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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_MOUSE             Reviewed;         512 AA.
P48794; Q7TSD6; Q812F4; Q9DAQ1;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
22-NOV-2017, entry version 141.
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, Spam;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
TISSUE=Sperm;
Ramarao C.S., Primakoff P.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ; TISSUE=Testis;
PubMed=12065596; DOI=10.1074/jbc.M204596200;
Baba D., Kashiwabara S., Honda A., Yamagata K., Wu Q., Ikawa M.,
Okabe M., Baba T.;
"Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through
the layer of cumulus cells and fertilize the egg.";
J. Biol. Chem. 277:30310-30314(2002).
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=BALB/cJ; TISSUE=Testis;
Hardy C.M., Mobbs K.J.;
"Assessment of contraceptive vaccines based on mouse sperm protein PH-
20 (SPAM-1).";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
CHARACTERIZATION.
PubMed=7794889; DOI=10.1021/bi00024a002;
Thaler C.D., Cardullo R.A.;
"Biochemical characterization of a glycosylphosphatidylinositol-linked
hyaluronidase on mouse sperm.";
Biochemistry 34:7788-7795(1995).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U33958; AAA76603.1; -; mRNA.
EMBL; AB085677; BAC55070.1; -; Genomic_DNA.
EMBL; AY228460; AAP49832.1; -; mRNA.
EMBL; AK005638; BAB24161.1; -; mRNA.
CCDS; CCDS19947.1; -.
RefSeq; NP_001073344.1; NM_001079875.2.
RefSeq; NP_033267.2; NM_009241.3.
RefSeq; XP_006505088.1; XM_006505025.2.
UniGene; Mm.4688; -.
ProteinModelPortal; P48794; -.
SMR; P48794; -.
BioGrid; 203421; 1.
STRING; 10090.ENSMUSP00000031693; -.
CAZy; GH56; Glycoside Hydrolase Family 56.
PaxDb; P48794; -.
PeptideAtlas; P48794; -.
PRIDE; P48794; -.
DNASU; 20690; -.
Ensembl; ENSMUST00000031693; ENSMUSP00000031693; ENSMUSG00000029682.
Ensembl; ENSMUST00000202331; ENSMUSP00000143944; ENSMUSG00000029682.
Ensembl; ENSMUST00000202569; ENSMUSP00000143970; ENSMUSG00000029682.
GeneID; 20690; -.
KEGG; mmu:20690; -.
UCSC; uc009bby.2; mouse.
CTD; 6677; -.
MGI; MGI:109335; Spam1.
eggNOG; ENOG410YDEI; LUCA.
GeneTree; ENSGT00550000074476; -.
HOGENOM; HOG000015133; -.
HOVERGEN; HBG052053; -.
InParanoid; P48794; -.
KO; K01197; -.
OMA; NANTYLC; -.
OrthoDB; EOG091G064G; -.
PhylomeDB; P48794; -.
TreeFam; TF321598; -.
Reactome; R-MMU-2534343; Interaction With Cumulus Cells.
PRO; PR:P48794; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029682; -.
CleanEx; MM_SPAM1; -.
Genevisible; P48794; MM.
GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:MGI.
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 involved in single fertilization; IEA:InterPro.
GO; GO:0007338; P:single fertilization; IMP:MGI.
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;
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_0000012093.
PROPEP ? 512 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012094.
ACT_SITE 147 147 Proton donor. {ECO:0000250}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 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}.
CONFLICT 182 182 E -> R (in Ref. 1; AAA76603).
{ECO:0000305}.
CONFLICT 191 191 F -> L (in Ref. 1; AAA76603).
{ECO:0000305}.
CONFLICT 271 271 N -> H (in Ref. 2; BAC55070).
{ECO:0000305}.
CONFLICT 495 495 H -> R (in Ref. 4; BAB24161).
{ECO:0000305}.
SEQUENCE 512 AA; 58498 MW; 6502F9FC75E7C86F CRC64;
MGELRFKHLF WGSFVESGGT FQTVLIFLLI PCSLTVDYRA APILSNTTFL WIWNVPTERC
VGNVNDPIDL SFFSLIGSPR KTATGQPVTL FYVDRLGLYP HIDANQAEHY GGIPQRGDYQ
AHLRKAKTDI EHYIPDDKLG LAIIDWEEWR PTWLRNWKPK DNYRNKSIEL VQSTNPGLSI
TEATQKAIQQ FEEAGRKFME GTLHLGKFLR PNQLWGYYLF PDCYNNKFQD PKYDGQCPAV
EKKRNDNLKW LWKASTGLYP SVYLKKDLKS NRQATLYVRY RVVEAIRVSK VGNASDPVPI
FVYIRLVFTD RTSEYLLEDD LVNTIGEIVA LGTSGIIIWD AMSLAQRAAG CPILHKYMQT
TLNPYIVNVT LAAKMCSQTL CNEKGMCSRR KESSDVYLHL NPSHFDIMLT ETGKYEVLGN
PRVGDLEYFS EHFKCSCFSR MTCKETSDVK NVQDVNVCVG DNVCIKAKVE PNPAFYLLPG
KSLLFMTTLG HVLYHLPQDI FVFPRKTLVS TP


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