FUCO_CANLF
ID FUCO_CANLF Reviewed; 465 AA.
AC P48300;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Tissue alpha-L-fucosidase;
DE EC=3.2.1.51;
DE AltName: Full=Alpha-L-fucosidase I;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 1;
DE Short=Alpha-L-fucosidase 1;
DE Flags: Precursor;
GN Name=FUCA1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DISEASE.
RC STRAIN=English Springer spaniel; TISSUE=Blood, and Liver;
RX PubMed=8730282; DOI=10.1136/jmg.33.4.284;
RA Skelly B.J., Sargan D.R., Herrtage M.E., Winchester B.G.;
RT "The molecular defect underlying canine fucosidosis.";
RL J. Med. Genet. 33:284-288(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DISEASE.
RC STRAIN=English Springer spaniel;
RX PubMed=8661697; DOI=10.1007/s003359900081;
RA Occhiodoro T., Anson D.S.;
RT "Isolation of the canine alpha-L-fucosidase cDNA and definition of the
RT fucosidosis mutation in English Springer Spaniels.";
RL Mamm. Genome 7:271-274(1996).
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 -!- 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 -!- 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:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC Evidence={ECO:0000250|UniProtKB:P04066};
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:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC Evidence={ECO:0000250|UniProtKB:P04066};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P04066}.
CC -!- DISEASE: Note=Defects in FUCA1 are the cause of fucosidosis. It is a
CC lysosomal storage disease characterized by accumulation of fucose-
CC containing glycolipids and glycoproteins in various tissues.
CC {ECO:0000269|PubMed:8661697, ECO:0000269|PubMed:8730282}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR EMBL; X92671; CAA63362.1; -; Genomic_DNA.
DR EMBL; X92672; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92673; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92674; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92675; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92676; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92677; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92678; CAA63362.1; JOINED; Genomic_DNA.
DR EMBL; X92448; CAA63197.1; -; mRNA.
DR EMBL; U29765; AAB17403.1; -; mRNA.
DR EMBL; U29766; AAB17401.1; -; Genomic_DNA.
DR RefSeq; NP_001003250.1; NM_001003250.1.
DR AlphaFoldDB; P48300; -.
DR SMR; P48300; -.
DR STRING; 9615.ENSCAFP00000052105; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR PaxDb; P48300; -.
DR GeneID; 403929; -.
DR KEGG; cfa:403929; -.
DR CTD; 2517; -.
DR eggNOG; KOG3340; Eukaryota.
DR InParanoid; P48300; -.
DR OrthoDB; 929780at2759; -.
DR BRENDA; 3.2.1.51; 1153.
DR Proteomes; UP000002254; Unplaced.
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 GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR028755; FUCA1.
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; PTHR10030; 1.
DR PANTHER; PTHR10030:SF2; PTHR10030:SF2; 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; SSF51445; 1.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..465
FT /note="Tissue alpha-L-fucosidase"
FT /id="PRO_0000010307"
FT SITE 296
FT /note="May be important for catalysis"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14..15
FT /note="AV -> LPL (in Ref. 2; AAB17403/AAB17401)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..32
FT /note="AAA -> GPP (in Ref. 2; AAB17403/AAB17401)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="E -> V (in Ref. 2; AAB17403/AAB17401)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="K -> E (in Ref. 2; AAB17403)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="D -> G (in Ref. 1; CAA63197)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> H (in Ref. 2; AAB17403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53757 MW; 832BA3C3510341B7 CRC64;
MKPWAVGLGP PPPAVPLLLL LLLGAALVRA AAPPRRYTPD WQSLDSRPLP DWFDKAKFGV
FVHWGEFAVP AWGSEWFWWH WKGEGLPQYE QFMSENYPPG FSYADFGPQF TARFFHPDTW
ADLFQAAGAR YVVLTTKHHE GFTNWPSSVS WNWNSNDVGP HRDLVGELGR ALRKRNIRYG
LYHSLLEWFH PLYLLDKKNN FKTQFFVRAK TMPELYDLVN RYEPDLIWSD GEWKCPDTYW
NSTEFLSWLY NDSPVKDHVV VNDRWGQNCS CHHGGYYNCQ DKYKPESLPD LKWEMCTSID
KVSWGYRRNM VMSDVASECE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLSIGK
WLSINGEAIY ASKPWRVQLE KNTTSVWYTS RGMTVYAIFL RWPENGVLSL KSPVTTSTTQ
ITMLGIQKDL KWSTEPEGLL IYLPQLSLFT LPVEFGWTIK LTGVE
