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Q5E985 (HYAL1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length450 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.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Sequence caution

The sequence AAX08792.1 differs from that shown. Reason: Frameshift at position 139.

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 – 3535 Potential
Chain36 – 450415Hyaluronidase-1
PRO_0000042623

Regions

Domain433 – 44412EGF-like

Sites

Active site1461Proton donor By similarity

Amino acid modifications

Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 348 By similarity
Disulfide bond222 ↔ 236 By similarity
Disulfide bond373 ↔ 384 By similarity
Disulfide bond378 ↔ 433 By similarity
Disulfide bond435 ↔ 444 By similarity

Experimental info

Sequence conflict3331V → L in AAI02474. Ref.2
Sequence conflict4491M → L in AAI02474. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5E985 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 576DD38745585AB5

FASTA45050,508
        10         20         30         40         50         60 
MRPFSLEVSL HLPWAMAAHL LPVCTLFLNL LSMTQGSRDP VVPNQPFTTI WNANTEWCMK 

        70         80         90        100        110        120 
KHGVDVDISI FDVVTNPGQT FRGPNMTIFY SSQLGTYPYY TSAGEPVFGG LPQNASLNAH 

       130        140        150        160        170        180 
LARTFQDILA AMPEPRFSGL AVIDWEAWRP RWAFNWDTKD IYRQRSRALV QKQHPDWLAP 

       190        200        210        220        230        240 
RVEAAAQDQF EGAAEEWMAG TLKLGQALRP QGLWGFYNFP ECYNYDFKSP NYTGRCPLNI 

       250        260        270        280        290        300 
CAQNDQLGWL WGQSRALYPS IYLPAALEGT KKTQMFVQHR VAEAFRVAAG AGDPKLPVLP 

       310        320        330        340        350        360 
YMQLFYDMTN HFLPAEELEH SLGESAAQGA AGVVLWVSWL STSTKESCQA IKEYVDTTLG 

       370        380        390        400        410        420 
PSILNVTSGA RLCSQVLCSG HGRCARRPSY PKARLILNST SFSIKPTPGG GPLTLQGALS 

       430        440        450 
LEDRLRMAVE FECRCYRGWR GTRCEQWGMW 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT020775 mRNA. Translation: AAX08792.1. Frameshift.
BT021035 mRNA. Translation: AAX09052.1.
BC102473 mRNA. Translation: AAI02474.1.
RefSeqNP_001017941.1. NM_001017941.1.
UniGeneBt.4740.

3D structure databases

ProteinModelPortalQ5E985.
SMRQ5E985. Positions 38-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000000611.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PRIDEQ5E985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID515397.
KEGGbta:515397.

Organism-specific databases

CTD3373.

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidQ5E985.
KOK01197.

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

NextBio20871809.

Entry information

Entry nameHYAL1_BOVIN
AccessionPrimary (citable) accession number: Q5E985
Secondary accession number(s): Q3T0A8, Q5E9Z4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 67 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