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Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface protein PH-20)

 HYALP_HUMAN             Reviewed;         509 AA.
P38567; Q8TC30;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=Hyaluronidase PH-20;
Short=Hyal-PH20;
EC=3.2.1.35;
AltName: Full=Hyaluronoglucosaminidase PH-20;
AltName: Full=Sperm adhesion molecule 1;
AltName: Full=Sperm surface protein PH-20;
Flags: Precursor;
Name=SPAM1; Synonyms=HYAL3, PH20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=8234258; DOI=10.1073/pnas.90.21.10071;
Lin Y., Kimmel L.H., Myles D.G., Primakoff P.;
"Molecular cloning of the human and monkey sperm surface protein PH-
20.";
Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Testis;
PubMed=8282124; DOI=10.1016/0014-5793(93)80873-S;
Gmachl M., Sagan S., Ketter S., Kreil G.;
"The human sperm protein PH-20 has hyaluronidase activity.";
FEBS Lett. 336:545-548(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=8575780; DOI=10.1006/geno.1995.9931;
Jones M.H., Davey P.M., Aplin H., Affara N.A.;
"Expression analysis, genomic structure, and mapping to 7q31 of the
human sperm adhesion molecule gene SPAM1.";
Genomics 29:796-800(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
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.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
MUTAGENESIS OF ASP-146; GLU-148; ARG-211; GLU-284 AND ARG-287, AND
GLYCOSYLATION.
PubMed=9288901; DOI=10.1111/j.1432-1033.1997.t01-1-00810.x;
Arming S., Strobl B., Wechselberger C., Kreil G.;
"In vitro mutagenesis of PH-20 hyaluronidase from human sperm.";
Eur. J. Biochem. 247:810-814(1997).
[9]
VARIANT GLN-5.
PubMed=21248752; DOI=10.1038/nature09639;
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., 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.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- 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.
{ECO:0000269|PubMed:8282124}.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P38567-1; Sequence=Displayed;
Name=2;
IsoId=P38567-2; Sequence=VSP_042714;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:8234258}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9288901}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SPAM1ID42361ch7q31.html";
-----------------------------------------------------------------------
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EMBL; L13781; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S67798; AAC60607.2; -; mRNA.
EMBL; X84347; CAA59086.1; -; mRNA.
EMBL; AC004690; AAQ96882.1; -; Genomic_DNA.
EMBL; CH236947; EAL24329.1; -; Genomic_DNA.
EMBL; CH471070; EAW83606.1; -; Genomic_DNA.
EMBL; BC026163; AAH26163.1; -; mRNA.
CCDS; CCDS5790.1; -. [P38567-2]
CCDS; CCDS5791.1; -. [P38567-1]
PIR; S40465; S40465.
RefSeq; NP_001167515.1; NM_001174044.1. [P38567-1]
RefSeq; NP_001167516.1; NM_001174045.1. [P38567-1]
RefSeq; NP_001167517.1; NM_001174046.1. [P38567-1]
RefSeq; NP_003108.2; NM_003117.4. [P38567-2]
RefSeq; NP_694859.1; NM_153189.2. [P38567-1]
UniGene; Hs.121494; -.
ProteinModelPortal; P38567; -.
SMR; P38567; -.
STRING; 9606.ENSP00000345849; -.
CAZy; GH56; Glycoside Hydrolase Family 56.
iPTMnet; P38567; -.
PhosphoSitePlus; P38567; -.
BioMuta; SPAM1; -.
DMDM; 585673; -.
PaxDb; P38567; -.
PeptideAtlas; P38567; -.
PRIDE; P38567; -.
DNASU; 6677; -.
Ensembl; ENST00000223028; ENSP00000223028; ENSG00000106304. [P38567-1]
Ensembl; ENST00000340011; ENSP00000345849; ENSG00000106304. [P38567-2]
Ensembl; ENST00000402183; ENSP00000386028; ENSG00000106304. [P38567-2]
Ensembl; ENST00000439500; ENSP00000402123; ENSG00000106304. [P38567-1]
Ensembl; ENST00000460182; ENSP00000417934; ENSG00000106304. [P38567-1]
GeneID; 6677; -.
KEGG; hsa:6677; -.
UCSC; uc003vle.4; human. [P38567-1]
CTD; 6677; -.
DisGeNET; 6677; -.
EuPathDB; HostDB:ENSG00000106304.15; -.
GeneCards; SPAM1; -.
HGNC; HGNC:11217; SPAM1.
HPA; HPA017984; -.
MIM; 600930; gene.
neXtProt; NX_P38567; -.
OpenTargets; ENSG00000106304; -.
PharmGKB; PA36053; -.
eggNOG; ENOG410IECJ; Eukaryota.
eggNOG; ENOG410XPZT; LUCA.
GeneTree; ENSGT00550000074476; -.
HOGENOM; HOG000015133; -.
HOVERGEN; HBG052053; -.
InParanoid; P38567; -.
KO; K01197; -.
OMA; HLNPDNF; -.
OrthoDB; EOG091G064G; -.
PhylomeDB; P38567; -.
TreeFam; TF321598; -.
BioCyc; MetaCyc:HS02884-MONOMER; -.
Reactome; R-HSA-2534343; Interaction With Cumulus Cells.
GeneWiki; SPAM1; -.
GenomeRNAi; 6677; -.
PRO; PR:P38567; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106304; -.
CleanEx; HS_HYAL3; -.
CleanEx; HS_SPAM1; -.
ExpressionAtlas; P38567; baseline and differential.
Genevisible; P38567; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0007339; P:binding of sperm to zona pellucida; TAS:ProtInc.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
GO; GO:0035036; P:sperm-egg recognition; TAS:Reactome.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR018155; Hyaluronidase.
InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
PANTHER; PTHR11769; PTHR11769; 1.
Pfam; PF01630; Glyco_hydro_56; 1.
PIRSF; PIRSF038193; Hyaluronidase; 1.
PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 1.
PRINTS; PR00846; GLHYDRLASE56.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
Lipoprotein; Membrane; Polymorphism; Reference proteome; Signal.
SIGNAL 1 35 {ECO:0000250}.
CHAIN 36 490 Hyaluronidase PH-20.
/FTId=PRO_0000012089.
PROPEP 491 509 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012090.
ACT_SITE 148 148 Proton donor. {ECO:0000250}.
LIPID 490 490 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 393 393 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 351 {ECO:0000250}.
DISULFID 224 238 {ECO:0000250}.
DISULFID 376 387 {ECO:0000250}.
DISULFID 381 435 {ECO:0000250}.
DISULFID 437 464 {ECO:0000250}.
VAR_SEQ 496 509 VSILFLIISSVASL -> WRLEVWDQGISRIGFF (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042714.
VARIANT 5 5 K -> Q (found in a renal cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064756.
VARIANT 47 47 V -> A (in dbSNP:rs34633019).
/FTId=VAR_049213.
MUTAGEN 146 146 D->N: Reduces activity by 80%.
{ECO:0000269|PubMed:9288901}.
MUTAGEN 148 148 E->Q: Loss of activity.
{ECO:0000269|PubMed:9288901}.
MUTAGEN 211 211 R->G: Reduces activity by over 90%.
{ECO:0000269|PubMed:9288901}.
MUTAGEN 284 284 E->Q: Loss of activity.
{ECO:0000269|PubMed:9288901}.
MUTAGEN 287 287 R->T: Loss of activity.
{ECO:0000269|PubMed:9288901}.
CONFLICT 48 48 P -> A (in Ref. 2; AAC60607).
{ECO:0000305}.
CONFLICT 499 499 L -> W (in Ref. 2; AAC60607).
{ECO:0000305}.
SEQUENCE 509 AA; 57848 MW; 5ADB4739747E32E8 CRC64;
MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPVIPNVPFL WAWNAPSEFC
LGKFDEPLDM SLFSFIGSPR INATGQGVTI FYVDRLGYYP YIDSITGVTV NGGIPQKISL
QDHLDKAKKD ITFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS
LTEATEKAKQ EFEKAGKDFL VETIKLGKLL RPNHLWGYYL FPDCYNHHYK KPGYNGSCFN
VEIKRNDDLS WLWNESTALY PSIYLNTQQS PVAATLYVRN RVREAIRVSK IPDAKSPLPV
FAYTRIVFTD QVLKFLSQDE LVYTFGETVA LGASGIVIWG TLSIMRSMKS CLLLDNYMET
ILNPYIINVT LAAKMCSQVL CQEQGVCIRK NWNSSDYLHL NPDNFAIQLE KGGKFTVRGK
PTLEDLEQFS EKFYCSCYST LSCKEKADVK DTDAVDVCIA DGVCIDAFLK PPMETEEPQI
FYNASPSTLS ATMFIVSILF LIISSVASL


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