ID   FUCO_DROME              Reviewed;         494 AA.
AC   Q9VTJ4; A4V1U8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Putative alpha-L-fucosidase;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase;
DE   Flags: Precursor;
GN   Name=Fuca; ORFNames=CG6128;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|EMBL:AAM50292.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   HOMOLOGY.
RX   PubMed=11698403; DOI=10.1074/jbc.m107927200;
RA   Roos C., Kolmer M., Mattila P., Renkonen R.;
RT   "Composition of Drosophila melanogaster proteome involved in fucosylated
RT   glycan metabolism.";
RL   J. Biol. Chem. 277:3168-3175(2002).
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:0000250|UniProtKB:P04066}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the cysteine thought to be important for catalysis. It
CC       is replaced by Ala-288. {ECO:0000305}.
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DR   EMBL; AE014296; AAO41255.1; -; Genomic_DNA.
DR   EMBL; AY119638; AAM50292.1; -; mRNA.
DR   RefSeq; NP_001303363.1; NM_001316434.1.
DR   RefSeq; NP_648472.1; NM_140215.3.
DR   AlphaFoldDB; Q9VTJ4; -.
DR   SMR; Q9VTJ4; -.
DR   DIP; DIP-19942N; -.
DR   STRING; 7227.FBpp0312400; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GlyCosmos; Q9VTJ4; 2 sites, No reported glycans.
DR   GlyGen; Q9VTJ4; 2 sites.
DR   PaxDb; 7227-FBpp0100046; -.
DR   DNASU; 3772574; -.
DR   EnsemblMetazoa; FBtr0100588; FBpp0100046; FBgn0285958.
DR   EnsemblMetazoa; FBtr0346860; FBpp0312400; FBgn0285958.
DR   GeneID; 3772574; -.
DR   KEGG; dme:Dmel_CG6128; -.
DR   UCSC; CG6128-RA; d. melanogaster.
DR   AGR; FB:FBgn0285958; -.
DR   CTD; 3772574; -.
DR   FlyBase; FBgn0285958; Fuca.
DR   VEuPathDB; VectorBase:FBgn0285958; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   GeneTree; ENSGT00440000035378; -.
DR   HOGENOM; CLU_002934_1_1_1; -.
DR   InParanoid; Q9VTJ4; -.
DR   OMA; WESTDKH; -.
DR   OrthoDB; 2955544at2759; -.
DR   PhylomeDB; Q9VTJ4; -.
DR   BRENDA; 3.2.1.51; 1994.
DR   Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-DME-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR   BioGRID-ORCS; 3772574; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Fuca; fly.
DR   GenomeRNAi; 3772574; -.
DR   PRO; PR:Q9VTJ4; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0285958; Expressed in invertebrate nurse cell and 19 other cell types or tissues.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0002081; C:outer acrosomal membrane; IDA:FlyBase.
DR   GO; GO:0097524; C:sperm plasma membrane; IDA:FlyBase.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:FlyBase.
DR   GO; GO:0042806; F:fucose binding; IDA:FlyBase.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:FlyBase.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR   GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; NAS:UniProtKB.
DR   GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
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; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 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   Genevisible; Q9VTJ4; DM.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..494
FT                   /note="Putative alpha-L-fucosidase"
FT                   /id="PRO_0000010318"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  57723 MW;  96E0B3C893E45F56 CRC64;
     MAISAWMPLL VALIVVWISA AEVDAQVPGP RTRYQPNWAS LDQRPLPQWY DDAKVGIFLH
     YGVYSVPSFG SEWFWTNWKN LRNPEYVQFM QRNYKPDFTY QEFASQFTAE LFNATKWALL
     FKDSGARYVV LTSKHHDGFT LWPSKNSYGW NSMDVGPKRD IVKELAAAIR KESDLRFGLY
     YSLFEWFNPL WTDDKLHLLM QQHFVERKVR PEQMELVQQY LPEIIWSDGD WEAPAKYWRS
     EEFIAWLYND SPVRDTVVTN DRWGFGTACM HGDFYNCADR FNPGVLQAHK WENAFTLDRT
     SWGQRFDVSL SDFMTSKEVI KEIITTVSCN GNVLINVGPT KFGTILPIFE ERLRDMGRWL
     KFNGEGIYGS VPWIYQNDTI NGNVWYTRQK EASNGKITIY AFVLEYPYDT NELDIYPLGK
     DINIFRNVML TGIDMGTGGD ILNEQSTEVV MLGMEDTKIK WNADHNRLHI VFPPKNHIDK
     RGLDYAWTFK ITIT
//