ID A0A3P8PWT2_ASTCA Unreviewed; 515 AA.
AC A0A3P8PWT2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=HYAL4 {ECO:0000313|Ensembl:ENSACLP00000021505.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000021505.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000021505.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000021505.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8PWT2; -.
DR STRING; 8154.ENSACLP00000021505; -.
DR Ensembl; ENSACLT00000022003.1; ENSACLP00000021505.1; ENSACLG00000014630.1.
DR GeneTree; ENSGT01020000230364; -.
DR OMA; AGQDINY; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000265100; Chromosome 7.
DR Bgee; ENSACLG00000014630; Expressed in camera-type eye and 1 other cell type or tissue.
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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..515
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018158537"
FT REGION 456..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 59..352
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 224..238
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 377..388
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 382..436
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 438..447
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 515 AA; 59833 MW; 74B1133A046602C0 CRC64;
MPVVPVLGES SSHHAVPVAL TCSWLILLFH SAFGQKPAKL PLIGRKPFIA AWNAPLDLCT
FRYNITTNVN HLFHIQGSPR ADWTGQNVTI FYANRLGYYP HYTPHGKAVF GGLPQNCSLD
RHLFKAHQDI NYFIPAEDFR GLAVIDWEFW RPQWSRNWHK KDIYRRKSKE LTKKAYINVT
AAQVEELARR RFEKSAKMFM LKTIQLGRQL RPSALWGFYL YPDCHNYNLH DQNYTGFCPL
LERLRNDELV WLWNSSMALY PSVTIRKHHS NSISNLHFTQ HRIRESLRVA SLTSKEYDLP
TYVYLRLGYR DEALNFLTTD DLIHTIGESA ALGTAGFVIW GDLNLTSSRH SCTHVKSFLS
HRLGLYITNV TRAAEICSEF LCQSNGRCIR RDPHARHYLH LSADSYRIHP SEDGDFTVNG
WHSPHEQQLL MERFRCHCYE GHNGENCDSI NKVREDKGPW EEEEEYEDHD KKRTEWEDEQ
DEQQEAGESA AAPTCVSHHL TLLLLLNLLL VKIYV
//
