ID F6RLC0_HORSE Unreviewed; 481 AA.
AC F6RLC0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=HYAL4 {ECO:0000313|Ensembl:ENSECAP00000024169.1,
GN ECO:0000313|VGNC:VGNC:56029};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000024169.1, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000024169.1, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000024169.1,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000024169.1}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000024169.1};
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 RefSeq; XP_001502439.1; XM_001502389.3.
DR AlphaFoldDB; F6RLC0; -.
DR SMR; F6RLC0; -.
DR STRING; 9796.ENSECAP00000024169; -.
DR GlyCosmos; F6RLC0; 1 site, No reported glycans.
DR PaxDb; 9796-ENSECAP00000024169; -.
DR Ensembl; ENSECAT00000063012.2; ENSECAP00000024169.1; ENSECAG00000024782.4.
DR VGNC; VGNC:56029; HYAL4.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; F6RLC0; -.
DR OMA; AGQDINY; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000002281; Chromosome 4.
DR Bgee; ENSECAG00000024782; Expressed in chorionic villus and 3 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030207; P:chondroitin sulfate catabolic process; IEA:Ensembl.
DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
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:UP000002281}.
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 59..351
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 223..237
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 376..387
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 381..435
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 437..446
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 481 AA; 54699 MW; 68C582A3C8826579 CRC64;
MKLLSEGQFR FCVVQPIHLT SWLLIFFILK SISSLKPARL PIYQRKPFIA AWNAPTDQCL
IKYNIRLNLK MFQVIGSPLA KARGQNVTIF YVNRLGYYPW YTSQGVPVNG GLPQNISLQV
HLEKADEDIN YYIPAEDFSG LAVIDWEYWR PQWARNWNTK DVYRQKSRKL ISDMQENVSA
TDIEYLAKAT FEESAKAFMK ETIELGIKSR PKGLWGYYLY PDCHNYNVYD PNYTGSCPEE
EVLRNNELSW LWNSSAALYP SIGVRKSLGD SENILRFSQF RVHESMRIST MTSHDYALPV
FVYTRLGYRD EPLFFLSKQD LISTIGESAA LGAAGFVIWG DMNLTSSEGN CTKVKQFVSS
VLGRYIVNVT RAAEACSLHL CRNNGRCLRK VWKAPDYLHL NPASYYIEAS EDGEFIVEGK
ASDTDLALMA EKFSCQCYQG YEGADCREMK TADGCSGLPS FSGSLITLCP LFLAGYQSIQ
L
//
