Q08169 (HUGA_APIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hyaluronidase Short name=Hya EC=3.2.1.35 Alternative name(s): Allergen Api m II Hyaluronoglucosaminidase Allergen=Api m 2
Organism	Apis mellifera (Honeybee) [Reference proteome]
Taxonomic identifier	7460 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apinae › Apini › Apis

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides By similarity.
Catalytic activity	Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
Subunit structure	Homotetramer.
Subcellular location	Secreted.
Tissue specificity	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.
Post-translational modification	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. Ref.3 Ref.4
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the glycosyl hydrolase 56 family.

Ontologies

Keywords
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hyalurononglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Or 24 Potential

Propeptide

29 – 33

5

Potential

PRO_0000012105

Chain

34 – 382

349

Hyaluronidase

PRO_0000012106

Sites

Active site

145

1

Proton donor Probable

Amino acid modifications

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

263

1

N-linked (GlcNAc...) (complex) Ref.4

Disulfide bond

54 ↔ 345

Disulfide bond

221 ↔ 233

Natural variations

Natural variant

371

1

D → S in clone HYA-2.

Experimental info

Sequence conflict

37

1

N → D AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

382

Helix Strand Turn

Details...

Beta strand

44 – 49

6

Helix

51 – 57

7

Helix

63 – 66

4

Helix

74 – 76

3

Beta strand

78 – 88

11

Beta strand

94 – 97

4

Beta strand

103 – 106

4

Helix

111 – 113

3

Helix

116 – 130

15

Beta strand

138 – 143

6

Helix

151 – 153

3

Helix

156 – 158

3

Helix

159 – 172

14

Helix

178 – 207

30

Beta strand

211 – 216

6

Beta strand

225 – 227

3

Beta strand

230 – 232

3

Helix

235 – 242

8

Helix

245 – 248

4

Beta strand

252 – 255

4

Beta strand

262 – 264

3

Helix

266 – 286

21

Beta strand

288 – 290

3

Beta strand

297 – 302

6

Beta strand

305 – 309

5

Helix

312 – 324

13

Beta strand

328 – 333

6

Helix

336 – 338

3

Beta strand

339 – 341

3

Helix

342 – 354

13

Helix

356 – 361

6

Sequences

	Sequence		Length	Mass (Da)
	Q08169 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 3E6822E95CA11856	FASTA	382	44,260
	10 20 30 40 50 60 MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP TFMCHKYGLR 70 80 90 100 110 120 FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN GNVVARNGGV PQLGNLTKHL 130 140 150 160 170 180 QVFRDHLINQ IPDKSFPGVG VIDFESWRPI FRQNWASLQP YKKLSVEVVR REHPFWDDQR 190 200 210 220 230 240 VEQEAKRRFE KYGQLFMEET LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE 250 260 270 280 290 300 NDKMSWLFES EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY 310 320 330 340 350 360 KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE YLNNELGPAV 370 380 KRIALNNNAN DRLTVDVSVD QV

References

[1]	"Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm." Gmachl M., Kreil G. Proc. Natl. Acad. Sci. U.S.A. 90:3569-3573(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"The cross-reactivity between bee and vespid hyaluronidases has a structural basis." Jacobson R.S., Hoffman D.R., Kemeny D.M. J. Allergy Clin. Immunol. 89:292-292(1991) Cited for: PROTEIN SEQUENCE OF 34-64. Tissue: Venom.
[3]	"The asparagine-linked carbohydrate of honeybee venom hyaluronidase." Kubelka V., Altmann F., Marz L. Glycoconj. J. 12:77-83(1995) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[4]	"N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1." Kolarich D., Altmann F. Anal. Biochem. 285:64-75(2000) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-263.
[5]	"Crystal structure of hyaluronidase, a major allergen of bee venom." Markovic-Housley Z., Miglierini G., Soldatova L., Rizkallah P.J., Mueller U., Schirmer T. Structure 8:1025-1035(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 42-362, ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10710 mRNA. Translation: AAA27730.1.

PIR

A47477.

RefSeq

NP_001011619.1. NM_001011619.1.

UniGene

Ame.165.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FCQ	X-ray	1.60	A	33-382	[»]
1FCU	X-ray	2.10	A	33-382	[»]
1FCV	X-ray	2.65	A	33-382	[»]
2J88	X-ray	2.60	A	33-382	[»]

ProteinModelPortal

Q08169.

SMR

Q08169. Positions 42-365.

ModBase

Search...

Protein-protein interaction databases

STRING

7460.Q08169.

Protein family/group databases

Allergome

2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.

CAZy

GH56. Glycoside Hydrolase Family 56.

PTM databases

GlycoSuiteDB

Q08169.

Proteomic databases

PaxDb

Q08169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

406146.

KEGG

ame:406146.

Phylogenomic databases

eggNOG

NOG77606.

InParanoid

Q08169.

KO

K01197.

PhylomeDB

Q08169.

Enzyme and pathway databases

BRENDA

3.2.1.35. 387.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR001329. Glyco_hydro_56_Api/Dol.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]

PANTHER

PTHR11769. PTHR11769. 1 hit.
PTHR11769:SF2. PTHR11769:SF2. 1 hit.

Pfam

PF01630. Glyco_hydro_56. 1 hit.
[Graphical view]

PRINTS

PR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q08169.

Entry information

Entry name

HUGA_APIME

Accession

Primary (citable) accession number: Q08169

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)