ID A0A3Q1AHA1_AMPOC Unreviewed; 476 AA.
AC A0A3Q1AHA1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=HYAL2 {ECO:0000313|Ensembl:ENSAOCP00000000393.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000000393.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000000393.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|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}.
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DR STRING; 80972.ENSAOCP00000000392; -.
DR Ensembl; ENSAOCT00000015008.1; ENSAOCP00000000392.1; ENSAOCG00000003226.1.
DR Ensembl; ENSAOCT00000015009.1; ENSAOCP00000000393.1; ENSAOCG00000003226.1.
DR GeneTree; ENSGT01020000230364; -.
DR OMA; FPSIYMD; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005886; C:plasma membrane; 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:SF6; HYALURONIDASE-2; 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 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|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU610713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..476
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041084702"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 58..350
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 222..238
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 375..386
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 380..433
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 435..444
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 476 AA; 53962 MW; B5592B987F792276 CRC64;
MGAVLDSLLT TAGQLPWLLL TLFAWWTVLC SADTKQTRWP LYSQKPVLLA WNAPTQECAP
RHGVTLSLDQ FDIVASPNEG FVRQNLTIFY KERLGLYPYY ERGGTAVNGG LPQLASLSQH
YEKMPEGLQK YIREIDAKGL AVIDWEEWRP LWIRNWYTKD IYRNKSREMV AKKNPKWTPE
QVGKVAQQEF ELSARKFMLE TLRLAKNLRP NQLWGFYLFP DCYNHDYRNG LKNYTGRCPA
VEVARNDQLN WLWMECTAFF PSIYMGSILR STKYGRLFVR NRVKEALRLA SVGDGLARPV
FVYTRPTYIS QMTLLTETDL VSTIGESVAL GAAGVIFWGD TSYADSSVSC STVNQYLLGP
LGRYLLNVST AAEQCSQVLC KSHGRCLRRA PDSDVYLHLS PSTHRITTQS GQLKVTGVPG
QAELAVFRTH FQCQCYSGYR GDSCAQKEKG QNRASSVFGT WPLCLLLPLG LLTLLH
//
