ID A0A218URN4_9PASE Unreviewed; 941 AA.
AC A0A218URN4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Hyaluronidase {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
GN Name=HYAL2 {ECO:0000313|EMBL:OWK56012.1};
GN ORFNames=RLOC_00013153 {ECO:0000313|EMBL:OWK56012.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK56012.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK56012.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK56012.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC an intermediate-sized product which is further hydrolyzed by sperm
CC hyaluronidase to give small oligosaccharides. Displays very low levels
CC of activity. Associates with and negatively regulates MST1R.
CC {ECO:0000256|ARBA:ARBA00037675}.
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 Evidence={ECO:0000256|ARBA:ARBA00000251,
CC ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC ECO:0000256|RuleBase:RU610713}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK56012.1}.
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DR EMBL; MUZQ01000178; OWK56012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218URN4; -.
DR STRING; 299123.ENSLSDP00000025072; -.
DR GlyCosmos; A0A218URN4; 1 site, No reported glycans.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF6; HYALURONIDASE-2; 1.
DR Pfam; PF01630; Glyco_hydro_56; 2.
DR PIRSF; PIRSF038193; Hyaluronidase; 2.
DR PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 2.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR038193-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR038193};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038193};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..941
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012148936"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 49..342
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 213..229
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 367..378
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 372..431
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 433..442
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 941 AA; 107011 MW; 7E92E80D7D7BA96F CRC64;
MRGGCAAAVA VPWLALLALA RQPPEKPSAA PHLTRRPFLV AWNVPTQDCK PRFQVSFDFS
IFDLYASPNE GFVGQNLTIF YKERLGLYPY YTRQGVAVNG GVPQNSSLSE HLARLQEGIN
KYIRSSTKEG LAIIDWEEWR PVWARNWKPK DIYREASQEL VLQRQPTWPP EKVNKQAAFE
FESAAQEFMV RTLRKAKSFR PKQLWGFYLF PDCYNHDYSK NKESYTGQCP DVEKSRNDQL
KWLWKESMAL YPSIYLDPLL DSTPNSRKFV RARVMEAMRI SQKHHDDYSL PVFVYTRPTY
IRKLNVLSQA DLISTIGESA ALGAAGAILW GDAVDTRNRE LCQFMKNYLE GDLGRYVVNV
TTAAELCSTT LCQGRGRCLR QDSHADVFLH LNSTSFQLRR RDADHPERPL FWAEGQLSSA
DVLFLRTHFH CHCYQGWQGS GCQTRAGPRT ADKFGDFEEV EEVTLADRHR LGTEVWINAG
PDLGIKASRS RFYPGSSRTH PEHTGIMASA WSCWVLLLLL PALTHAGGPG PVLVNRPFVT
IWNIPTERCA EKYNVSLSLE VFDVLANDQQ SFTGQDITLF YSDKIGLFPY YTPEGVPVNG
GLPQNASLEA HIHQATQDIK VTLPSPDYSG LAVIDWEKWR PLWIRNWDSM EIYQQKSEEL
VQQQHPQWPP KEVEEMAKQQ FEKSACDFMN ETLWLGKSLR PSAYWGFYGF PDCYNNDFDS
LPYNGTCPDV EQQRNQNLSW LWKGSQALYP SIYLPLRLNG TNKVLAYVRH RVAEAFAVQQ
GILDSGIPVL PYSQIAFERT LDFLSQEDLM NTIGESAAQG AAGIILWGSL NYSTSKEMCL
RLKDYVEGPL GHYIVNVTAG ADLCSQTLCS GRGRCVRQDK QQGYLHLDPS RFTIDLRAGK
PWLVAQSLEP GEDISKLAKE FSCQCYDKWQ GPRCDTQGFA K
//
