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Protein

Hyaluronidase-2

Gene

HYAL2

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Receptor

Keywords - Biological processi

Host-virus interaction

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase-2 (EC:3.2.1.35)
Short name:
Hyal-2
Alternative name(s):
Hyaluronoglucosaminidase-2
Gene namesi
Name:HYAL2
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 451431Hyaluronidase-2PRO_0000239065Add
BLAST
Propeptidei452 – 47625Removed in mature formSequence AnalysisPRO_0000239066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 343By similarity
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi214 ↔ 230By similarity
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi368 ↔ 379By similarity
Disulfide bondi373 ↔ 430By similarity
Disulfide bondi432 ↔ 441By similarity
Lipidationi451 – 4511GPI-anchor amidated glycineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Interacts with MST1R (By similarity). Interacts with Jaagsiekte sheep retrovirus (JSRV) envelope proteins.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8SQG7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini364 – 44279EGF-likeAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated
Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

GeneTreeiENSGT00550000074476.
HOVERGENiHBG052053.
KOiK01197.
OMAiWGGEQCQ.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8SQG7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTGLGPAVT LALVLVVAWA TELKPTAPPI FTGRPFVVAW DVPTQDCGPR
60 70 80 90 100
HKMPLDPKDM KAFDVQASPN EGFVNQNITI FYRDRLGMYP HFNSVGRSVH
110 120 130 140 150
GGVPQNGSLW VHLEMLKGHV EHYIRTQEPA GLAVIDWEDW RPVWVRNWQD
160 170 180 190 200
KDVYRRLSRQ LVASHHPDWP PERIVKEAQY EFEFAARQFM LETLRFVKAF
210 220 230 240 250
RPRHLWGFYL FPDCYNHDYV QNWETYTGRC PDVEVSRNDQ LSWLWAESTA
260 270 280 290 300
LFPSVYLEET LASSTHGRNF VSFRVQEALR VADVHHANHA LPVYVFTRPT
310 320 330 340 350
YSRGLTGLSE MDLISTIGES AALGAAGVIL WGDAGFTTSN ETCRRLKDYL
360 370 380 390 400
TRSLVPYVVN VSWAAQYCSW AQCHGHGRCV RRDPNAHTFL HLSASSFRLV
410 420 430 440 450
PSHAPDEPRL RPEGELSWAD RNHLQTHFRC QCYLGWGGEQ CQWDRRRAAG
460 470
GASGAWAGSH LTGLLAVAVL AFTWTS
Length:476
Mass (Da):54,229
Last modified:June 1, 2002 - v1
Checksum:i427C9277ACF7AAAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411974 mRNA. Translation: AAL78386.1.
RefSeqiNP_001009754.1. NM_001009754.1.
UniGeneiOar.905.

Genome annotation databases

EnsembliENSOART00000010462; ENSOARP00000010309; ENSOARG00000009614.
GeneIDi443154.
KEGGioas:443154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411974 mRNA. Translation: AAL78386.1.
RefSeqiNP_001009754.1. NM_001009754.1.
UniGeneiOar.905.

3D structure databases

ProteinModelPortaliQ8SQG7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOART00000010462; ENSOARP00000010309; ENSOARG00000009614.
GeneIDi443154.
KEGGioas:443154.

Organism-specific databases

CTDi8692.

Phylogenomic databases

GeneTreeiENSGT00550000074476.
HOVERGENiHBG052053.
KOiK01197.
OMAiWGGEQCQ.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mechanism of cell entry and transformation by enzootic nasal tumor virus."
    Dirks C., Duh F.-M., Rai S.K., Lerman M.I., Miller A.D.
    J. Virol. 76:2141-2149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: INTERACTION WITH JSRV ENVELOPE PROTEINS.

Entry informationi

Entry nameiHYAL2_SHEEP
AccessioniPrimary (citable) accession number: Q8SQG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2002
Last modified: May 27, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Acts as a receptor for the Jaagsiekte sheep retrovirus (JSRV), which induces ovine pulmonary adenocarcinoma. A possible mechanism is that binding to JSRV envelope proteins may liberate the oncogenic factor MST1R that is normally negatively regulated by HYAL2, leading to oncogenic transformation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.