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P38566 (HYALP_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase PH-20

Short name=Hyal-PH20
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase PH-20
Sperm adhesion molecule 1
Sperm surface protein PH-20
Gene names
Name:SPAM1
Synonyms:PH20
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Testis.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 By similarity
Chain36 – ?Hyaluronidase PH-20PRO_0000012095
Propeptide? – 545Removed in mature form PotentialPRO_0000012096

Sites

Active site1481Proton donor By similarity

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 355 By similarity
Disulfide bond224 ↔ 239 By similarity
Disulfide bond380 ↔ 391 By similarity
Disulfide bond385 ↔ 439 By similarity
Disulfide bond441 ↔ 468 By similarity

Sequences

Sequence LengthMass (Da)Tools
P38566 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 125AF314FE05AEB4

FASTA54562,412
        10         20         30         40         50         60 
MGVLKFKHIF FGSAVELSGV FQIVFIFLLI PCCLTANFRA PPVIPNVPFL WAWNAPTEFC 

        70         80         90        100        110        120 
LGKSGEPLDM SLFSLFGSPR KNKTGQGITI FYVDRLGYYP YIDPHTGAIV HGRIPQLGPL 

       130        140        150        160        170        180 
QQHLTKLRQE ILYYMPKDNV GLAVIDWEEW LPTWLRNWKP KDIYRIKSIE LVKSQHPQYN 

       190        200        210        220        230        240 
HSYATEKAKR DFEKAGKDFM EETLKLGRLL RPNHLWGYYL FPDCYNHHYD KPNLYKGSCF 

       250        260        270        280        290        300 
DIEKKRNDDL SWLWKESTAL FPSVYLTSRA RSATALSKLY VVRNRVHEAI RVSKIPDDKS 

       310        320        330        340        350        360 
PLPNFVYTRL VFTDQIFQFL SHHDLVYTIG EIVALGASGI VVWGSQSLAR SMKSCLHLDN 

       370        380        390        400        410        420 
YMKTILNPYL INVTLAAKMC NQVLCQEQGV CTRKNWNPND YLHLNPGNFA IQLGSNGTYK 

       430        440        450        460        470        480 
VDGKPTLTDL EQFSKNFQCS CYTNLNCKER TDMNNVRTVN VCAVENVCID TNVGPQAVTY 

       490        500        510        520        530        540 
APKEKKDVAH ILSNTTSINS STTMSLPFPR KHVSGCLLVL CMYSQYLNIC YRLVAIGIQH 


GYYLK 

« Hide

References

[1]"The nucleic acid sequence of rabbit PH-20 cDNA."
Andrews J.B., Holland M.K.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09183 mRNA. Translation: AAA88913.1.
RefSeqNP_001076141.1. NM_001082672.1.
UniGeneOcu.2048.

3D structure databases

ProteinModelPortalP38566.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009391.

Organism-specific databases

CTD6677.

Phylogenomic databases

HOVERGENHBG052053.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001439. Hyaluronidase_PH20.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYALP_RABIT
AccessionPrimary (citable) accession number: P38566
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries