ID   FUCO2_PONAB             Reviewed;         465 AA.
AC   Q5RFI5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Plasma alpha-L-fucosidase;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase 2;
DE            Short=Alpha-L-fucosidase 2;
DE   Flags: Precursor;
GN   Name=FUCA2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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.
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR   EMBL; CR857171; CAH89472.1; -; mRNA.
DR   RefSeq; NP_001127152.1; NM_001133680.2.
DR   AlphaFoldDB; Q5RFI5; -.
DR   SMR; Q5RFI5; -.
DR   STRING; 9601.ENSPPYP00000019105; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GeneID; 100174203; -.
DR   KEGG; pon:100174203; -.
DR   CTD; 2519; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   InParanoid; Q5RFI5; -.
DR   OrthoDB; 929780at2759; -.
DR   BRENDA; 3.2.1.51; 9017.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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   Gene3D; 2.60.40.1180; -; 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; PTHR10030; 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; Phosphoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..465
FT                   /note="Plasma alpha-L-fucosidase"
FT                   /id="PRO_0000010314"
FT   SITE            292
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTY2"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  53963 MW;  820A0284528A8CEE CRC64;
     MRPQELPRLA FPLLLLLLLP PPPCPAHSAT RFDPTWESLD ARQLPAWFDQ AKFGIFIHWG
     VFSVPSFGSE WFWWYWQKEK IPKYVEFMKD NYPPSFKYED FGPLFTAKFF NANQWADIFQ
     ASGAKYIVLT SKHHKGFTLW GSEYSWNWNA IDEGPKRDIV KELEVAIRNR TDLRFGLYYS
     LFEWFHPLFL EDESSSFHKR QFPVSKTLPE LYELVNNYQP EVLWSDGDGG APDQYWNSTG
     FLAWLYNESP VRETVVTNDR WGAGSIYKHG GFYTCSDRYN PGHLLPHKWE NCMTIDKLSW
     GYRREAGISD YLTIEELVKQ LVETVSCGGN LLMNIGPTLD GTISVVFEER LRQMGSWLKV
     NGEAIYETHT WQSQNDTVTP DVWYTSKPKE KLVYAIFLKW PTSGQLFLGQ PKAILGATEV
     KLLGHGQPLN WISLERNGIM VELPQLTIHQ MPCKWGWALA LTNVI