FUCO_BOVIN
ID FUCO_BOVIN Reviewed; 468 AA.
AC Q2KIM0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tissue alpha-L-fucosidase;
DE EC=3.2.1.51;
DE AltName: Full=Alpha-L-fucosidase I;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 1;
DE Short=Alpha-L-fucosidase 1;
DE Flags: Precursor;
GN Name=FUCA1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose;
CC Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691; Evidence={ECO:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC Evidence={ECO:0000250|UniProtKB:P04066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC ChEBI:CHEBI:91121; Evidence={ECO:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC Evidence={ECO:0000250|UniProtKB:P04066};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P04066}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR EMBL; BC112588; AAI12589.1; -; mRNA.
DR RefSeq; NP_001039500.1; NM_001046035.2.
DR AlphaFoldDB; Q2KIM0; -.
DR SMR; Q2KIM0; -.
DR STRING; 9913.ENSBTAP00000040572; -.
DR BindingDB; Q2KIM0; -.
DR ChEMBL; CHEMBL3545; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR PaxDb; Q2KIM0; -.
DR PeptideAtlas; Q2KIM0; -.
DR PRIDE; Q2KIM0; -.
DR Ensembl; ENSBTAT00000042970; ENSBTAP00000040572; ENSBTAG00000030434.
DR GeneID; 509522; -.
DR KEGG; bta:509522; -.
DR CTD; 2517; -.
DR VEuPathDB; HostDB:ENSBTAG00000030434; -.
DR VGNC; VGNC:29140; FUCA1.
DR eggNOG; KOG3340; Eukaryota.
DR GeneTree; ENSGT00440000035378; -.
DR HOGENOM; CLU_002934_1_1_1; -.
DR InParanoid; Q2KIM0; -.
DR OMA; LPEHKWE; -.
DR OrthoDB; 929780at2759; -.
DR TreeFam; TF313034; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR PRO; PR:Q2KIM0; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000030434; Expressed in corpus epididymis and 105 other tissues.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:BHF-UCL.
DR GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR GO; GO:0019377; P:glycolipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR028755; FUCA1.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR018526; Glyco_hydro_29_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; PTHR10030; 1.
DR PANTHER; PTHR10030:SF2; PTHR10030:SF2; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF16757; Fucosidase_C; 1.
DR PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism; Lysosome;
KW Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..468
FT /note="Tissue alpha-L-fucosidase"
FT /id="PRO_0000281855"
FT SITE 299
FT /note="May be important for catalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04066"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 468 AA; 54089 MW; E01841FC016A9E38 CRC64;
MRSWVVGARL LLLLQLVLVL GAVRLPPCTD PRHCTDPPRY TPDWPSLDSR PLPAWFDEAK
FGVFVHWGVF SVPAWGSEWF WWHWQGEKLP QYESFMKENY PPDFSYADFG PRFTARFFNP
DSWADLFKAA GAKYVVLTTK HHEGYTNWPS PVSWNWNSKD VGPHRDLVGE LGTAIRKRNI
RYGLYHSLLE WFHPLYLRDK KNGFKTQYFV NAKTMPELYD LVNRYKPDLI WSDGEWECPD
TYWNSTDFLA WLYNDSPVKD EVVVNDRWGQ NCSCHHGGYY NCKDKFQPET LPDHKWEMCT
SIDQRSWGYR RDMEMADITN ESTIISELVQ TVSLGGNYLL NVGPTKDGLI VPIFQERLLA
VGKWLSINGE AIYASKPWRV QSEKNSVWYT SKGLAVYAIL LHWPEYGILS LISPIATSTT
KVTMLGIQKD LKWSLNPSGK GLLVFLPQLP PAALPTEFAW TIKLTGVK
