ID A0A3B1JHA9_ASTMX Unreviewed; 456 AA.
AC A0A3B1JHA9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alpha-L-fucosidase {ECO:0000256|PIRNR:PIRNR001092};
DE EC=3.2.1.51 {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:ENSAMXP00000040699.1, 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:ENSAMXP00000040699.1}
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=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; A0A3B1JHA9; -.
DR STRING; 7994.ENSAMXP00000040699; -.
DR Ensembl; ENSAMXT00000033025.1; ENSAMXP00000040699.1; ENSAMXG00000040084.1.
DR GeneTree; ENSGT00440000035378; -.
DR InParanoid; A0A3B1JHA9; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000040084; Expressed in intestine and 14 other cell types or tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF2; TISSUE 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.
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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Signal {ECO:0000256|PIRNR:PIRNR001092}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT CHAIN 28..456
FT /note="Alpha-L-fucosidase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT /id="PRO_5017107579"
FT DOMAIN 375..453
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 289
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 456 AA; 52270 MW; 0A01E842BA9DA642 CRC64;
MGSAAPLSLL LLNAVLLLLS SVSGSTARYT PDWKSLDARP LPSWYDQSKF GIFIHWGVFS
VPSFGSEWFW WYWKGQKIPG YIWFMDKNYP PGFEYAEFAP GFKAEFWDPD EWAEIFEASG
AKYIVFTSKH HEGFTNWGSP TSWNWNSVDN GPHRDIVGEL ATAVRKRKSV HFGLYHSLFE
WFHPLYLSDK ASNFTKQDFV SSKVMPEFYD LVTRYKPELI WSDGDWEAPD TYWNSTEFLA
WLYNDSPVKD VIVVNDRWGQ GCYCKHGGYY NCADKYTPTE PPKHKWEKCN SMDKYSWGYR
RNMKFSDVLD LPAIIQDFVY TVALGGNYLL NIGPASDGKI PIVFEERLRS IGAWLKINGE
AIYGTKPWRL STENGTVPVW YTSTDSAVYA IFLTNPGQYS FQLFTPVTSE KTVVTLLGIP
DPLKWAPLHS SGLVMLLPEL PYTPAQAWVI KMQGVA
//
