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Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface antigen 2B1) (Sperm surface protein PH-20)

 HYALP_RAT               Reviewed;         512 AA.
Q62803;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 116.
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 antigen 2B1;
AltName: Full=Sperm surface protein PH-20;
Flags: Precursor;
Name=Spam1; Synonyms=Ph20, Spam;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Testis;
PubMed=8914077;
DOI=10.1002/(SICI)1098-2795(199610)45:2<193::AID-MRD12>3.0.CO;2-2;
Hou S.T., Ma A., Jones R., Hall L.;
"Molecular cloning and characterization of rat sperm surface antigen
2B1, a glycoprotein implicated in sperm-zona binding.";
Mol. Reprod. Dev. 45:193-203(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X89999; CAA62016.1; -; mRNA.
EMBL; BC081748; AAH81748.1; -; mRNA.
RefSeq; NP_446419.1; NM_053967.2.
UniGene; Rn.87544; -.
ProteinModelPortal; Q62803; -.
SMR; Q62803; -.
STRING; 10116.ENSRNOP00000009537; -.
CAZy; GH56; Glycoside Hydrolase Family 56.
PaxDb; Q62803; -.
PRIDE; Q62803; -.
Ensembl; ENSRNOT00000009537; ENSRNOP00000009537; ENSRNOG00000007231.
GeneID; 117037; -.
KEGG; rno:117037; -.
UCSC; RGD:620547; rat.
CTD; 6677; -.
RGD; 620547; Spam1.
eggNOG; ENOG410YDEI; LUCA.
GeneTree; ENSGT00550000074476; -.
HOGENOM; HOG000015133; -.
HOVERGEN; HBG052053; -.
InParanoid; Q62803; -.
KO; K01197; -.
OMA; NANTYLC; -.
OrthoDB; EOG091G064G; -.
PhylomeDB; Q62803; -.
TreeFam; TF321598; -.
PRO; PR:Q62803; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000007231; -.
Genevisible; Q62803; RN.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; TAS:RGD.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane; TAS:RGD.
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;
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 ? Hyaluronidase PH-20.
/FTId=PRO_0000012097.
PROPEP ? 512 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012098.
ACT_SITE 147 147 Proton donor. {ECO:0000250}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 351 {ECO:0000250}.
DISULFID 223 237 {ECO:0000250}.
DISULFID 376 387 {ECO:0000250}.
DISULFID 381 435 {ECO:0000250}.
DISULFID 437 464 {ECO:0000250}.
SEQUENCE 512 AA; 58412 MW; 5ED01DA50F9153B0 CRC64;
MGELQFKWLF WRSFAESGGT FQTVLIFLFI PYSLTVDYRA TPVLSDTTFV WVWNVPTEAC
VENVTEPIDL SFFSLIGSPR KTAIGQPVTL FYVDRLGNYP HIDAQQTEHH GGIPQKGDLT
THLVKAKEDV ERYIPTDKLG LAIIDWEEWR PTWMRNWTPK DIYRNKSIEL VQAADPAINI
TEATVRAKAQ FEGAAKEFME GTLKLGKHIR PKHLWGFYLF PDCYNNKFQV DNYDGQCPDV
EKKRNDDLDW LWKESTGLYP SVYLKKDLKS SRKATLYVRY RVLESIRVSK VSDESNPVPI
FVYIRLVFTD HVSEYLLEDD LVNTIGEIVA QGTSGIIIWD AMSLAQRSAG CPILRQYMKT
TLNPYIVNVT LAAKMCSQTL CKEKGMCSRK TESSDAYLHL DPSSFSINVT EAGKYEVLGK
PEVKDLEYFS EHFKCSCFSK MTCEETSDMR SIQDVNVCMG DNVCIKATLG PNSAFHLLPG
KGLLLMTTLA HILHHLPHDI FVFPWKMLVS TP


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