FUCO_RAT
ID FUCO_RAT Reviewed; 462 AA.
AC P17164; Q642C6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 140.
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; Synonyms=Fuca;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-40; 90-124 AND
RP 307-372.
RC TISSUE=Liver;
RX PubMed=2482732; DOI=10.1042/bj2640695;
RA Fisher K.J., Aronson N.N. Jr.;
RT "Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-
RT fucosidase.";
RL Biochem. J. 264:695-701(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P04066}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR EMBL; X16145; CAA34268.1; -; mRNA.
DR EMBL; BC081844; AAH81844.1; -; mRNA.
DR PIR; S07074; S10235.
DR RefSeq; NP_036694.2; NM_012562.2.
DR AlphaFoldDB; P17164; -.
DR SMR; P17164; -.
DR IntAct; P17164; 1.
DR STRING; 10116.ENSRNOP00000012455; -.
DR BindingDB; P17164; -.
DR ChEMBL; CHEMBL2710; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR GlyGen; P17164; 3 sites.
DR jPOST; P17164; -.
DR PaxDb; P17164; -.
DR PRIDE; P17164; -.
DR GeneID; 24375; -.
DR KEGG; rno:24375; -.
DR UCSC; RGD:2636; rat.
DR CTD; 2517; -.
DR RGD; 2636; Fuca1.
DR eggNOG; KOG3340; Eukaryota.
DR InParanoid; P17164; -.
DR OrthoDB; 929780at2759; -.
DR PhylomeDB; P17164; -.
DR TreeFam; TF313034; -.
DR BRENDA; 3.2.1.51; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SABIO-RK; P17164; -.
DR PRO; PR:P17164; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0015928; F:fucosidase activity; IDA:RGD.
DR GO; GO:0006004; P:fucose metabolic process; ISO:RGD.
DR GO; GO:0016139; P:glycoside catabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Lipid metabolism; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2482732"
FT CHAIN 29..462
FT /note="Tissue alpha-L-fucosidase"
FT /id="PRO_0000010311"
FT SITE 292
FT /note="May be important for catalysis"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="D -> E (in Ref. 2; AAH81844)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="R -> K (in Ref. 2; AAH81844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 53487 MW; B9B06B62E6019C15 CRC64;
MWDLKSEWWA VGFGLLLLLA ASAQAGGLAP HHYTPDWPSL DSRPLPRWFD EAKFGLFVHW
GVYSVPAWGS EWFWWHWQGE QSSAYVRFMK ENYPPGFSYA DFAPQFTARF FHPEEWADLF
QAAGAKYVVL TAKHHEGFTN WPSAVSWNWN SKDVGPHRDL VGELGAAVRK RNIRYGLYHS
LFEWFHPLYL LDKKNGLKTQ HFVSTKTMPE LYDLVNRYKP DLIWSDGEWE CPDSYWNSTE
FLAWLYNESP VKDQVVVNDR WGQNCSCRHG GYYNCEDKYR PHSLPDHKWE MCTSVDKASW
GYRRDMSMST IVDENEIIEE LVQTISLGGN YLLNIGPNKD GVIVPIFQER LLAVGKWLQI
NGEAIYASKP WRVQSERNKT VVWYTTKDSA VYATFLHWPE DGVVNLQSPK MTSATKITML
GMEGELHWTQ DPLEGVLITL PQLPPGTFPV ESAWTLKLTK VN
