ID A0A091CLA4_FUKDA Unreviewed; 1217 AA.
AC A0A091CLA4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Hyaluronidase {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
GN ORFNames=H920_19990 {ECO:0000313|EMBL:KFO18562.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18562.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18562.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18562.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}. Secreted
CC {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 EMBL; KN125357; KFO18562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CLA4; -.
DR STRING; 885580.ENSFDAP00000009186; -.
DR eggNOG; ENOG502QUYI; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR018155; Hyaluronidase.
DR InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF23; HYALURONIDASE-1; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF01630; Glyco_hydro_56; 2.
DR PIRSF; PIRSF038193; Hyaluronidase; 2.
DR PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 2.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR038193};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1217
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001872436"
FT DOMAIN 992..1143
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1160..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 632
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 544..834
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 708..722
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 859..870
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 1217 AA; 136961 MW; A0B7F70B0DAD6408 CRC64;
MQAGLRPTIT MALVLAVAWA MELKPTVPPI FTGRPFVVAW DVPTQDCGPR HKVLLDLKAF
DVEASPNEGF VNQSITIFYY DRLGLYPHFN AAGTSIHGGV PQNGSLQEHL GMLKKPVEHY
IRTREPAGLA VIDWEHWRPV WVRNWQDKDV YRQWSRQLVA SRHPDWPKDR IVKQAQYEFE
FAARQFMLKT LHYVKSVRPQ HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW
LWAESTALFP SVYLDETLAS SVHGRNFVSF RVQEALRVAQ SHHGNHALPV YVFTRPTYTH
TSRLTGLSEM DLVSTIGESA ALGAAGVILW GDTSSMETCQ YLQNYLTDLL VPYVINVSWA
TQYCSRAQCH GHGRCVRRNP TSNTFLHLNT SSFRLVPGRA PDEPQLRPEG ELSWADLNYL
RTHFRCQCYL GWGGEQCQDH GRAAGAQSFQ QLLFLRNLLE QLGHCVELNL AKISLGSHPL
GQEIWKMRPF SPEVSPHPPR VVTAHLLRIC TLFLTLLDMT PSSRAPVVPN QPFITVWNAD
TQQCLEKYSV DVDISVFDVV ANPGQTFLGP NMTIFYSSKL GTYPYYTATG EPVFGGLPQN
ASLSEHLAYA FYDIQAAMPA PDFSGLVVID WEAWRPRWAF NWDTKDIYRQ RSQALIQAQH
PDWPESRVKT VAKEQFQEAA KAWMAGTLQL GQTLHPRGLW GFYGLPDCYN YDFKSPNYTG
QCPFGISPEN DQLGWLWNQS QALYPSIYIP ADLIGTGITQ RYVRHRVGEA FRVARTSRNT
SLPVLPYVQI FYDTTNHLLP LEELEHTLGE SAAQGAAGVV FWVSSEDTNS KESCQAIKEY
MDTTLGPFIL NVTSGALLCS QALCSGHGRC ARRPSHPEAL LILNPDSFSI QFTPGGKPLS
LKDPAPWMEL ILSTSLAKLT LNLVYQREVA LRFNLTTSTL DPTHQPELIL NPRIAELTLD
SRTFSPGPAE LTLDSKHQLE DTPAPRLAEL TLEPVHCRPE LMDACADLIN DQWPRSRASR
LHSLGQSSDA FPLCLLLLNP HPRSEAAPIV VGHARLSRVL DRPQSLLVET VVIARALRGR
GFGRRLMEGL EDFARVRGFR RLHLTTHDQL YFYSHLGYHL GEPVQGLVFS SQRLPTSLLR
ALPRAPTSNP PCMVPSLTVQ AAAPSSPKGP PLPPPPPLPQ SLTTLPSPPA GPFPQNLLET
QYQDLRGCPI FWMEKDI
//
