HYALP_MACFA
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 25-MAY-2022, entry version 100.
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.XP_005550707.1; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR eggNOG; ENOG502R6HD; Eukaryota.
DR Proteomes; UP000009130; Chromosome 3.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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 GO; GO:0007341; P:penetration of zona pellucida; IMP:UniProtKB.
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 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
