ID D2GWD1_AILME Unreviewed; 463 AA.
AC D2GWD1;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Tissue alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00014025};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
DE AltName: Full=Alpha-L-fucosidase I {ECO:0000256|ARBA:ARBA00031765};
DE AltName: Full=Alpha-L-fucoside fucohydrolase 1 {ECO:0000256|ARBA:ARBA00032971};
DE Flags: Fragment;
GN ORFNames=PANDA_001104 {ECO:0000313|EMBL:EFB27144.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB27144.1};
RN [1] {ECO:0000313|EMBL:EFB27144.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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 -!- 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC {ECO:0000256|ARBA:ARBA00007951}.
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DR EMBL; GL192357; EFB27144.1; -; Genomic_DNA.
DR AlphaFoldDB; D2GWD1; -.
DR InParanoid; D2GWD1; -.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
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; 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: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.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..463
FT /note="Tissue alpha-L-fucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003030602"
FT DOMAIN 376..461
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 294
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB27144.1"
FT NON_TER 463
FT /evidence="ECO:0000313|EMBL:EFB27144.1"
SQ SEQUENCE 463 AA; 53524 MW; 302DDB0561B0C4A7 CRC64;
RTADMKSRAV GPGPRLLLLP LLLLLVLRAA YVRGVQRARR YTPDWQSLDS RPLPDWFDKA
KFGVFVHWGV FSVPAWGSEW FWWHWKGEGL PQYERFMSDN YPPGFSYADF GPQFTARFFH
PETWTDLFQA AGAKYVVLTT KHHEGFTNWP SPVSWNWNSK DVGPHRDLVG ELGKALRKRN
IRYGLYHSLL EWFHPLYSIF FGYYHTNNKL CPHRVSSRYE PDLIWSDGEW ECPDTYWNST
EFLSWLYNDS PVKACDLVVN DRWGQNTSCH HGGYYNCQDK FKPESLPEHK WEMCTSIDRV
SWGFRRNMVM GDIASECEII SELVQTVSLG GNYLLNIGPT KDGLIVPIFQ ERLLAVGKWL
SINGEAIYAS KPWRVQLEKN TTSVWYTSRG AAVYAIFLHW PDDGVLYLAS PVTTSTTQIT
MLGIEKDLKW STDPEEGLLV YLPQLPLFTL PVEIGWTIKL TGV
//
