HYALP_RAT
ID HYALP_RAT Reviewed; 512 AA.
AC Q62803;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 antigen 2B1;
DE AltName: Full=Sperm surface protein PH-20;
DE Flags: Precursor;
GN Name=Spam1; Synonyms=Ph20, Spam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=8914077;
RX DOI=10.1002/(sici)1098-2795(199610)45:2<193::aid-mrd12>3.0.co;2-2;
RA Hou S.T., Ma A., Jones R., Hall L.;
RT "Molecular cloning and characterization of rat sperm surface antigen 2B1, a
RT glycoprotein implicated in sperm-zona binding.";
RL Mol. Reprod. Dev. 45:193-203(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). {ECO:0000250}.
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; X89999; CAA62016.1; -; mRNA.
DR EMBL; BC081748; AAH81748.1; -; mRNA.
DR RefSeq; NP_446419.1; NM_053967.2.
DR AlphaFoldDB; Q62803; -.
DR SMR; Q62803; -.
DR STRING; 10116.ENSRNOP00000009537; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q62803; 5 sites.
DR PaxDb; Q62803; -.
DR Ensembl; ENSRNOT00000009537; ENSRNOP00000009537; ENSRNOG00000007231.
DR GeneID; 117037; -.
DR KEGG; rno:117037; -.
DR UCSC; RGD:620547; rat.
DR CTD; 6677; -.
DR RGD; 620547; Spam1.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_1_1; -.
DR InParanoid; Q62803; -.
DR OMA; DDQASCE; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; Q62803; -.
DR TreeFam; TF321598; -.
DR PRO; PR:Q62803; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007231; Expressed in testis.
DR Genevisible; Q62803; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; TAS:RGD.
DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; ISO:RGD.
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_0000012097"
FT PROPEP ?..512
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012098"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
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 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
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"
SQ SEQUENCE 512 AA; 58412 MW; 5ED01DA50F9153B0 CRC64;
MGELQFKWLF WRSFAESGGT FQTVLIFLFI PYSLTVDYRA TPVLSDTTFV WVWNVPTEAC
VENVTEPIDL SFFSLIGSPR KTAIGQPVTL FYVDRLGNYP HIDAQQTEHH GGIPQKGDLT
THLVKAKEDV ERYIPTDKLG LAIIDWEEWR PTWMRNWTPK DIYRNKSIEL VQAADPAINI
TEATVRAKAQ FEGAAKEFME GTLKLGKHIR PKHLWGFYLF PDCYNNKFQV DNYDGQCPDV
EKKRNDDLDW LWKESTGLYP SVYLKKDLKS SRKATLYVRY RVLESIRVSK VSDESNPVPI
FVYIRLVFTD HVSEYLLEDD LVNTIGEIVA QGTSGIIIWD AMSLAQRSAG CPILRQYMKT
TLNPYIVNVT LAAKMCSQTL CKEKGMCSRK TESSDAYLHL DPSSFSINVT EAGKYEVLGK
PEVKDLEYFS EHFKCSCFSK MTCEETSDMR SIQDVNVCMG DNVCIKATLG PNSAFHLLPG
KGLLLMTTLA HILHHLPHDI FVFPWKMLVS TP
