ID   HYALP_RABIT             Reviewed;         545 AA.
AC   P38566;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 103.
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;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Andrews J.B., Holland M.K.;
RT   "The nucleic acid sequence of rabbit PH-20 cDNA.";
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Testis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; U09183; AAA88913.1; -; mRNA.
DR   RefSeq; NP_001076141.1; NM_001082672.1.
DR   AlphaFoldDB; P38566; -.
DR   SMR; P38566; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PRIDE; P38566; -.
DR   GeneID; 100009391; -.
DR   KEGG; ocu:100009391; -.
DR   CTD; 6677; -.
DR   InParanoid; P38566; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR   PANTHER; PTHR11769; PTHR11769; 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   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript 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_0000012095"
FT   PROPEP          ?..545
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012096"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..355
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..239
FT                   /evidence="ECO:0000250"
FT   DISULFID        380..391
FT                   /evidence="ECO:0000250"
FT   DISULFID        385..439
FT                   /evidence="ECO:0000250"
FT   DISULFID        441..468
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  62412 MW;  125AF314FE05AEB4 CRC64;
     MGVLKFKHIF FGSAVELSGV FQIVFIFLLI PCCLTANFRA PPVIPNVPFL WAWNAPTEFC
     LGKSGEPLDM SLFSLFGSPR KNKTGQGITI FYVDRLGYYP YIDPHTGAIV HGRIPQLGPL
     QQHLTKLRQE ILYYMPKDNV GLAVIDWEEW LPTWLRNWKP KDIYRIKSIE LVKSQHPQYN
     HSYATEKAKR DFEKAGKDFM EETLKLGRLL RPNHLWGYYL FPDCYNHHYD KPNLYKGSCF
     DIEKKRNDDL SWLWKESTAL FPSVYLTSRA RSATALSKLY VVRNRVHEAI RVSKIPDDKS
     PLPNFVYTRL VFTDQIFQFL SHHDLVYTIG EIVALGASGI VVWGSQSLAR SMKSCLHLDN
     YMKTILNPYL INVTLAAKMC NQVLCQEQGV CTRKNWNPND YLHLNPGNFA IQLGSNGTYK
     VDGKPTLTDL EQFSKNFQCS CYTNLNCKER TDMNNVRTVN VCAVENVCID TNVGPQAVTY
     APKEKKDVAH ILSNTTSINS STTMSLPFPR KHVSGCLLVL CMYSQYLNIC YRLVAIGIQH
     GYYLK