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Database: UniProt
Entry: K6ZCA9_PANTR
LinkDB: K6ZCA9_PANTR
Original site: K6ZCA9_PANTR 
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}.
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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
//
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