ID A0A3B3XUK4_9TELE Unreviewed; 431 AA.
AC A0A3B3XUK4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000018769.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000018769.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3XUK4; -.
DR Ensembl; ENSPMET00000027982.1; ENSPMEP00000018769.1; ENSPMEG00000021940.1.
DR Proteomes; UP000261480; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 41..320
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 202..218
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 345..356
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 350..403
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 405..414
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 431 AA; 48879 MW; DA11A6461B343EBA CRC64;
MVKQRKNLFP VLGSADTKQT SWPLHPKKPV IFVWNAPTQD CETQERVKLS LDQFDIVSTP
TQGVVGQNLT LFYKERLGIY PYYDTKDTEV NGGIPQSVSL SQHLEQMSKD LDTYIPDHQA
KGVSVINWEE WRPLWVRNWS AKDIYRRKSR ELLNSTLTQG QVATAAKEEF ELSASNFMLE
TLKQAKSLRP NQLWGFYQFP DCYNHNFKGK MDSYTGRCPD VEYERNDQLN WLWNESTALF
PSIYLDPELR STDQGRLFVL SRVKEAMRLA SVGDGLARPV YVYSRPTYNN LVSTIGESVA
LGAAGVIFWG GSSYATSSGC SDLNNYFRGP MGRYLLNVTT AAKECSQKLC KFNGRCLRRA
PDSAVFLHLS PSTHKIISQS GKLKVTGSPG QAELKAFRQH FKCQCYNGTK GESCDGHLDN
FSLNYDEIQK N
//
