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Database: UniProt
Entry: A0A2K6CTA0_MACNE
LinkDB: A0A2K6CTA0_MACNE
Original site: A0A2K6CTA0_MACNE 
ID   A0A2K6CTA0_MACNE        Unreviewed;       435 AA.
AC   A0A2K6CTA0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN   Name=HYAL1 {ECO:0000313|Ensembl:ENSMNEP00000026881.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000026881.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000026881.1}
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   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; A0A2K6CTA0; -.
DR   STRING; 9545.ENSMNEP00000026881; -.
DR   GlyCosmos; A0A2K6CTA0; 1 site, No reported glycans.
DR   Ensembl; ENSMNET00000051169.1; ENSMNEP00000026881.1; ENSMNEG00000036864.1.
DR   GeneTree; ENSGT01020000230364; -.
DR   OMA; KEFSCQC; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000036864; Expressed in liver and 10 other cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0036117; C:hyaluranon cable; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0052757; F:chondroitin hydrolase activity; IEA:Ensembl.
DR   GO; GO:0050501; F:hyaluronan synthase activity; IEA:Ensembl.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0071493; P:cellular response to UV-B; IEA:Ensembl.
DR   GO; GO:0030207; P:chondroitin sulfate catabolic process; IEA:Ensembl.
DR   GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR   GO; GO:0030213; P:hyaluronan biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
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:SF23; HYALURONIDASE-1; 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   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..435
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014472789"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        43..333
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        207..221
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        358..369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        363..418
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        420..429
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   435 AA;  48456 MW;  C1237FE82BB89BDD CRC64;
     MAAHLLPICT LFLTLLDMAQ GSRGPLLPNR PFATVWNANT QWCLERHSVD VDVSIFDVVA
     NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP
     DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPVTQVEAV AQDQFQGAAR
     AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR
     ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDMTNHFLPL
     DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN VTSGALLCSQ
     ALCSSHGRCV RRPSHPKALL ILNPASFSIQ LTPDGGPLSL RGALSLEDQA QMAVEFKCRC
     YPGWQGPWCE QKSMW
//
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