FUCO_MACFA
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 25-MAY-2022, entry version 68.
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.XP_005544511.1; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
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; 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..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
