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Database: UniProt
Entry: V5H5I0_IXORI
LinkDB: V5H5I0_IXORI
Original site: V5H5I0_IXORI 
ID   V5H5I0_IXORI            Unreviewed;       461 AA.
AC   V5H5I0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB69537.1};
RN   [1] {ECO:0000313|EMBL:JAB69537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB69537.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
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DR   EMBL; GANP01014931; JAB69537.1; -; mRNA.
DR   AlphaFoldDB; V5H5I0; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001092};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001092};
KW   Signal {ECO:0000256|PIRNR:PIRNR001092}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT   CHAIN           20..461
FT                   /note="alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT                   /id="PRO_5016196528"
FT   DOMAIN          364..458
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
SQ   SEQUENCE   461 AA;  53454 MW;  79FBC385BE3B9207 CRC64;
     MMQGSLLLLF LASLGSTSSR RYTPDWKSLD TRPSPSWFDE AKVGIFLHWG VFSVPSFKSE
     WFWSEWSNKD PEVVEFMRQN YKPNFTYPEF APQFTAQFFD PDRWADLFYK SGARYVVLTS
     KHHEGYTLWP SSVSWNWNAG DVGPKRDLVG DLATAIRKKG GGVHFGLYHS LYEWFNPLYL
     ADKAARWTTN DFVVRKTMPE LREIVERYKP DVIWSDGDWE ANDTYWNSTE FLAWLYNDSP
     VKSSVVVNDR WGIGIPCHHG DFYNCHDRYN PGILLKHKWE NAMTIDKHSW GYRRNANLSD
     YLSIEKLIEE LASTVSCNGN ILINIGPTKD GIIEPVFEER LLQLGRWLGV NGEAVYGSKP
     WKHQNDTLTP GIWYTTNKDM DVVYVFVLRW PRFNKLTLES LVLSQRARIT MLGLNDDLFQ
     WDRTGGSDDS SRRTVTILFP PLTPDLLPTP WAWVLKVEGA L
//
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