ID I3MR46_ICTTR Unreviewed; 333 AA.
AC I3MR46;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=HYAL2 {ECO:0000313|Ensembl:ENSSTOP00000014515.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000014515.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000014515.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01046208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MR46; -.
DR Ensembl; ENSSTOT00000016216.3; ENSSTOP00000014515.3; ENSSTOG00000016213.3.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_2_0_1; -.
DR TreeFam; TF321598; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..333
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012858962"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT DISULFID 211..227
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 333 AA; 38108 MW; FEC4A99EB3F859B0 CRC64;
MLAGLGPTIT LALVLAVAWA MELKPTVPPI FTGRPFVVAW DVPTQDCAPR HKVPLDLSAF
DVEASPNEGF VNQNITIFYY DRLGLYPRFD STGTSVHGGV PQNVNLRAHL QMLKKPVEHY
IRTQEPAGLA VIDWEDWRPV WVRNWQDKDV YRQSSRQLVA SRHPDWPSDR IVKQAQYEFE
SNARQFMLET LRYVKAVRPR HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW
LWAESTALFP SVYLDETLAS SAHGRNFVSF RVQEALRVAH THHANHALPV YVFTRPTYTR
KLTGLSKVCS FQGAAFFLLL GTTGSIPSTT KIK
//
