ID A0A3B4FVX6_9CICH Unreviewed; 481 AA.
AC A0A3B4FVX6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000013456.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000013456.1}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3B4FVX6; -.
DR Ensembl; ENSPNYT00000013787.1; ENSPNYP00000013456.1; ENSPNYG00000010033.1.
DR GeneTree; ENSGT01020000230364; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF19; HYALURONIDASE-3; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 2.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|RuleBase:RU610713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..481
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017310545"
FT DOMAIN 379..430
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT DISULFID 62..358
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 225..241
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 383..394
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 388..418
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 420..429
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 481 AA; 54960 MW; 04069BACA4344D0E CRC64;
MELSLLLLPV FFISSLRCNS LPQNSPQADA FIGTSLQAVA AAHPILQNQP FILVWNMPTA
NCPQRYNIHL DLGDFHIVEN KKERFQGQKM TIFYRDHLGK YPYLSRNGKK VNGGLPQLGD
LASHLSLTVT QLSDLLLPDF SGLAVIDWEE WRPLWETNFG SKVEYRRLSK LLVKQEQPDL
SERAVTSLAR RMFEESARKF MEETLQSAVG ERPKGFWGFY GFPTCFNKNK RKTDKTYTGR
CLRGTRQQND ELSWLWTKSS ALYPSIYLPQ KLAGSADAAL MVRHRLLEAL RVASGWPYHN
NTDHATPVLP YARLAFTHSL KFLSKMDLEH TLGESASLGA AGVVLWGELK FAKNKKQCVL
LRDYVHNVLG PFVRSLRSDA ERCSLQVCHG NGRCTRRHLS SGHRLSDSSK HFQKHFMCHC
YQGWTGQGCQ DKKSERGKYA HCLLQKAQLM SNSFVDHLNE RCRNLGIALK CKERLWNFKV
P
//
