GenomeNet

Database: UniProt
Entry: H3BX70_TETNG
LinkDB: H3BX70_TETNG
Original site: H3BX70_TETNG 
ID   H3BX70_TETNG            Unreviewed;       456 AA.
AC   H3BX70;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN   Name=HYAL4 {ECO:0000313|Ensembl:ENSTNIP00000000583.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000583.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000000583.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; H3BX70; -.
DR   STRING; 99883.ENSTNIP00000000583; -.
DR   Ensembl; ENSTNIT00000002654.1; ENSTNIP00000000583.1; ENSTNIG00000000981.1.
DR   GeneTree; ENSGT01020000230364; -.
DR   InParanoid; H3BX70; -.
DR   TreeFam; TF321598; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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:SF7; HYALURONIDASE-4; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00848; SPERMPH20.
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:UP000007303};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..456
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012858916"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        37..330
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        202..216
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        355..366
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        360..414
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        416..425
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   456 AA;  52413 MW;  8E96AEABA7C2EEAD CRC64;
     SWLLLLLHAA SGHKAARLPL IGRKPFIAAW NAPLDRCTTR YNISTNVERL FHIQGSPRAE
     WTGQNITIFY ANRLGFYPHY TPQGVAVNGG LPQNCSLDLH LLKAHQDIRR FIPARDVRGL
     AVIDWEFWRP QWKRNWHKKV IYRRRSKELT ARAYGNVTEA QVEELARRRF EKSAKAFMQQ
     TLQLGTRLRP NTLWGFYLYP DCHNYNLEQQ NYTGLCPLLE RRRNDELRWL WNSSSALFPS
     VAIRRDHSDS ASNRHFSQHR IREALRVASL TSREYQLPTF VYLRLGYRDE ALTFLSAKDL
     VHTIGESAAL GAAGFVIWGD LNLTSSRLNC SRVRSFLRHR LGRYITNVTR AAEFCSDFLC
     QGNGRCVRRD PRAHHYLHLS GRSHRIRLSD DGAFAVSGGP SQQELRLLPR RFRCHCYEGH
     EGERCDSCSG AVSTGPGLEL VALALLLLHL LTTTVQ
//
DBGET integrated database retrieval system