ID   FUCO_BRAFL              Reviewed;         449 AA.
AC   C3YWU0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Alpha-L-fucosidase;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase;
DE   Flags: Precursor;
GN   ORFNames=BRAFLDRAFT_56888;
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82;
RX   PubMed=18563158; DOI=10.1038/nature06967;
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEN55334.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GG666561; EEN55334.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002599322.1; XM_002599276.1.
DR   AlphaFoldDB; C3YWU0; -.
DR   SMR; C3YWU0; -.
DR   STRING; 7739.C3YWU0; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   InParanoid; C3YWU0; -.
DR   Proteomes; UP000001554; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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:SF46; ALPHA-L-FUCOSIDASE-RELATED; 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   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..449
FT                   /note="Alpha-L-fucosidase"
FT                   /id="PRO_0000406973"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  51880 MW;  932A818CAAF41315 CRC64;
     MGLLLLLSLL SACFQPRYAP TWDSLDQRPL PSWYDEAKFG IFMHWGVFSV PSFGSEWFWW
     DWKGAHDQNF IKDFMKRNYP PGFRYADFAP MFTAEWYNPL QWAEVLQASG AKYVVLTSKH
     HEGFTNWPSK YSWNWNSVDN GPHRDLVGEL AMAIRNNSDL HFGLYYSLFE WFHPLYLKDK
     QNKWTTQDYT KDVGLAELYE LVNAYHPEVV WSDGDWEAPY TYWNSTNFLA WLYNDSPVKD
     TVVTNDRWGS GMLCHHGGYY TCSDRYNPGV LQKHKWENCM TIDKKSWGFR REATLADYLD
     MDDLVKILAE TVSCGGNLLM NIGPTHDGRI VPIFEERLRS MGKWLQVNGD AIYATKPWRA
     QNDTRESGVW YTSKNDSVYA IVLDWPNSGQ LTLGVPRSSP TTTVTMLGWA APLKWVAVSG
     SGITVQMPTA SSNQLPCQWA WVIRMKGVM
//