ID K6ZCA9_PANTR Unreviewed; 466 AA.
AC K6ZCA9; A0A2J8K3W1; A0A8I3B2S0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Alpha-L-fucosidase {ECO:0000256|PIRNR:PIRNR001092};
DE EC=3.2.1.51 {ECO:0000256|PIRNR:PIRNR001092};
GN Name=FUCA1 {ECO:0000313|EMBL:JAA25683.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA25683.1};
RN [1] {ECO:0000313|EMBL:JAA25683.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02191.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA40710.1}, Skin {ECO:0000313|EMBL:JAA25683.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA19070.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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=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 -!- 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|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR001092}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GABC01009147; JAA02191.1; -; mRNA.
DR EMBL; GABF01003075; JAA19070.1; -; mRNA.
DR EMBL; GABD01007417; JAA25683.1; -; mRNA.
DR EMBL; GABE01004029; JAA40710.1; -; mRNA.
DR RefSeq; XP_016811787.1; XM_016956298.1.
DR AlphaFoldDB; K6ZCA9; -.
DR STRING; 9598.ENSPTRP00000086955; -.
DR GeneID; 469222; -.
DR KEGG; ptr:469222; -.
DR CTD; 2517; -.
DR OrthoDB; 2955544at2759; -.
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; 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 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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR001092}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT CHAIN 28..466
FT /note="Alpha-L-fucosidase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT /id="PRO_5014579996"
FT DOMAIN 378..463
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 296
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 466 AA; 53804 MW; 71F3B5D945B3B2DD CRC64;
MRAPGMRSRP AGPALLLLLL FLEAAESVRR AQPRRRYTPD WPSLDSRPLP AWFDEAKFGV
FIHWGVFSVP AWGSEWFWWH WQGEGRPQYQ RFMRDNYPPG FSYADFGPQF TARFFHPEEW
ADLFQAAGAK YVVLTTKHHE GFTNWPSPVS WNWNSKDVGP HRDLVGELGT ALRKRNIRYG
LYHSLLEWFH PLYLLDKKNG FKTQHFVSAK TMPELYDLVN SYKPDLIWSD GEWECPDTYW
NSTNFLSWLY NDSPVKDEVV VNDRWGQNCS CHHGGYYNCE DKFKPQSLPD HKWEMCTSID
KFSWGYRRDM AMSDVTEESE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLAVGK
WLSINGEAIY ASKPWRVQWE KNTTSVWYTS KGSAVYAIFL HWPENGVLNL ESPITTSTTK
ITMLGIQGDL KWSTDPDKGL LISLPQLPPS AVPAEFAWTI KLTGVK
//