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Protein

Hyaluronidase-2

Gene

Hyal2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

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: May 23, 2018
This is version 117 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

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