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Protein

Hyaluronidase-1

Gene
N/A
Organism
Mesobuthus martensii (Manchurian scorpion) (Buthus martensii)
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. In venom, it may participate in the degradation of the extracellular matrix thus allowing a rapid spread of other venom components during the envenomation process.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by heparin, and to a lesser extent by DTT, Fe3+ and Cu2+. Not inhibited by reduced glutathione, L-cysteine, EDTA, Ca2+ or Mg2+.1 Publication

pH dependencei

Optimum pH is 4.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Activity decreases when incubated at temperatures above 24 degrees Celsius for 10 minutes. No activity remains after 10 minutes at 65 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei130 – 1301Proton donorBy similarity

GO - Molecular functioni

  1. hyalurononglucosaminidase activity Source: UniProtKB

GO - Biological processi

  1. pathogenesis Source: UniProtKB
  2. polysaccharide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase-11 Publication (EC:3.2.1.35)
Short name:
BmHYA1
Short name:
HYA11 Publication
Alternative name(s):
Hyaluronoglucosaminidase-1
Venom spreading factor
OrganismiMesobuthus martensii (Manchurian scorpion) (Buthus martensii)
Taxonomic identifieri34649 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeMesobuthus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 410385Hyaluronidase-1PRO_0000355081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 331PROSITE-ProRule annotation
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi199 ↔ 242PROSITE-ProRule annotation
Disulfide bondi206 ↔ 220PROSITE-ProRule annotation
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi356 ↔ 367PROSITE-ProRule annotation
Disulfide bondi361 ↔ 395PROSITE-ProRule annotation
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi397 ↔ 406PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini352 – 40756EGF-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.1 Publication
Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
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.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P86100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQNIQMTEM YQIILFASIL AAISATSADF KVVWEVPSIM CSKKFKINVT
60 70 80 90 100
DLLTSHKILV NQEETFNGDK IVIFYESQLG KYPHIESHGD INGGMLQVSD
110 120 130 140 150
LANHLKIARD NISKFIPDPN FNGVGIIDWE AWRPLWKYNW GRMSEYRDRS
160 170 180 190 200
KDLVKAKHPD WSPAQIEKVA IEEWENSAKE WMLKTLKLVE DMRPNAAWCY
210 220 230 240 250
YLFPDCYNYG GKDQPSEYFC KNDIQEANDK LSWLWKQSTA LCPSIYMQES
260 270 280 290 300
HITKYNTSQR AWWIYARLRE TIRLSHPNTL IYPYINYILP GTKKTVPSMD
310 320 330 340 350
FKRVLGQIGS LGLDGAIIWG SSYHVNTEEM CKEMKTYVKD VIAPVASTVI
360 370 380 390 400
QNVNRCSQQI CKGRGNCVWP EEPYTSWKYL IDPKNPTFKH TNISCKCKGG
410
YTGRYCQIAP
Length:410
Mass (Da):47,433
Last modified:March 19, 2014 - v2
Checksum:i4472C474E9E4DF56
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481N → C AA sequence (PubMed:18611448).Curated
Sequence conflicti102 – 1021A → T no nucleotide entry (PubMed:20417653).Curated
Sequence conflicti132 – 1321W → G no nucleotide entry (PubMed:20417653).Curated
Sequence conflicti135 – 1351L → F no nucleotide entry (PubMed:20417653).Curated
Sequence conflicti189 – 1891V → A in ACY69673 (PubMed:20417653).Curated
Sequence conflicti235 – 2351W → G no nucleotide entry (PubMed:20417653).Curated
Sequence conflicti329 – 3291E → G in ACY69673 (PubMed:20417653).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF588514 mRNA. Translation: AHA36327.1.
GU130249 mRNA. Translation: ACY69673.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF588514 mRNA. Translation: AHA36327.1.
GU130249 mRNA. Translation: ACY69673.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
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.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and molecular characterization of scorpion Buthus martensi venom hyaluronidases: a novel full-length and diversiform no-code stop sequences."
    Xue S., Zhao Y., Ma Y., Gui G., Huang C.
    Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion Buthus martensi Karsch."
    Feng L., Gao R., Meng J., Gopalakrishnakone P.
    Toxicon 56:474-479(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-410.
  3. "Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi."
    Feng L., Gao R., Gopalakrishnakone P.
    Comp. Biochem. Physiol. 148C:250-257(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-55, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom1 Publication.

Entry informationi

Entry nameiHYAL1_MESMA
AccessioniPrimary (citable) accession number: P86100
Secondary accession number(s): D1MBU1, U6BKM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: March 19, 2014
Last modified: October 1, 2014
This is version 8 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.