Reviewed, UniProtKB/Swiss-Prot P48794 (HYALP_MOUSE)

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 surface protein PH-20
    Sperm adhesion molecule 1

Gene names

Name:	Spam1
Synonyms:	Ph20, Spam

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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
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
Cellular component	acrosomal vesicle Inferred from direct assay. Source: MGI anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW external side of plasma membrane Inferred from direct assay. Source: MGI
Molecular function	hyalurononglucosaminidase activity Ref.2 Inferred from direct assay. Source: MGI protein binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	By similarity
	Chain	36 – ?		Hyaluronidase PH-20		PRO_0000012093
	Propeptide	? – 512		Removed in mature form Potential		PRO_0000012094
Sites
	Active site	147	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	46	1	N-linked (GlcNAc...) Potential
	Glycosylation	165	1	N-linked (GlcNAc...) Potential
	Glycosylation	293	1	N-linked (GlcNAc...) Potential
	Glycosylation	368	1	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	1	E → R in AAA76603. Ref.1
	Sequence conflict	191	1	F → L in AAA76603. Ref.1
	Sequence conflict	271	1	N → H in BAC55070. Ref.2
	Sequence conflict	495	1	H → R in BAB24161. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P48794-1 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: 6502F9FC75E7C86F	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

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: 12065596] [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. , 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: 16141072] [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: 7794889] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. NP_033267.2.
UniGene	Mm.4688
3D structure databases
HSSP	HSSP built from PDB template 1FCQ based on UniProtKB Q08169.
ModBase	Search...
Protein family/group databases
CAZy	GH56. Glycoside Hydrolase Family 56.
Genome annotation databases
Ensembl	ENSMUSG00000029682. Mus musculus. [Contig view]
GeneID	20690.
KEGG	mmu:20690.
Organism-specific databases
MGI	MGI:109335. Spam1.
Phylogenomic databases
HOGENOM	P48794.
HOVERGEN	P48794.
OMA	P48794. LEYFSEH.
Enzyme and pathway databases
BRENDA	3.2.1.35. 244.
Gene expression databases
ArrayExpress	P48794.
Bgee	P48794.
CleanEx	MM_SPAM1.
GermOnline	ENSMUSG00000029682. Mus musculus.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR017430. Glyco_hydro_56_Hyaluronidase. IPR001439. Glyco_hydro_56_PH20. IPR001968. Glycoside_hydrolase_family_56. IPR018155. Hyaluronidase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11769. Glyco_hydro_56. 1 hit. PTHR11769:SF4. Glyco_hydro_56_PH20. 1 hit.
Pfam	PF01630. Glyco_hydro_56. 1 hit. [Graphical view]
PIRSF	PIRSF038193. Hyaluronidase. 1 hit.
PRINTS	PR00846. GLHYDRLASE56. PR00848. SPERMPH20.
ProDom	PD003549. Glyco_hydro_56. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)