ID   FUCO_MACFA              Reviewed;         468 AA.
AC   Q60HF8; Q4R563;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 71.
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; ORFNames=QccE-17330;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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}.
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; AB125169; BAD51957.1; -; mRNA.
DR   EMBL; AB169681; BAE01762.1; -; mRNA.
DR   AlphaFoldDB; Q60HF8; -.
DR   SMR; Q60HF8; -.
DR   STRING; 9541.ENSMFAP00000008915; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GlyCosmos; Q60HF8; 3 sites, No reported glycans.
DR   eggNOG; KOG3340; Eukaryota.
DR   BRENDA; 3.2.1.51; 1793.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
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; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF2; TISSUE ALPHA-L-FUCOSIDASE; 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; (Trans)glycosidases; 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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..468
FT                   /note="Tissue alpha-L-fucosidase"
FT                   /id="PRO_0000010309"
FT   SITE            298
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT   MOD_RES         172
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04066"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  54127 MW;  847FFF17AEC7109E CRC64;
     MRAPGERWRP AGAALWLLLL LLLLGATESV RRAQPLRRYT PDWPSLDSRP LPSWFDEAKF
     GVFIHWGVFS VPAWGSEWFW WNWQGEGRPQ YQRFMRDNYP PGSSYADFGP QFTARFFHPE
     EWADLFQAAG AKYVVLTTKH HEGFTNWPSP VSWNWNSKDV GPHRDLVGEL GTALRKRNIR
     YGLYHSLLEW FHPLYLLDKK NGFKTQYFVG AKTMPELYDL VNSYKPDLIW SDGEWECPDT
     YWNSTNFLSW LYNDSPVKDE VVVNDRWGQN CSCHHGGYYN CEDKFKPQSL PDHKWEMCTS
     IDKFSWGYRR DMAMSDVTEE SEIISELVQT VSLGGNYLLN IGPTKDGLIV PIFQERLLAL
     GKWLSINGEA IYASKPWRVQ WEKNTTSVWY TSKGSAVYAI FLHWPENGVL NLESPITTST
     TKIMMLRIQG DLKWSTDPDK GLLISLPQLP PSAVPAEFAW TIKLTGVK
//