HYALP_CAVPO
ID HYALP_CAVPO Reviewed; 529 AA.
AC P23613;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=PH-20, PH20;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Hartley;
RX PubMed=2269661; DOI=10.1083/jcb.111.6.2939;
RA Lathrop W.F., Carmichael E.P., Myles D.G., Primakoff P.;
RT "cDNA cloning reveals the molecular structure of a sperm surface protein,
RT PH-20, involved in sperm-egg adhesion and the wide distribution of its gene
RT among mammals.";
RL J. Cell Biol. 111:2939-2949(1990).
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 -!- PTM: Endoproteolysis (toward the C-terminus producing two disulfide-
CC linked fragments) could activate PH-20.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; X56332; CAA39768.1; -; mRNA.
DR PIR; A36343; A36343.
DR RefSeq; NP_001166492.1; NM_001173021.2.
DR AlphaFoldDB; P23613; -.
DR SMR; P23613; -.
DR STRING; 10141.ENSCPOP00000001550; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR Ensembl; ENSCPOT00000001737; ENSCPOP00000001550; ENSCPOG00000001716.
DR GeneID; 100135624; -.
DR KEGG; cpoc:100135624; -.
DR CTD; 6677; -.
DR eggNOG; ENOG502R6HD; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_1_1; -.
DR InParanoid; P23613; -.
DR OMA; RAKIVFE; -.
DR OrthoDB; 1096692at2759; -.
DR TreeFam; TF321598; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000001716; Expressed in testis and 2 other tissues.
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 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..35
FT CHAIN 36..492
FT /note="Hyaluronidase PH-20"
FT /id="PRO_0000012087"
FT PROPEP 493..529
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012088"
FT REGION 478..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 492
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
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 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
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 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..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"
SQ SEQUENCE 529 AA; 60365 MW; B3432356AED46245 CRC64;
MGAFTFKHSF FGSFVECSGV LQTVFIFLLI PCCLADKRAP PLIPNVPLLW VWNAPTEFCI
GGTNQPLDMS FFSIVGTPRK NITGQSITLY YVDRLGYYPY IDPHTGAIVH GGLPQLMNLQ
QHLRKSRQDI LFYMPTDSVG LAVIDWEEWR PTWTRNWRPK DIYRNKSIEL VKSQHPQYNH
SYAVAVAKRD FERTGKAFML ETLKLGKSLR PSSLWGYYLF PDCYNTHFTK PNYDGHCPPI
ELQRNNDLQW LWNDSTALYP SVYLTSRVRS SQNGALYVRN RVHESIRVSK LMDDKNPLPI
YVYIRLVFTD QTTTFLELDD LVHSVGEIVP LGVSGIIIWG SLSLTRSLVS CIGLENYMKG
TLLPYLINVT LAAKMCGQVL CKNQGICTRK DWNTNTYLHL NATNFDIELQ QNGKFVVHGK
PSLEDLQEFS KNFHCSCYTN VACKDRLDVH NVRSVNVCTA NNICIDAVLN FPSLDDDDEP
PITDDTSQNQ DSISDITSSA PPSSHILPKD LSWCLFLLSI FSQHWKYLL
