ID A0A2Y9F022_PHYMC Unreviewed; 450 AA.
AC A0A2Y9F022;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=LOC102996103 {ECO:0000313|RefSeq:XP_007112219.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007112219.1};
RN [1] {ECO:0000313|RefSeq:XP_007112219.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007112219.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU610713};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC ECO:0000256|RuleBase:RU610713}.
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DR RefSeq; XP_007112219.1; XM_007112157.3.
DR AlphaFoldDB; A0A2Y9F022; -.
DR GlyCosmos; A0A2Y9F022; 1 site, No reported glycans.
DR Ensembl; ENSPCTT00005026949; ENSPCTP00005024453; ENSPCTG00005017484.
DR GeneID; 102996103; -.
DR KEGG; pcad:102996103; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000248484; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF23; HYALURONIDASE-1; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|RuleBase:RU610713};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 58..348
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 222..236
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 373..384
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 378..433
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 435..444
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 450 AA; 50314 MW; A3ED61DB2E046BDE CRC64;
MRPFSPEVSL DLPCATAAHL LPICTLFLNL LGMAKGSRDP VVPNRPFTTI WNANTQWCLE
RHGVDVDVSV FDVVANPGQT FRGPDMTIFY SYQLGTYPYY TSAGEPVFGG LPQNASLAVH
LVRTFQDILA AMPASNFSGL AVIDWEAWRP RWAFNWDTKD IYRQRSRALV QGQHPDWPAP
WVEAAAQDQF EGAARAWMAG TLRLGQALQP RGLWGFYGFP DCYNYDFKNP NYTGQCPPGI
RAQNDQLGWL WGQSRALYPS IYLPAALEGT KKAQMFVQHR VGEAFRLAVG AGYPDLPVLP
YVQIFYDMTN RFLPLEELEH SLGESADQGA AGVVLWVSWE NTRTKESCQA IKEYVDTTLG
PFILNVTSGA LLCSQVLCSG HGRCARRPSH PEAHLILSPT SFSIESTPGG GPLTLRGALS
LKDRLRMAVE FKCRCYRGWM GTWCEQWGMW
//
