ID   HYALP_MOUSE             Reviewed;         512 AA.
AC   P48794; Q7TSD6; Q812F4; Q9DAQ1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Hyaluronidase PH-20;
DE            Short=Hyal-PH20;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase PH-20;
DE   AltName: Full=Sperm adhesion molecule 1;
DE   AltName: Full=Sperm surface protein PH-20;
DE   Flags: Precursor;
GN   Name=Spam1; Synonyms=Ph20, Spam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Sperm;
RA   Ramarao C.S., Primakoff P.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Testis;
RX   PubMed=12065596; DOI=10.1074/jbc.m204596200;
RA   Baba D., Kashiwabara S., Honda A., Yamagata K., Wu Q., Ikawa M., Okabe M.,
RA   Baba T.;
RT   "Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the
RT   layer of cumulus cells and fertilize the egg.";
RL   J. Biol. Chem. 277:30310-30314(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RA   Hardy C.M., Mobbs K.J.;
RT   "Assessment of contraceptive vaccines based on mouse sperm protein PH-20
RT   (SPAM-1).";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=7794889; DOI=10.1021/bi00024a002;
RA   Thaler C.D., Cardullo R.A.;
RT   "Biochemical characterization of a glycosylphosphatidylinositol-linked
RT   hyaluronidase on mouse sperm.";
RL   Biochemistry 34:7788-7795(1995).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in sperm-egg adhesion. Upon fertilization sperm must
CC       first penetrate a layer of cumulus cells that surrounds the egg before
CC       reaching the zona pellucida. The cumulus cells are embedded in a matrix
CC       containing hyaluronic acid which is formed prior to ovulation. This
CC       protein aids in penetrating the layer of cumulus cells by digesting
CC       hyaluronic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; U33958; AAA76603.1; -; mRNA.
DR   EMBL; AB085677; BAC55070.1; -; Genomic_DNA.
DR   EMBL; AY228460; AAP49832.1; -; mRNA.
DR   EMBL; AK005638; BAB24161.1; -; mRNA.
DR   CCDS; CCDS19947.1; -.
DR   RefSeq; NP_001073344.1; NM_001079875.2.
DR   RefSeq; NP_033267.2; NM_009241.3.
DR   RefSeq; XP_006505088.1; XM_006505025.3.
DR   AlphaFoldDB; P48794; -.
DR   SMR; P48794; -.
DR   BioGRID; 203421; 1.
DR   FunCoup; P48794; 147.
DR   STRING; 10090.ENSMUSP00000143970; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   GlyCosmos; P48794; 4 sites, No reported glycans.
DR   GlyGen; P48794; 4 sites.
DR   PhosphoSitePlus; P48794; -.
DR   SwissPalm; P48794; -.
DR   PaxDb; 10090-ENSMUSP00000143970; -.
DR   PeptideAtlas; P48794; -.
DR   ProteomicsDB; 269512; -.
DR   DNASU; 20690; -.
DR   Ensembl; ENSMUST00000031693.3; ENSMUSP00000031693.3; ENSMUSG00000029682.6.
DR   Ensembl; ENSMUST00000202331.4; ENSMUSP00000143944.2; ENSMUSG00000029682.6.
DR   Ensembl; ENSMUST00000202569.4; ENSMUSP00000143970.2; ENSMUSG00000029682.6.
DR   GeneID; 20690; -.
DR   KEGG; mmu:20690; -.
DR   UCSC; uc009bby.2; mouse.
DR   AGR; MGI:109335; -.
DR   CTD; 6677; -.
DR   MGI; MGI:109335; Spam1.
DR   VEuPathDB; HostDB:ENSMUSG00000029682; -.
DR   eggNOG; ENOG502R6HD; Eukaryota.
DR   GeneTree; ENSGT01020000230364; -.
DR   InParanoid; P48794; -.
DR   OMA; SLAAKMC; -.
DR   OrthoDB; 5796153at2759; -.
DR   PhylomeDB; P48794; -.
DR   BioGRID-ORCS; 20690; 1 hit in 76 CRISPR screens.
DR   PRO; PR:P48794; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P48794; protein.
DR   Bgee; ENSMUSG00000029682; Expressed in spermatid and 9 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
DR   GO; GO:0007338; P:single fertilization; IMP:MGI.
DR   FunFam; 3.20.20.70:FF:000065; Hyaluronidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR018155; Hyaluronidase.
DR   InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF17; HYALURONIDASE PH-20; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00848; SPERMPH20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Glycosidase;
KW   GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..?
FT                   /note="Hyaluronidase PH-20"
FT                   /id="PRO_0000012093"
FT   PROPEP          ?..512
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012094"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        376..387
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..435
FT                   /evidence="ECO:0000250"
FT   DISULFID        437..464
FT                   /evidence="ECO:0000250"
FT   CONFLICT        182
FT                   /note="E -> R (in Ref. 1; AAA76603)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="F -> L (in Ref. 1; AAA76603)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="N -> H (in Ref. 2; BAC55070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="H -> R (in Ref. 4; BAB24161)"
FT                   /evidence="ECO:0000305"
SQ   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
//