ID   FUCO2_RAT               Reviewed;         459 AA.
AC   Q6AYS4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
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   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 [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   -!- 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; BC078933; AAH78933.1; -; mRNA.
DR   RefSeq; NP_001004218.1; NM_001004218.1.
DR   AlphaFoldDB; Q6AYS4; -.
DR   SMR; Q6AYS4; -.
DR   STRING; 10116.ENSRNOP00000020946; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GlyGen; Q6AYS4; 3 sites.
DR   jPOST; Q6AYS4; -.
DR   PaxDb; Q6AYS4; -.
DR   PRIDE; Q6AYS4; -.
DR   GeneID; 292485; -.
DR   KEGG; rno:292485; -.
DR   UCSC; RGD:1303053; rat.
DR   CTD; 2519; -.
DR   RGD; 1303053; Fuca2.
DR   VEuPathDB; HostDB:ENSRNOG00000015551; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   HOGENOM; CLU_002934_1_1_1; -.
DR   InParanoid; Q6AYS4; -.
DR   OMA; WESTDKH; -.
DR   OrthoDB; 929780at2759; -.
DR   PhylomeDB; Q6AYS4; -.
DR   TreeFam; TF313034; -.
DR   BRENDA; 3.2.1.51; 5301.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q6AYS4; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015551; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6AYS4; RN.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:RGD.
DR   GO; GO:0006004; P:fucose metabolic process; ISO:RGD.
DR   GO; GO:0016139; P:glycoside catabolic process; ISO:RGD.
DR   GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..459
FT                   /note="Plasma alpha-L-fucosidase"
FT                   /id="PRO_0000010315"
FT   SITE            286
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTY2"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   459 AA;  53258 MW;  EB194E6F811D851B CRC64;
     MRLGLLMFLP LLLLATRYRA VTALSYDPTW ESLDRRPLPA WFDQAKFGIF IHWGVFSVPS
     FGSEWFWWYW QKERRPKFVD FMDNNYPPGF KYEDFGVLFT AKYFNANQWA DLLQASGAKY
     VVLTSKHHEG FTLWGSAHSW NWNAVDEGPK RDIVKELEVA VRNRTDLHFG LYYSLFEWFH
     PLFLEDQSSA FQKQRFPVAK TLPELYELVT KYQPEVLWSD GDGGAPDHYW NSTDFLAWLY
     NESPVRDTVV TNDRWGAGSI CKHGGYYTCS DRYNPGHLLP HKWENCMTID KFSWGYRREA
     EIGDYLTIEE LVKQLVETVS CGGNLLMNIG PTLDGIIPVI FEERLRQMGT WLKVNGEAIY
     ETHTWRSQND TVTPDVWYTS KPEKKLVYAI FLKWPISGKL FLGQPIGSLG ETEVELLGHG
     RPLTWTSSKP SGIVVELPRL SVHQMPCKWG WTLALTNVT