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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_MACFA             Reviewed;         510 AA.
P38568; G7P0K2;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
10-MAY-2017, entry version 89.
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=PH20; ORFNames=EGM_12920;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [LARGE SCALE GENOMIC DNA].
PubMed=22002653; DOI=10.1038/nbt.1992;
Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N.,
Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P.,
Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T.,
Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D.,
Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X.,
Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J.,
Wang X., Wang J.;
"Genome sequencing and comparison of two nonhuman primate animal
models, the cynomolgus and Chinese rhesus macaques.";
Nat. Biotechnol. 29:1019-1023(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.
-!- 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=P38568-1; Sequence=Displayed;
Name=2;
IsoId=P38568-2; Sequence=VSP_046430;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Testis.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L13780; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CM001278; EHH52472.1; -; Genomic_DNA.
ProteinModelPortal; P38568; -.
SMR; P38568; -.
CAZy; GH56; Glycoside Hydrolase Family 56.
HOVERGEN; HBG052053; -.
Proteomes; UP000009130; Chromosome 3.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane; IEA:InterPro.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR018155; Hyaluronidase.
InterPro; IPR001439; Hyaluronidase_PH20.
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.
2: Evidence at transcript level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
Lipoprotein; Membrane; Reference proteome; Signal.
SIGNAL 1 35 {ECO:0000250}.
CHAIN 36 491 Hyaluronidase PH-20.
/FTId=PRO_0000012091.
PROPEP 492 510 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012092.
ACT_SITE 148 148 Proton donor. {ECO:0000250}.
LIPID 491 491 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}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 484 484 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 497 510 VNILFLIISSVASL -> WRLEVWDQGISRIGFF (in
isoform 2). {ECO:0000305}.
/FTId=VSP_046430.
SEQUENCE 510 AA; 57935 MW; D50EE36C67CF1BBF CRC64;
MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPIIPNVPFL WAWNAPSEFC
LGKFNEPLDM SLFTLMGSPR INVTGQGVTI FYVDRLGYYP YIDLTTGVTV HGGIPQKVSL
QDHLDKSKQD ILFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS
LPQATDKAKQ EFEKAGKDFM LETIKLGRSL RPNHLWGYYL FPDCYNHHYR KPGYNGSCFD
VEIKRNDDLS WLWNESTALY PSIYLNTQQS VVVATLYVRN RVREAIRVSK IPDAKNPLPV
FVYARLVFTD QVLKFLSREE LVSTLGETVA LGASGIVIWG SLSITRSMKS CLLLDTYMET
ILNPYIINVT LAAKMCSQVL CQEQGVCIRK DWNSSDYLHL NPDNFDIRLE KGGKFTVHGK
PTVEDLEEFS EKFYCSCYTN LSCKEKADVK DTDAVDVCIA DGVCIDASLK PPVETEGSPP
IFYNTSSSTV STTMFIVNIL FLIISSVASL


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