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Protein

Hyaluronidase

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides.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 sitei145Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.35. 387.

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase (EC:3.2.1.35)
Short name:
Hya
Alternative name(s):
Allergen Api m II
Hyaluronoglucosaminidase
Allergen: Api m 2
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
Proteomesi
  • UP000005203 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Or 24Sequence analysisAdd BLAST28
PropeptideiPRO_000001210529 – 33Sequence analysis5
ChainiPRO_000001210634 – 382HyaluronidaseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 345
Glycosylationi115N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi221 ↔ 233
Glycosylationi263N-linked (GlcNAc...) (complex)1 Publication1

Post-translational modificationi

N-glycosylated. Glycans found include a majority of small oligosaccharides (Man1-3GlcNAc2), most of which are either alpha 1,3-monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the innermost GlcNAc residue, approximately 5% of high-mannose type structures, and 8% contains the terminal trisaccharide GalNAc beta 1-4[Fuc alpha 1-3]GlcNAc beta 1-in beta 1,2-linkage to the core alpha 1,3-mannosyl residue.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ08169.
PRIDEiQ08169.

PTM databases

UniCarbKBiQ08169.

Expressioni

Tissue specificityi

Expressed in the venom glands of worker bees. It is also detected in the testes of drones but not in the queen-bee venom glands or in pupae.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi7460.GB18543-PA.

Structurei

Secondary structure

1382
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 49Combined sources6
Helixi51 – 57Combined sources7
Helixi63 – 66Combined sources4
Helixi74 – 76Combined sources3
Beta strandi78 – 88Combined sources11
Beta strandi94 – 97Combined sources4
Beta strandi103 – 106Combined sources4
Helixi111 – 113Combined sources3
Helixi116 – 130Combined sources15
Beta strandi138 – 143Combined sources6
Helixi151 – 153Combined sources3
Helixi156 – 158Combined sources3
Helixi159 – 172Combined sources14
Helixi178 – 207Combined sources30
Beta strandi211 – 216Combined sources6
Beta strandi225 – 227Combined sources3
Beta strandi230 – 232Combined sources3
Helixi235 – 242Combined sources8
Helixi245 – 248Combined sources4
Beta strandi252 – 255Combined sources4
Beta strandi262 – 264Combined sources3
Helixi266 – 286Combined sources21
Beta strandi288 – 290Combined sources3
Beta strandi297 – 302Combined sources6
Beta strandi305 – 309Combined sources5
Helixi312 – 324Combined sources13
Beta strandi328 – 333Combined sources6
Helixi336 – 338Combined sources3
Beta strandi339 – 341Combined sources3
Helixi342 – 354Combined sources13
Helixi356 – 361Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FCQX-ray1.60A33-382[»]
1FCUX-ray2.10A33-382[»]
1FCVX-ray2.65A33-382[»]
2J88X-ray2.60A33-382[»]
ProteinModelPortaliQ08169.
SMRiQ08169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08169.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IECJ. Eukaryota.
ENOG410XPZT. LUCA.
KOiK01197.
PhylomeDBiQ08169.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q08169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP
60 70 80 90 100
TFMCHKYGLR FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN
110 120 130 140 150
GNVVARNGGV PQLGNLTKHL QVFRDHLINQ IPDKSFPGVG VIDFESWRPI
160 170 180 190 200
FRQNWASLQP YKKLSVEVVR REHPFWDDQR VEQEAKRRFE KYGQLFMEET
210 220 230 240 250
LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE NDKMSWLFES
260 270 280 290 300
EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY
310 320 330 340 350
KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE
360 370 380
YLNNELGPAV KRIALNNNAN DRLTVDVSVD QV
Length:382
Mass (Da):44,260
Last modified:October 1, 1994 - v1
Checksum:i3E6822E95CA11856
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37N → D AA sequence (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti371D → S in clone HYA-2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10710 mRNA. Translation: AAA27730.1.
PIRiA47477.
RefSeqiNP_001011619.1. NM_001011619.1.
UniGeneiAme.165.

Genome annotation databases

GeneIDi406146.
KEGGiame:406146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10710 mRNA. Translation: AAA27730.1.
PIRiA47477.
RefSeqiNP_001011619.1. NM_001011619.1.
UniGeneiAme.165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FCQX-ray1.60A33-382[»]
1FCUX-ray2.10A33-382[»]
1FCVX-ray2.65A33-382[»]
2J88X-ray2.60A33-382[»]
ProteinModelPortaliQ08169.
SMRiQ08169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7460.GB18543-PA.

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.
CAZyiGH56. Glycoside Hydrolase Family 56.

PTM databases

UniCarbKBiQ08169.

Proteomic databases

PaxDbiQ08169.
PRIDEiQ08169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi406146.
KEGGiame:406146.

Phylogenomic databases

eggNOGiENOG410IECJ. Eukaryota.
ENOG410XPZT. LUCA.
KOiK01197.
PhylomeDBiQ08169.

Enzyme and pathway databases

BRENDAi3.2.1.35. 387.

Miscellaneous databases

EvolutionaryTraceiQ08169.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHUGA_APIME
AccessioniPrimary (citable) accession number: Q08169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.