ID   FUCO_CAEEL              Reviewed;         482 AA.
AC   P49713;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Putative alpha-L-fucosidase;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase;
DE   Flags: Precursor;
GN   ORFNames=W03G11.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR   EMBL; Z67738; CAA91546.2; -; Genomic_DNA.
DR   PIR; T26127; T26127.
DR   RefSeq; NP_510020.2; NM_077619.3.
DR   AlphaFoldDB; P49713; -.
DR   SMR; P49713; -.
DR   STRING; 6239.W03G11.3.1; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   EPD; P49713; -.
DR   PaxDb; 6239-W03G11-3; -.
DR   PeptideAtlas; P49713; -.
DR   EnsemblMetazoa; W03G11.3.1; W03G11.3.1; WBGene00012225.
DR   GeneID; 189173; -.
DR   KEGG; cel:CELE_W03G11.3; -.
DR   UCSC; W03G11.3; c. elegans.
DR   AGR; WB:WBGene00012225; -.
DR   WormBase; W03G11.3; CE37417; WBGene00012225; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   GeneTree; ENSGT00440000035378; -.
DR   HOGENOM; CLU_002934_1_2_1; -.
DR   InParanoid; P49713; -.
DR   OMA; GKIDIMW; -.
DR   OrthoDB; 2955544at2759; -.
DR   PhylomeDB; P49713; -.
DR   BRENDA; 3.2.1.51; 1045.
DR   Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-CEL-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR   PRO; PR:P49713; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00012225; Expressed in adult organism and 3 other cell types or tissues.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IBA:GO_Central.
DR   GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR   GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR018526; Glyco_hydro_29_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 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   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..482
FT                   /note="Putative alpha-L-fucosidase"
FT                   /id="PRO_0000010316"
FT   SITE            276
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   482 AA;  56460 MW;  8818D452AD261A5D CRC64;
     MIFLIFSILF LHLANCDYTP DWESLDNRPL PSWYDDSKFG IFCHWGLYSV PAFRSEWMWW
     YWKGTQPDKD VVNFVDKNYK PGTTYADFAK DFTAEYFNAN QFAETVKTSG ARYFVFTSKH
     HEGFTMWPSR TSWNWNSMDI GPKRDIVGEL RDAFKKTDVH FGLYFSQFEW FHPMFLDDGK
     FNTTFYPEQV SYPQMIDIVT KYNPEVVWSD GEWDKSDDYW KAKEFLAWLY NSSPVKDQVV
     VNDRWGTGTM GKHGGFMTYS DHYDPGKLLE KKWENCMTLD KHSWGNRRDM KASEVNTAYE
     IIEQLARTIA CNGNLLLNVG PNMHGQIPAI FEDRLEEIGR FVNITSEAIF GTRPWIHQND
     TSASNVWYTS KYSSGKKPLK NLYQNVYNFQ LEEHTIVYAW ILDTSHEQFE LKSVKTTKNT
     TATILGTDVV LTGFEESDSM IILSSKIDWK KLPRRDIIVL KIEKAASYLR NPLMSTNEHH
     VQ
//