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P38567

- HYALP_HUMAN

UniProt

P38567 - HYALP_HUMAN

Protein

Hyaluronidase PH-20

Gene

SPAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      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.1 Publication

    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 sitei148 – 1481Proton donorBy similarity

    GO - Molecular functioni

    1. hyalurononglucosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. binding of sperm to zona pellucida Source: ProtInc
    2. carbohydrate metabolic process Source: ProtInc
    3. cell adhesion Source: UniProtKB-KW
    4. fusion of sperm to egg plasma membrane Source: InterPro
    5. multicellular organism reproduction Source: Reactome
    6. single fertilization Source: Reactome
    7. sperm-egg recognition Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02884-MONOMER.
    ReactomeiREACT_163796. 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:HYAL3, PH20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:11217. SPAM1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi146 – 1461D → N: Reduces activity by 80%. 1 Publication
    Mutagenesisi148 – 1481E → Q: Loss of activity. 1 Publication
    Mutagenesisi211 – 2111R → G: Reduces activity by over 90%. 1 Publication
    Mutagenesisi284 – 2841E → Q: Loss of activity. 1 Publication
    Mutagenesisi287 – 2871R → T: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36053.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535By similarityAdd
    BLAST
    Chaini36 – 490455Hyaluronidase PH-20PRO_0000012089Add
    BLAST
    Propeptidei491 – 50919Removed in mature formSequence AnalysisPRO_0000012090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi60 ↔ 351By similarity
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi224 ↔ 238By similarity
    Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 387By similarity
    Disulfide bondi381 ↔ 435By similarity
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi437 ↔ 464By similarity
    Lipidationi490 – 4901GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP38567.
    PRIDEiP38567.

    PTM databases

    PhosphoSiteiP38567.

    Expressioni

    Tissue specificityi

    Testis.1 Publication

    Gene expression databases

    ArrayExpressiP38567.
    BgeeiP38567.
    CleanExiHS_HYAL3.
    HS_SPAM1.
    GenevestigatoriP38567.

    Organism-specific databases

    HPAiHPA017984.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000345849.

    Structurei

    3D structure databases

    ProteinModelPortaliP38567.
    SMRiP38567. Positions 53-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77606.
    HOGENOMiHOG000015133.
    HOVERGENiHBG052053.
    KOiK01197.
    OMAiHLNPDNF.
    PhylomeDBiP38567.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P38567-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPVIPNVPFL    50
    WAWNAPSEFC LGKFDEPLDM SLFSFIGSPR INATGQGVTI FYVDRLGYYP 100
    YIDSITGVTV NGGIPQKISL QDHLDKAKKD ITFYMPVDNL GMAVIDWEEW 150
    RPTWARNWKP KDVYKNRSIE LVQQQNVQLS LTEATEKAKQ EFEKAGKDFL 200
    VETIKLGKLL RPNHLWGYYL FPDCYNHHYK KPGYNGSCFN VEIKRNDDLS 250
    WLWNESTALY PSIYLNTQQS PVAATLYVRN RVREAIRVSK IPDAKSPLPV 300
    FAYTRIVFTD QVLKFLSQDE LVYTFGETVA LGASGIVIWG TLSIMRSMKS 350
    CLLLDNYMET ILNPYIINVT LAAKMCSQVL CQEQGVCIRK NWNSSDYLHL 400
    NPDNFAIQLE KGGKFTVRGK PTLEDLEQFS EKFYCSCYST LSCKEKADVK 450
    DTDAVDVCIA DGVCIDAFLK PPMETEEPQI FYNASPSTLS ATMFIVSILF 500
    LIISSVASL 509
    Length:509
    Mass (Da):57,848
    Last modified:October 1, 1994 - v1
    Checksum:i5ADB4739747E32E8
    GO
    Isoform 2 (identifier: P38567-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         496-509: VSILFLIISSVASL → WRLEVWDQGISRIGFF

    Note: No experimental confirmation available.

    Show »
    Length:511
    Mass (Da):58,395
    Checksum:i8620113DE58741C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481P → A in AAC60607. (PubMed:8282124)Curated
    Sequence conflicti499 – 4991L → W in AAC60607. (PubMed:8282124)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51K → Q Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064756
    Natural varianti47 – 471V → A.
    Corresponds to variant rs34633019 [ dbSNP | Ensembl ].
    VAR_049213

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei496 – 50914VSILF…SVASL → WRLEVWDQGISRIGFF in isoform 2. 1 PublicationVSP_042714Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13781 mRNA. No translation available.
    S67798 mRNA. Translation: AAC60607.2.
    X84347 mRNA. Translation: CAA59086.1.
    AC004690 Genomic DNA. Translation: AAQ96882.1.
    CH236947 Genomic DNA. Translation: EAL24329.1.
    CH471070 Genomic DNA. Translation: EAW83606.1.
    BC026163 mRNA. Translation: AAH26163.1.
    CCDSiCCDS5790.1. [P38567-2]
    CCDS5791.1. [P38567-1]
    PIRiS40465.
    RefSeqiNP_001167515.1. NM_001174044.1. [P38567-1]
    NP_001167516.1. NM_001174045.1. [P38567-1]
    NP_001167517.1. NM_001174046.1. [P38567-1]
    NP_003108.2. NM_003117.4. [P38567-2]
    NP_694859.1. NM_153189.2. [P38567-1]
    UniGeneiHs.121494.

    Genome annotation databases

    EnsembliENST00000223028; ENSP00000223028; ENSG00000106304. [P38567-1]
    ENST00000340011; ENSP00000345849; ENSG00000106304. [P38567-2]
    ENST00000402183; ENSP00000386028; ENSG00000106304. [P38567-1]
    ENST00000439500; ENSP00000402123; ENSG00000106304. [P38567-1]
    ENST00000460182; ENSP00000417934; ENSG00000106304. [P38567-1]
    GeneIDi6677.
    KEGGihsa:6677.
    UCSCiuc003vld.3. human. [P38567-1]
    uc003vle.3. human. [P38567-2]

    Polymorphism databases

    DMDMi585673.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13781 mRNA. No translation available.
    S67798 mRNA. Translation: AAC60607.2 .
    X84347 mRNA. Translation: CAA59086.1 .
    AC004690 Genomic DNA. Translation: AAQ96882.1 .
    CH236947 Genomic DNA. Translation: EAL24329.1 .
    CH471070 Genomic DNA. Translation: EAW83606.1 .
    BC026163 mRNA. Translation: AAH26163.1 .
    CCDSi CCDS5790.1. [P38567-2 ]
    CCDS5791.1. [P38567-1 ]
    PIRi S40465.
    RefSeqi NP_001167515.1. NM_001174044.1. [P38567-1 ]
    NP_001167516.1. NM_001174045.1. [P38567-1 ]
    NP_001167517.1. NM_001174046.1. [P38567-1 ]
    NP_003108.2. NM_003117.4. [P38567-2 ]
    NP_694859.1. NM_153189.2. [P38567-1 ]
    UniGenei Hs.121494.

    3D structure databases

    ProteinModelPortali P38567.
    SMRi P38567. Positions 53-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000345849.

    Chemistry

    DrugBanki DB00070. Hyaluronidase.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    PTM databases

    PhosphoSitei P38567.

    Polymorphism databases

    DMDMi 585673.

    Proteomic databases

    PaxDbi P38567.
    PRIDEi P38567.

    Protocols and materials databases

    DNASUi 6677.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223028 ; ENSP00000223028 ; ENSG00000106304 . [P38567-1 ]
    ENST00000340011 ; ENSP00000345849 ; ENSG00000106304 . [P38567-2 ]
    ENST00000402183 ; ENSP00000386028 ; ENSG00000106304 . [P38567-1 ]
    ENST00000439500 ; ENSP00000402123 ; ENSG00000106304 . [P38567-1 ]
    ENST00000460182 ; ENSP00000417934 ; ENSG00000106304 . [P38567-1 ]
    GeneIDi 6677.
    KEGGi hsa:6677.
    UCSCi uc003vld.3. human. [P38567-1 ]
    uc003vle.3. human. [P38567-2 ]

    Organism-specific databases

    CTDi 6677.
    GeneCardsi GC07P123565.
    HGNCi HGNC:11217. SPAM1.
    HPAi HPA017984.
    MIMi 600930. gene.
    neXtProti NX_P38567.
    PharmGKBi PA36053.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77606.
    HOGENOMi HOG000015133.
    HOVERGENi HBG052053.
    KOi K01197.
    OMAi HLNPDNF.
    PhylomeDBi P38567.
    TreeFami TF321598.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02884-MONOMER.
    Reactomei REACT_163796. Interaction With Cumulus Cells.

    Miscellaneous databases

    GeneWikii SPAM1.
    GenomeRNAii 6677.
    NextBioi 26035.
    PROi P38567.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38567.
    Bgeei P38567.
    CleanExi HS_HYAL3.
    HS_SPAM1.
    Genevestigatori P38567.

    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. "Molecular cloning of the human and monkey sperm surface protein PH-20."
      Lin Y., Kimmel L.H., Myles D.G., Primakoff P.
      Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "The human sperm protein PH-20 has hyaluronidase activity."
      Gmachl M., Sagan S., Ketter S., Kreil G.
      FEBS Lett. 336:545-548(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Testis.
    3. "Expression analysis, genomic structure, and mapping to 7q31 of the human sperm adhesion molecule gene SPAM1."
      Jones M.H., Davey P.M., Aplin H., Affara N.A.
      Genomics 29:796-800(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    8. "In vitro mutagenesis of PH-20 hyaluronidase from human sperm."
      Arming S., Strobl B., Wechselberger C., Kreil G.
      Eur. J. Biochem. 247:810-814(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-146; GLU-148; ARG-211; GLU-284 AND ARG-287, GLYCOSYLATION.
    9. Cited for: VARIANT GLN-5.

    Entry informationi

    Entry nameiHYALP_HUMAN
    AccessioniPrimary (citable) accession number: P38567
    Secondary accession number(s): Q8TC30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3