronidase-1
PRO_0000042625

Regions

Domain418 – 42912EGF-like

Sites

Active site1311Proton donor By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 333 By similarity
Disulfide bond207 ↔ 221 By similarity
Disulfide bond358 ↔ 369 By similarity
Disulfide bond363 ↔ 418 By similarity
Disulfide bond420 ↔ 429 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6RHW4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5C5B7FB408B70B28

FASTA43548,507
        10         20         30         40         50         60 
MAAHLLPICT LFLNLLSVAQ GSRDPVVLNR PFTTIWNANT QWCLKRHGVD VDVSVFEVVV 

        70         80         90        100        110        120 
NPGQTFRGPN MTIFYSSQLG TYPYYTSAGE PVFGGLPQNA SLDVHLNRTF KDILAAMPES 

       130        140        150        160        170        180 
NFSGLAVIDW EAWRPRWAFN WDAKDIYRQR SRALVQKQHP DWPAPWVEAA AQDQFQEAAQ 

       190        200        210        220        230        240 
TWMAGTLKLG QTLRPHGLWG FYGFPDCYNY DFQSSNYTGQ CPPGVSAQND QLGWLWGQSR 

       250        260        270        280        290        300 
ALYPSIYLPS ALEGTNKTQL YVQHRVNEAF RVAAAAGDPN LPVLPYAQIF HDMTNRLLSR 

       310        320        330        340        350        360 
EELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQSIKEYV DTTLGPFILN VTSGALLCSQ 

       370        380        390        400        410        420 
AVCSGHGRCV RRPSHTEALP ILNPSSFSIK PTPGGGPLTL QGALSLKDRV QMAEEFQCRC 

       430 
YPGWRGTWCE QQGTR 

« Hide

References

[1]"Molecular characterization of porcine hyaluronidase genes 1, 2, and 3 clustered on SSC13q21."
Gatphayak K., Knorr C., Beck J., Brenig B.
Cytogenet. Genome Res. 106:98-106(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY497543 mRNA. Translation: AAR91599.1.
RefSeqNP_999606.1. NM_214441.1.
UniGeneSsc.26119.

3D structure databases

ProteinModelPortalQ6RHW4.
SMRQ6RHW4. Positions 23-432.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID404698.
KEGGssc:404698.

Organism-specific databases

CTD3373.

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
KOK01197.

Enzyme and pathway databases

BRENDA3.2.1.35. 6170.

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...

Entry information

Entry nameHYAL1_PIG
AccessionPrimary (citable) accession number: Q6RHW4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 62 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