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P23613 (HYALP_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PH-20, PH20
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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-anchor › GPI-anchor.

Tissue specificity

Testis.

Post-translational modification

Endoproteolysis (toward the C-terminus producing two disulfide-linked fragments) could activate PH-20.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535
Chain36 – 492457Hyaluronidase PH-20
PRO_0000012087
Propeptide493 – 52937Removed in mature form Potential
PRO_0000012088

Sites

Active site1471Proton donor By similarity

Amino acid modifications

Lipidation4921GPI-anchor amidated serine Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 351 By similarity
Disulfide bond223 ↔ 237 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 435 By similarity
Disulfide bond437 ↔ 464 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23613 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: B3432356AED46245

FASTA52960,365
        10         20         30         40         50         60 
MGAFTFKHSF FGSFVECSGV LQTVFIFLLI PCCLADKRAP PLIPNVPLLW VWNAPTEFCI 

        70         80         90        100        110        120 
GGTNQPLDMS FFSIVGTPRK NITGQSITLY YVDRLGYYPY IDPHTGAIVH GGLPQLMNLQ 

       130        140        150        160        170        180 
QHLRKSRQDI LFYMPTDSVG LAVIDWEEWR PTWTRNWRPK DIYRNKSIEL VKSQHPQYNH 

       190        200        210        220        230        240 
SYAVAVAKRD FERTGKAFML ETLKLGKSLR PSSLWGYYLF PDCYNTHFTK PNYDGHCPPI 

       250        260        270        280        290        300 
ELQRNNDLQW LWNDSTALYP SVYLTSRVRS SQNGALYVRN RVHESIRVSK LMDDKNPLPI 

       310        320        330        340        350        360 
YVYIRLVFTD QTTTFLELDD LVHSVGEIVP LGVSGIIIWG SLSLTRSLVS CIGLENYMKG 

       370        380        390        400        410        420 
TLLPYLINVT LAAKMCGQVL CKNQGICTRK DWNTNTYLHL NATNFDIELQ QNGKFVVHGK 

       430        440        450        460        470        480 
PSLEDLQEFS KNFHCSCYTN VACKDRLDVH NVRSVNVCTA NNICIDAVLN FPSLDDDDEP 

       490        500        510        520 
PITDDTSQNQ DSISDITSSA PPSSHILPKD LSWCLFLLSI FSQHWKYLL

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References

[1]"cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals."
Lathrop W.F., Carmichael E.P., Myles D.G., Primakoff P.
J. Cell Biol. 111:2939-2949(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Hartley.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56332 mRNA. Translation: CAA39768.1.
PIRA36343.
RefSeqNP_001166492.1. NM_001173021.2.

3D structure databases

ProteinModelPortalP23613.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000001550.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000001737; ENSCPOP00000001550; ENSCPOG00000001716.
GeneID100135624.

Organism-specific databases

CTD6677.

Phylogenomic databases

eggNOGNOG77606.
GeneTreeENSGT00550000074476.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidP23613.
OMALWLWERS.
OrthoDBEOG4QNMWH.

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.
PTHR11769:SF4. PTHR11769:SF4. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYALP_CAVPO
AccessionPrimary (citable) accession number: P23613
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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