ID A0A3Q4BTJ1_MOLML Unreviewed; 435 AA.
AC A0A3Q4BTJ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000024832.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000024832.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- 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 AlphaFoldDB; A0A3Q4BTJ1; -.
DR Ensembl; ENSMMOT00000025249.1; ENSMMOP00000024832.1; ENSMMOG00000018859.1.
DR Proteomes; UP000261620; Unplaced.
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:SF20; HYALURONIDASE PH-20; 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:UP000261620};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..435
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018751895"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 47..337
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 209..223
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 362..373
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 367..420
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 435 AA; 49840 MW; 92B1E8A47249C1DD CRC64;
MAPPFLPRLF LCLIVSITSI HTPPPAEPPP IHNYPFVAIW NAPTDTCEKL HIELDLAAFK
AVTTPAAVPG QYLTIFYEHR LGLYPKVGLD EGEQYHGGIP KKELLKKHLS KAQSQIDHYI
PQDSPGLAVI DWESWRPLWD QNWGSKRIYQ KLYIDFTKKK NPKLSSENIS ELVKKQFEED
ARRFMEKTIR LGIRMRPSRR WGFYLFPACY NYGWEKPGYT GKCSTKTKRQ NNQLLWLWRD
STALFPSIYL SSTLRNSPHV KLFVRNIVKE AQRVAEQPKH PYMVPIYVYS RPVYRDQIQK
FLTQMDLVST VGEAAALGAS GIIMWGGSKD FNSKGACRSL SRYLKSTVNP YIANATAAAM
LCSQVLCQSN GRCLRKDSDS SHYLHLNPAH FTIRRADEKY VVIGLPSSGD LQAWAQHFTC
QCYAGRNCPS FMPWR
//
