Hyaluronidase PH-20 precursor - Mus musculus (Mouse)

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P48794 (HYALP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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, Spam

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	512 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	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.
Sequence similarities	Belongs to the glycosyl hydrolase 56 family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW fusion of sperm to egg plasma membrane Inferred from electronic annotation. Source: InterPro single fertilization Inferred from mutant phenotype Ref.2. Source: MGI
Cellular_component	acrosomal vesicle Inferred from direct assay PubMed 16330764. Source: MGI anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW external side of plasma membrane Inferred from direct assay PubMed 16925524. Source: MGI membrane raft Inferred from direct assay PubMed 19144954. Source: MGI
Molecular_function	hyalurononglucosaminidase activity Inferred from direct assay PubMed 16330764 PubMed 16925524. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 35

By similarity

Chain

36 – ?

Hyaluronidase PH-20

PRO_0000012093

Propeptide

? – 512

Removed in mature form Potential

PRO_0000012094

Sites

Active site

147

Proton donor By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

165

N-linked (GlcNAc...) Potential

Glycosylation

293

N-linked (GlcNAc...) Potential

Glycosylation

368

N-linked (GlcNAc...) Potential

Disulfide bond

60 ↔ 351

By similarity

Disulfide bond

223 ↔ 237

By similarity

Disulfide bond

376 ↔ 387

By similarity

Disulfide bond

381 ↔ 435

By similarity

Disulfide bond

437 ↔ 464

By similarity

Experimental info

Sequence conflict

182

E → R in AAA76603. Ref.1

Sequence conflict

191

F → L in AAA76603. Ref.1

Sequence conflict

271

N → H in BAC55070. Ref.2

Sequence conflict

495

H → R in BAB24161. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P48794 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: 6502F9FC75E7C86F
Show »

FASTA

512

58,498

        10         20         30         40         50         60 
MGELRFKHLF WGSFVESGGT FQTVLIFLLI PCSLTVDYRA APILSNTTFL WIWNVPTERC 

        70         80         90        100        110        120 
VGNVNDPIDL SFFSLIGSPR KTATGQPVTL FYVDRLGLYP HIDANQAEHY GGIPQRGDYQ 

       130        140        150        160        170        180 
AHLRKAKTDI EHYIPDDKLG LAIIDWEEWR PTWLRNWKPK DNYRNKSIEL VQSTNPGLSI 

       190        200        210        220        230        240 
TEATQKAIQQ FEEAGRKFME GTLHLGKFLR PNQLWGYYLF PDCYNNKFQD PKYDGQCPAV 

       250        260        270        280        290        300 
EKKRNDNLKW LWKASTGLYP SVYLKKDLKS NRQATLYVRY RVVEAIRVSK VGNASDPVPI 

       310        320        330        340        350        360 
FVYIRLVFTD RTSEYLLEDD LVNTIGEIVA LGTSGIIIWD AMSLAQRAAG CPILHKYMQT 

       370        380        390        400        410        420 
TLNPYIVNVT LAAKMCSQTL CNEKGMCSRR KESSDVYLHL NPSHFDIMLT ETGKYEVLGN 

       430        440        450        460        470        480 
PRVGDLEYFS EHFKCSCFSR MTCKETSDVK NVQDVNVCVG DNVCIKAKVE PNPAFYLLPG 

       490        500        510 
KSLLFMTTLG HVLYHLPQDI FVFPRKTLVS TP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Ramarao C.S., Primakoff P. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Sperm.
[2]	"Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg." Baba D., Kashiwabara S., Honda A., Yamagata K., Wu Q., Ikawa M., Okabe M., Baba T. J. Biol. Chem. 277:30310-30314(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ. Tissue: Testis.
[3]	"Assessment of contraceptive vaccines based on mouse sperm protein PH-20 (SPAM-1)." Hardy C.M., Mobbs K.J. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BALB/c. Tissue: Testis.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[5]	"Biochemical characterization of a glycosylphosphatidylinositol-linked hyaluronidase on mouse sperm." Thaler C.D., Cardullo R.A. Biochemistry 34:7788-7795(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33958 mRNA. Translation: AAA76603.1. AB085677 Genomic DNA. Translation: BAC55070.1. AY228460 mRNA. Translation: AAP49832.1. AK005638 mRNA. Translation: BAB24161.1.
IPI	IPI00114402.
RefSeq	NP_001073344.1. NM_001079875.1. NP_033267.2. NM_009241.2.
UniGene	Mm.4688.
3D structure databases
ProteinModelPortal	P48794.
SMR	P48794. Positions 53-366.
ModBase	Search...
Protein family/group databases
CAZy	GH56. Glycoside Hydrolase Family 56.
Proteomic databases
PRIDE	P48794.
Protocols and materials databases
DNASU	20690.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031693; ENSMUSP00000031693; ENSMUSG00000029682.
GeneID	20690.
KEGG	mmu:20690.
UCSC	uc009bby.1. mouse.
Organism-specific databases
CTD	6677.
MGI	MGI:109335. Spam1.
Phylogenomic databases
eggNOG	NOG77606.
GeneTree	ENSGT00550000074476.
HOGENOM	HOG000015133.
HOVERGEN	HBG052053.
InParanoid	P48794.
KO	K01197.
OMA	WDAMSLA.
OrthoDB	EOG4QNMWH.
Gene expression databases
Bgee	P48794.
CleanEx	MM_SPAM1.
Genevestigator	P48794.
GermOnline	ENSMUSG00000029682. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR017853. Glycoside_hydrolase_SF. IPR018155. Hyaluronidase. IPR001439. Hyaluronidase_PH20. [Graphical view]
PANTHER	PTHR11769. PTHR11769. 1 hit. PTHR11769:SF4. PTHR11769:SF4. 1 hit.
Pfam	PF01630. Glyco_hydro_56. 1 hit. [Graphical view]
PIRSF	PIRSF038193. Hyaluronidase. 1 hit. PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTS	PR00846. GLHYDRLASE56.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	299225.
SOURCE	Search...

Entry information

Entry name

HYALP_MOUSE

Accession

Primary (citable) accession number: P48794
Secondary accession number(s): Q7TSD6, Q812F4, Q9DAQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	May 24, 2004
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents