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P48794 (HYALP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, Spam
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length512 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-anchorGPI-anchor.

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_0000012093
Propeptide? – 512Removed in mature form PotentialPRO_0000012094

Sites

Active site1471Proton donor By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 351 By similarity
Disulfide bond223 ↔ 237 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 435 By similarity
Disulfide bond437 ↔ 464 By similarity

Experimental info

Sequence conflict1821E → R in AAA76603. Ref.1
Sequence conflict1911F → L in AAA76603. Ref.1
Sequence conflict2711N → H in BAC55070. Ref.2
Sequence conflict4951H → R in BAB24161. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P48794 [UniParc].

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

FASTA51258,498
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
CCDSCCDS19947.1.
RefSeqNP_001073344.1. NM_001079875.2.
NP_033267.2. NM_009241.3.
XP_006505088.1. XM_006505025.1.
UniGeneMm.4688.

3D structure databases

ProteinModelPortalP48794.
SMRP48794. Positions 53-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203421. 1 interaction.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PRIDEP48794.

Protocols and materials databases

DNASU20690.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031693; ENSMUSP00000031693; ENSMUSG00000029682.
GeneID20690.
KEGGmmu:20690.
UCSCuc009bby.1. mouse.

Organism-specific databases

CTD6677.
MGIMGI:109335. Spam1.

Phylogenomic databases

eggNOGNOG77606.
GeneTreeENSGT00550000074476.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidP48794.
KOK01197.
OMAWDAMSLA.
OrthoDBEOG74J97S.
PhylomeDBP48794.
TreeFamTF321598.

Gene expression databases

BgeeP48794.
CleanExMM_SPAM1.
GenevestigatorP48794.

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...

Other

NextBio299225.
PROP48794.
SOURCESearch...

Entry information

Entry nameHYALP_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 122 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

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries