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P38567 (HYALP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·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:HYAL3, PH20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 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. Ref.2

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.

Tissue specificity

Testis. Ref.1

Post-translational modification

N-glycosylated. Ref.8

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P38567-1)

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.
Isoform 2 (identifier: P38567-2)

The sequence of this isoform differs from the canonical sequence as follows:
     496-509: VSILFLIISSVASL → WRLEVWDQGISRIGFF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 By similarity
Chain36 – 490455Hyaluronidase PH-20
PRO_0000012089
Propeptide491 – 50919Removed in mature form Potential
PRO_0000012090

Sites

Active site1481Proton donor By similarity

Amino acid modifications

Lipidation4901GPI-anchor amidated serine Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 351 By similarity
Disulfide bond224 ↔ 238 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 435 By similarity
Disulfide bond437 ↔ 464 By similarity

Natural variations

Alternative sequence496 – 50914VSILF…SVASL → WRLEVWDQGISRIGFF in isoform 2.
VSP_042714
Natural variant51K → Q Found in a renal cell carcinoma sample; somatic mutation. Ref.9
VAR_064756
Natural variant471V → A.
Corresponds to variant rs34633019 [ dbSNP | Ensembl ].
VAR_049213

Experimental info

Mutagenesis1461D → N: Reduces activity by 80%. Ref.8
Mutagenesis1481E → Q: Loss of activity. Ref.8
Mutagenesis2111R → G: Reduces activity by over 90%. Ref.8
Mutagenesis2841E → Q: Loss of activity. Ref.8
Mutagenesis2871R → T: Loss of activity. Ref.8
Sequence conflict481P → A in AAC60607. Ref.2
Sequence conflict4991L → W in AAC60607. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 5ADB4739747E32E8

FASTA50957,848
        10         20         30         40         50         60 
MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPVIPNVPFL WAWNAPSEFC 

        70         80         90        100        110        120 
LGKFDEPLDM SLFSFIGSPR INATGQGVTI FYVDRLGYYP YIDSITGVTV NGGIPQKISL 

       130        140        150        160        170        180 
QDHLDKAKKD ITFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS 

       190        200        210        220        230        240 
LTEATEKAKQ EFEKAGKDFL VETIKLGKLL RPNHLWGYYL FPDCYNHHYK KPGYNGSCFN 

       250        260        270        280        290        300 
VEIKRNDDLS WLWNESTALY PSIYLNTQQS PVAATLYVRN RVREAIRVSK IPDAKSPLPV 

       310        320        330        340        350        360 
FAYTRIVFTD QVLKFLSQDE LVYTFGETVA LGASGIVIWG TLSIMRSMKS CLLLDNYMET 

       370        380        390        400        410        420 
ILNPYIINVT LAAKMCSQVL CQEQGVCIRK NWNSSDYLHL NPDNFAIQLE KGGKFTVRGK 

       430        440        450        460        470        480 
PTLEDLEQFS EKFYCSCYST LSCKEKADVK DTDAVDVCIA DGVCIDAFLK PPMETEEPQI 

       490        500 
FYNASPSTLS ATMFIVSILF LIISSVASL 

« Hide

Isoform 2 [UniParc].

Checksum: 8620113DE58741C7
Show »

FASTA51158,395

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS40465.
RefSeqNP_001167515.1. NM_001174044.1.
NP_001167516.1. NM_001174045.1.
NP_001167517.1. NM_001174046.1.
NP_003108.2. NM_003117.4.
NP_694859.1. NM_153189.2.
UniGeneHs.121494.

3D structure databases

ProteinModelPortalP38567.
SMRP38567. Positions 37-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000345849.

Chemistry

DrugBankDB00070. Hyaluronidase.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

PTM databases

PhosphoSiteP38567.

Polymorphism databases

DMDM585673.

Proteomic databases

PaxDbP38567.
PRIDEP38567.

Protocols and materials databases

DNASU6677.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223028; ENSP00000223028; ENSG00000106304. [P38567-1]
ENST00000340011; ENSP00000345849; ENSG00000106304. [P38567-2]
ENST00000402183; ENSP00000386028; ENSG00000106304. [P38567-1]
ENST00000439500; ENSP00000402123; ENSG00000106304. [P38567-1]
ENST00000460182; ENSP00000417934; ENSG00000106304. [P38567-1]
GeneID6677.
KEGGhsa:6677.
UCSCuc003vld.3. human. [P38567-1]
uc003vle.3. human. [P38567-2]

Organism-specific databases

CTD6677.
GeneCardsGC07P123565.
HGNCHGNC:11217. SPAM1.
HPAHPA017984.
MIM600930. gene.
neXtProtNX_P38567.
PharmGKBPA36053.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
KOK01197.
OMAHLNPDNF.
PhylomeDBP38567.
TreeFamTF321598.

Enzyme and pathway databases

BioCycMetaCyc:HS02884-MONOMER.
ReactomeREACT_163848. Reproduction.

Gene expression databases

ArrayExpressP38567.
BgeeP38567.
CleanExHS_HYAL3.
HS_SPAM1.
GenevestigatorP38567.

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.
PTHR11769:SF4. PTHR11769:SF4. 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

GeneWikiSPAM1.
GenomeRNAi6677.
NextBio26035.
PROP38567.
SOURCESearch...

Entry information

Entry nameHYALP_HUMAN
AccessionPrimary (citable) accession number: P38567
Secondary accession number(s): Q8TC30
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries