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P23613

- HYALP_CAVPO

UniProt

P23613 - HYALP_CAVPO

Protein

Hyaluronidase PH-20

Gene

SPAM1

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      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: UniProtKB-EC

    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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell adhesion

    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:PH-20, PH20
    OrganismiCavia porcellus (Guinea pig)
    Taxonomic identifieri10141 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
    ProteomesiUP000005447: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Add
    BLAST
    Chaini36 – 492457Hyaluronidase PH-20PRO_0000012087Add
    BLAST
    Propeptidei493 – 52937Removed in mature formSequence AnalysisPRO_0000012088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi59 ↔ 351By similarity
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi223 ↔ 237By similarity
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 387By similarity
    Disulfide bondi381 ↔ 435By similarity
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi437 ↔ 464By similarity
    Lipidationi492 – 4921GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Expressioni

    Tissue specificityi

    Testis.

    Interactioni

    Protein-protein interaction databases

    STRINGi10141.ENSCPOP00000001550.

    Structurei

    3D structure databases

    ProteinModelPortaliP23613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77606.
    GeneTreeiENSGT00550000074476.
    HOGENOMiHOG000015133.
    HOVERGENiHBG052053.
    InParanoidiP23613.
    OMAiQIDHYIS.
    OrthoDBiEOG74J97S.
    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.

    P23613-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAFTFKHSF FGSFVECSGV LQTVFIFLLI PCCLADKRAP PLIPNVPLLW    50
    VWNAPTEFCI GGTNQPLDMS FFSIVGTPRK NITGQSITLY YVDRLGYYPY 100
    IDPHTGAIVH GGLPQLMNLQ QHLRKSRQDI LFYMPTDSVG LAVIDWEEWR 150
    PTWTRNWRPK DIYRNKSIEL VKSQHPQYNH SYAVAVAKRD FERTGKAFML 200
    ETLKLGKSLR PSSLWGYYLF PDCYNTHFTK PNYDGHCPPI ELQRNNDLQW 250
    LWNDSTALYP SVYLTSRVRS SQNGALYVRN RVHESIRVSK LMDDKNPLPI 300
    YVYIRLVFTD QTTTFLELDD LVHSVGEIVP LGVSGIIIWG SLSLTRSLVS 350
    CIGLENYMKG TLLPYLINVT LAAKMCGQVL CKNQGICTRK DWNTNTYLHL 400
    NATNFDIELQ QNGKFVVHGK PSLEDLQEFS KNFHCSCYTN VACKDRLDVH 450
    NVRSVNVCTA NNICIDAVLN FPSLDDDDEP PITDDTSQNQ DSISDITSSA 500
    PPSSHILPKD LSWCLFLLSI FSQHWKYLL 529
    Length:529
    Mass (Da):60,365
    Last modified:November 1, 1991 - v1
    Checksum:iB3432356AED46245
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56332 mRNA. Translation: CAA39768.1.
    PIRiA36343.
    RefSeqiNP_001166492.1. NM_001173021.2.

    Genome annotation databases

    EnsembliENSCPOT00000001737; ENSCPOP00000001550; ENSCPOG00000001716.
    GeneIDi100135624.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56332 mRNA. Translation: CAA39768.1 .
    PIRi A36343.
    RefSeqi NP_001166492.1. NM_001173021.2.

    3D structure databases

    ProteinModelPortali P23613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10141.ENSCPOP00000001550.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCPOT00000001737 ; ENSCPOP00000001550 ; ENSCPOG00000001716 .
    GeneIDi 100135624.

    Organism-specific databases

    CTDi 6677.

    Phylogenomic databases

    eggNOGi NOG77606.
    GeneTreei ENSGT00550000074476.
    HOGENOMi HOG000015133.
    HOVERGENi HBG052053.
    InParanoidi P23613.
    OMAi QIDHYIS.
    OrthoDBi EOG74J97S.
    TreeFami TF321598.

    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. "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.

    Entry informationi

    Entry nameiHYALP_CAVPO
    AccessioniPrimary (citable) accession number: P23613
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3