ID A0A3B1ILY9_ASTMX Unreviewed; 453 AA.
AC A0A3B1ILY9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662, ECO:0000256|PIRNR:PIRNR001092};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662, ECO:0000256|PIRNR:PIRNR001092};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000030731.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000030731.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00004071,
CC ECO:0000256|PIRNR:PIRNR001092}.
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 -!- 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:0000256|PIRNR:PIRNR001092};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR001092}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
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DR AlphaFoldDB; A0A3B1ILY9; -.
DR STRING; 7994.ENSAMXP00000030731; -.
DR Ensembl; ENSAMXT00000035172.1; ENSAMXP00000030731.1; ENSAMXG00000040132.1.
DR GeneTree; ENSGT00440000035378; -.
DR InParanoid; A0A3B1ILY9; -.
DR OrthoDB; 2955544at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000040132; Expressed in intestine and 14 other cell types or tissues.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-UniRule.
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:SF45; PLASMA 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 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:UP000018467};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR001092}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT CHAIN 21..453
FT /note="Alpha-L-fucosidase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT /id="PRO_5017107431"
FT DOMAIN 364..450
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 453 AA; 51960 MW; CBCBC9941743A2EA CRC64;
MGAGNLCVLS LFLLMGSCLC QYQPNWDSID SRPVPEWFDQ AKLGIFIHWG VFSVPSYGSE
WFWWYWQGRK IPDYVSFMTK NFAPGFQYQD FAPKFTAEFF DPKQWMDIFS ASGAKYIVLT
SKHHEGYTLW GSKYSWNWNA VDVGPKRDLV DEIATALRKN TDLRLGLYHS QFEWFHPLFR
ADAANNFKTN VFATEKSLPE LYELINKYKP ELLWSDGDGD APDQYWNSTG FLAWLYNESP
VRETIVTNDR WGKGSICTHG GYYTCTDRYS PGHLLKHKWE SCMSIDKRSW GFRREAALSD
YLTIEELLKS FIETVSCGGN LLMNVGPTHD GRIVPVFEER LRQMGQWLKV NGEGIYNTTA
WRVQNDSVTP GVWYTSKPQD KAVYAFLLSW PDKGSVVLAD PIVSASTQVV LVGNKPLKFD
VLKPTGLQVY LPTLTPNEMP CSWAWTLRLT GIA
//
