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Database: UniProt
Entry: V4B5U1_LOTGI
LinkDB: V4B5U1_LOTGI
Original site: V4B5U1_LOTGI 
ID   V4B5U1_LOTGI            Unreviewed;       457 AA.
AC   V4B5U1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN   ORFNames=LOTGIDRAFT_230702 {ECO:0000313|EMBL:ESP01432.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP01432.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESP01432.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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.
CC       {ECO:0000256|ARBA:ARBA00004071}.
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:0000256|ARBA:ARBA00000419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC         Evidence={ECO:0000256|ARBA:ARBA00000419};
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:0000256|ARBA:ARBA00000321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC         Evidence={ECO:0000256|ARBA:ARBA00000321};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
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DR   EMBL; KB200521; ESP01432.1; -; Genomic_DNA.
DR   RefSeq; XP_009048066.1; XM_009049818.1.
DR   AlphaFoldDB; V4B5U1; -.
DR   EnsemblMetazoa; LotgiT230702; LotgiP230702; LotgiG230702.
DR   GeneID; 20248380; -.
DR   KEGG; lgi:LOTGIDRAFT_230702; -.
DR   CTD; 20248380; -.
DR   HOGENOM; CLU_002934_1_1_1; -.
DR   OMA; GKIDIMW; -.
DR   OrthoDB; 2955544at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001092};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR001092}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT   CHAIN           19..457
FT                   /note="alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT                   /id="PRO_5016197110"
FT   DOMAIN          364..453
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
FT   SITE            282
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ   SEQUENCE   457 AA;  53030 MW;  204409682DEA9C26 CRC64;
     MKWDVFNICL FLLSLCNAVR YEPNWKSIDS RPLPSWYDQG KIGIFIHWGV FSVPSFSTEW
     FWWQWKGSPP VPGVEAFMKD NYKPGFTYAD FAPEFTAEFY NPNEWAELFN ASGAQYVVLT
     TKHHEGFCNW HTNYSWNWNS MSTGPNRDLV GDLADAIRKY TDMRFGVYHS LFEWFNPLYL
     QDQANNYQTQ KFVESKTLPE LYELVNTYKP DLIWSDGDWM VSSDYWNATQ FLAWLYNDSP
     VKDYIIVNDR WGNDSRCKHG GFLDCSDSFD PGTLQKRKWE NCMHLDKYSW GYRRNMKIDD
     VLSMVDLLSE MMETISCGGN ILINIGPTKS GEIIPVFQER LRSMGDWLKV NGEAIYGSVP
     WSHQNDTVTR GIWYTSKKGP EGRIVYASIS SWPEKDQLFL GAPKPTASTK VTLLGYPQQF
     EFKPGPSGGI TLSIPVISIF DMPCQWVWIF KMEGLKN
//
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