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Database: UniProt
Entry: F1MTV1_BOVIN
LinkDB: F1MTV1_BOVIN
Original site: F1MTV1_BOVIN 
ID   F1MTV1_BOVIN            Unreviewed;       553 AA.
AC   F1MTV1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
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   Name=SPAM1 {ECO:0000313|Ensembl:ENSBTAP00000006089.3};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000006089.3, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000006089.3, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000006089.3,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000006089.3}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000006089.3};
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|PIRNR:PIRNR038193, 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   RefSeq; NP_001008413.3; NM_001008413.3.
DR   RefSeq; XP_005205684.1; XM_005205627.3.
DR   AlphaFoldDB; F1MTV1; -.
DR   SMR; F1MTV1; -.
DR   STRING; 9913.ENSBTAP00000006089; -.
DR   GlyCosmos; F1MTV1; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000006089; -.
DR   Ensembl; ENSBTAT00000006089.4; ENSBTAP00000006089.3; ENSBTAG00000004640.4.
DR   GeneID; 353352; -.
DR   KEGG; bta:353352; -.
DR   CTD; 6677; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004640; -.
DR   eggNOG; ENOG502R6HD; Eukaryota.
DR   GeneTree; ENSGT01020000230364; -.
DR   HOGENOM; CLU_036366_0_1_1; -.
DR   InParanoid; F1MTV1; -.
DR   OMA; PLWEQNW; -.
DR   OrthoDB; 5344684at2759; -.
DR   TreeFam; TF321598; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000004640; Expressed in spermatid and 91 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IBA:GO_Central.
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   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   InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF20; HYALURONIDASE PH-20; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 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   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:UP000009136};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..553
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003267600"
FT   REGION          477..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        60..353
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        225..239
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        378..389
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        383..437
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        439..445
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   553 AA;  62281 MW;  63B68C2A38B6DB35 CRC64;
     MRMLRRHHIS FRSFAGSSGT PQAVFTFLLL PCCLALDFRA PPLISNTSFL WAWNAPVERC
     VNRRFQLPPD LRLFSVKGSP QKSATGQFIT LFYADRLGYY PHIDEKTGKT VFGGIPQLGN
     LKSHLEKAKN DIAYYIPNDS VGLAVIDWEN WRPTWARNWK PKDVYRDESV ELVLQKNPQL
     SFPEASKIAK VDFETAGKSF MQETLKLGKL LRPNHLWGYY LFPDCYNHNH NQPTYNGNCP
     DVEKRRNDDL EWLWKESTAL FPSVYLNIRL KSTQNAALYV RNRVQEAIRL SKIASVESPL
     PVFVYARPVF TDGSSTYLSQ GDLVNSVGEI VSLGASGIIM WGSLNLSLSM QSCMNLGTYL
     NTTLNPYIIN VTLAAKMCSQ VLCHNEGVCT RKHWNSSDYL HLNPMNFAIQ TGEGGKYTVP
     GTVTLEDLQK FSDTFYCSCY ANIHCKKRVD IKNVHSVNVC MAEDICIDSP VKLQPSDHSS
     SQEASTTTFS SISPSTTTAT VSPCTPEKHS PECLKVRCSE VIPNVTQKAC QSVKLKNISY
     QSPIQNIKNQ TTY
//
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