ID   HYALP_MACFA             Reviewed;         510 AA.
AC   P38568; G7P0K2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 110.
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; ORFNames=EGM_12920;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=8234258; DOI=10.1073/pnas.90.21.10071;
RA   Lin Y., Kimmel L.H., Myles D.G., Primakoff P.;
RT   "Molecular cloning of the human and monkey sperm surface protein PH-20.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P38568-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P38568-2; Sequence=VSP_046430;
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; L13780; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CM001278; EHH52472.1; -; Genomic_DNA.
DR   AlphaFoldDB; P38568; -.
DR   SMR; P38568; -.
DR   STRING; 9541.ENSMFAP00000006823; -.
DR   GlyCosmos; P38568; 8 sites, No reported glycans.
DR   eggNOG; ENOG502R6HD; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0002079; C:inner acrosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
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; IEA:TreeGrafter.
DR   GO; GO:0007341; P:penetration of zona pellucida; IMP:UniProtKB.
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:SF20; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..491
FT                   /note="Hyaluronidase PH-20"
FT                   /id="PRO_0000012091"
FT   PROPEP          492..510
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012092"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           491
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..238
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   VAR_SEQ         497..510
FT                   /note="VNILFLIISSVASL -> WRLEVWDQGISRIGFF (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046430"
SQ   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
//