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Protein

Hyaluronidase-2

Gene

Hyal2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Active sitei135Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Receptor

Enzyme and pathway databases

BRENDAi3.2.1.35. 5301.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620321. Hyal2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001210321 – 448Hyaluronidase-2Add BLAST428
PropeptideiPRO_0000012104449 – 473Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 340By similarity
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi211 ↔ 227By similarity
Glycosylationi357N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi365 ↔ 376By similarity
Disulfide bondi370 ↔ 427By similarity
Disulfide bondi429 ↔ 438By similarity
Lipidationi448GPI-anchor amidated aspartateSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9Z2Q3.
PRIDEiQ9Z2Q3.

Interactioni

Subunit structurei

Interacts with MST1R.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017461.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2Q3.
SMRiQ9Z2Q3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini361 – 439EGF-likeAdd BLAST79

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiENOG410IECJ. Eukaryota.
ENOG410XPZT. LUCA.
HOGENOMiHOG000015133.
HOVERGENiHBG052053.
InParanoidiQ9Z2Q3.
PhylomeDBiQ9Z2Q3.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiView protein in Pfam
PF01630. Glyco_hydro_56. 1 hit.
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Z2Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAGLGPIIT LALVLEVAWA SELKPTAPPI FTGRPFVVAW NVPTQECAPR
60 70 80 90 100
HKVPLDLRAF DVEATPNEGF FNQNITTFYY DRLGLYPRFD AAGMSVHGGV
110 120 130 140 150
PQNGSLCAHL PMLKEAVERY IQTQEPAGLA VIDWEEWRPV WVRNWQEKDV
160 170 180 190 200
YRQSSRQLVA SRHPDWPSDR IVKQAQYEFE FAARQFMLNT LRYVKAVRPQ
210 220 230 240 250
HLWGFYLFPD CYNHDYVQNW DSYTGRCPDV EVAQNDQLAW LWAENTALFP
260 270 280 290 300
SVYLDKTLAS SKHSRNFVSF RVQEALRVAH THHANHALPV YVFTRPTYTR
310 320 330 340 350
RLTELNQMDL ISTIGESAAL GSAGVIFWGD SVYASSMENC QNLKKYLTQT
360 370 380 390 400
LVPYIVNVSW ATQYCSWTQC HGHGRCVRRN PSASTFLHLS PSSFRLVPGR
410 420 430 440 450
TPSEPQLRPE GELSEDDLSY LQMHFRCHCY LGWGGEQCQW NHKRAAGDAS
460 470
RAWAGAHLAS LLGLVAMTLT WTL
Length:473
Mass (Da):53,999
Last modified:May 1, 1999 - v1
Checksum:i46B90A2F260B0CE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034218 mRNA. Translation: AAD01980.1.
UniGeneiRn.8278.

Genome annotation databases

UCSCiRGD:620321. rat.

Similar proteinsi

Entry informationi

Entry nameiHYAL2_RAT
AccessioniPrimary (citable) accession number: Q9Z2Q3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 1999
Last modified: November 22, 2017
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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