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P48794

- HYALP_MOUSE

UniProt

P48794 - HYALP_MOUSE

Protein

Hyaluronidase PH-20

Gene

Spam1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (24 May 2004)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei147 – 1471Proton donorBy similarity

    GO - Molecular functioni

    1. hyalurononglucosaminidase activity Source: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell adhesion Source: UniProtKB-KW
    3. fusion of sperm to egg plasma membrane Source: InterPro
    4. single fertilization Source: MGI

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196631. Interaction With Cumulus Cells.

    Protein family/group databases

    CAZyiGH56. Glycoside Hydrolase Family 56.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronidase PH-20 (EC:3.2.1.35)
    Short name:
    Hyal-PH20
    Alternative name(s):
    Hyaluronoglucosaminidase PH-20
    Sperm adhesion molecule 1
    Sperm surface protein PH-20
    Gene namesi
    Name:Spam1
    Synonyms:Ph20, Spam
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:109335. Spam1.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: MGI
    2. anchored component of membrane Source: UniProtKB-KW
    3. external side of plasma membrane Source: MGI
    4. membrane raft Source: MGI
    5. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 512Removed in mature formSequence AnalysisPRO_0000012094
    Signal peptidei1 – 3535By similarityAdd
    BLAST
    Chaini36 – ?Hyaluronidase PH-20PRO_0000012093

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi60 ↔ 351By similarity
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi223 ↔ 237By similarity
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 387By similarity
    Disulfide bondi381 ↔ 435By similarity
    Disulfide bondi437 ↔ 464By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PRIDEiP48794.

    Expressioni

    Gene expression databases

    BgeeiP48794.
    CleanExiMM_SPAM1.
    GenevestigatoriP48794.

    Interactioni

    Protein-protein interaction databases

    BioGridi203421. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP48794.
    SMRiP48794. Positions 53-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77606.
    GeneTreeiENSGT00550000074476.
    HOGENOMiHOG000015133.
    HOVERGENiHBG052053.
    InParanoidiP48794.
    KOiK01197.
    OMAiWDAMSLA.
    OrthoDBiEOG74J97S.
    PhylomeDBiP48794.
    TreeFamiTF321598.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    IPR001439. Hyaluronidase_PH20.
    [Graphical view]
    PANTHERiPTHR11769. PTHR11769. 1 hit.
    PfamiPF01630. Glyco_hydro_56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
    PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
    PRINTSiPR00846. GLHYDRLASE56.
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P48794-1 [UniParc]FASTAAdd to Basket

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    MGELRFKHLF WGSFVESGGT FQTVLIFLLI PCSLTVDYRA APILSNTTFL    50
    WIWNVPTERC VGNVNDPIDL SFFSLIGSPR KTATGQPVTL FYVDRLGLYP 100
    HIDANQAEHY GGIPQRGDYQ AHLRKAKTDI EHYIPDDKLG LAIIDWEEWR 150
    PTWLRNWKPK DNYRNKSIEL VQSTNPGLSI TEATQKAIQQ FEEAGRKFME 200
    GTLHLGKFLR PNQLWGYYLF PDCYNNKFQD PKYDGQCPAV EKKRNDNLKW 250
    LWKASTGLYP SVYLKKDLKS NRQATLYVRY RVVEAIRVSK VGNASDPVPI 300
    FVYIRLVFTD RTSEYLLEDD LVNTIGEIVA LGTSGIIIWD AMSLAQRAAG 350
    CPILHKYMQT TLNPYIVNVT LAAKMCSQTL CNEKGMCSRR KESSDVYLHL 400
    NPSHFDIMLT ETGKYEVLGN PRVGDLEYFS EHFKCSCFSR MTCKETSDVK 450
    NVQDVNVCVG DNVCIKAKVE PNPAFYLLPG KSLLFMTTLG HVLYHLPQDI 500
    FVFPRKTLVS TP 512
    Length:512
    Mass (Da):58,498
    Last modified:May 24, 2004 - v2
    Checksum:i6502F9FC75E7C86F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1821E → R in AAA76603. 1 PublicationCurated
    Sequence conflicti191 – 1911F → L in AAA76603. 1 PublicationCurated
    Sequence conflicti271 – 2711N → H in BAC55070. (PubMed:12065596)Curated
    Sequence conflicti495 – 4951H → R in BAB24161. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33958 mRNA. Translation: AAA76603.1.
    AB085677 Genomic DNA. Translation: BAC55070.1.
    AY228460 mRNA. Translation: AAP49832.1.
    AK005638 mRNA. Translation: BAB24161.1.
    CCDSiCCDS19947.1.
    RefSeqiNP_001073344.1. NM_001079875.2.
    NP_033267.2. NM_009241.3.
    XP_006505088.1. XM_006505025.1.
    UniGeneiMm.4688.

    Genome annotation databases

    EnsembliENSMUST00000031693; ENSMUSP00000031693; ENSMUSG00000029682.
    GeneIDi20690.
    KEGGimmu:20690.
    UCSCiuc009bby.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33958 mRNA. Translation: AAA76603.1 .
    AB085677 Genomic DNA. Translation: BAC55070.1 .
    AY228460 mRNA. Translation: AAP49832.1 .
    AK005638 mRNA. Translation: BAB24161.1 .
    CCDSi CCDS19947.1.
    RefSeqi NP_001073344.1. NM_001079875.2.
    NP_033267.2. NM_009241.3.
    XP_006505088.1. XM_006505025.1.
    UniGenei Mm.4688.

    3D structure databases

    ProteinModelPortali P48794.
    SMRi P48794. Positions 53-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203421. 1 interaction.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    Proteomic databases

    PRIDEi P48794.

    Protocols and materials databases

    DNASUi 20690.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031693 ; ENSMUSP00000031693 ; ENSMUSG00000029682 .
    GeneIDi 20690.
    KEGGi mmu:20690.
    UCSCi uc009bby.1. mouse.

    Organism-specific databases

    CTDi 6677.
    MGIi MGI:109335. Spam1.

    Phylogenomic databases

    eggNOGi NOG77606.
    GeneTreei ENSGT00550000074476.
    HOGENOMi HOG000015133.
    HOVERGENi HBG052053.
    InParanoidi P48794.
    KOi K01197.
    OMAi WDAMSLA.
    OrthoDBi EOG74J97S.
    PhylomeDBi P48794.
    TreeFami TF321598.

    Enzyme and pathway databases

    Reactomei REACT_196631. Interaction With Cumulus Cells.

    Miscellaneous databases

    NextBioi 299225.
    PROi P48794.
    SOURCEi Search...

    Gene expression databases

    Bgeei P48794.
    CleanExi MM_SPAM1.
    Genevestigatori P48794.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    IPR001439. Hyaluronidase_PH20.
    [Graphical view ]
    PANTHERi PTHR11769. PTHR11769. 1 hit.
    Pfami PF01630. Glyco_hydro_56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
    PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
    PRINTSi PR00846. GLHYDRLASE56.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiHYALP_MOUSE
    AccessioniPrimary (citable) accession number: P48794
    Secondary accession number(s): Q7TSD6, Q812F4, Q9DAQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3