ID   Q505Q3_MOUSE            Unreviewed;       461 AA.
AC   Q505Q3;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662, ECO:0000256|PIRNR:PIRNR001092};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662, ECO:0000256|PIRNR:PIRNR001092};
GN   Name=Fuca2 {ECO:0000313|EMBL:AAH94449.1, ECO:0000313|MGI:MGI:1914098};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH94449.1};
RN   [1] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:AAH94449.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH94449.1};
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH94449.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
RN   [7] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE27052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30201.1}, and DBA/2
RC   {ECO:0000313|EMBL:BAE27052.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30201.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; BC094449; AAH94449.1; -; mRNA.
DR   EMBL; AK146295; BAE27052.1; -; mRNA.
DR   EMBL; AK151204; BAE30201.1; -; mRNA.
DR   EMBL; AK159288; BAE34964.1; -; mRNA.
DR   RefSeq; NP_001317127.1; NM_001330198.1.
DR   RefSeq; NP_080075.2; NM_025799.5.
DR   RefSeq; XP_006512890.1; XM_006512827.3.
DR   AlphaFoldDB; Q505Q3; -.
DR   SMR; Q505Q3; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   PeptideAtlas; Q505Q3; -.
DR   Antibodypedia; 33149; 383 antibodies from 28 providers.
DR   DNASU; 66848; -.
DR   GeneID; 66848; -.
DR   KEGG; mmu:66848; -.
DR   AGR; MGI:1914098; -.
DR   CTD; 2519; -.
DR   MGI; MGI:1914098; Fuca2.
DR   VEuPathDB; HostDB:ENSMUSG00000019810; -.
DR   HOGENOM; CLU_002934_1_1_1; -.
DR   OMA; CLIGNNH; -.
DR   OrthoDB; 2955544at2759; -.
DR   BioGRID-ORCS; 66848; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Fuca2; mouse.
DR   ExpressionAtlas; Q505Q3; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:Ensembl.
DR   GO; GO:0016139; P:glycoside catabolic process; IEA:Ensembl.
DR   GO; GO:2000535; P:regulation of entry of bacterium into host cell; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
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:SF45; PLASMA 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   1: Evidence at protein level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001092};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001092};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR001092}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT   CHAIN           26..461
FT                   /note="Alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT                   /id="PRO_5014309461"
FT   DOMAIN          370..457
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
FT   SITE            288
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ   SEQUENCE   461 AA;  53645 MW;  1E232FE5ED6A3C1F CRC64;
     MRLGFLMLLP LLLLPLLRPW GVTRALSYDP TWESLDRRPL PAWFDQAKFG IFIHWGVFSV
     PSFGSEWFWW YWQKEKKPQF VDFMNNNYAP GFKYEDFVVL FTAKYFNANQ WADILQASGA
     KYVVFTSKHH EGFTMWGSDR SWNWNAVDEG PKRDIVKELE VAVRNRTGLH FGLYYSLFEW
     FHPLFLEDQS SSFQKQRFPV SKTLPELYEL VNRYQPEVLW SDGDGGAPDH YWNSTGFLAW
     LYNESPVRKT VVTNDRWGVG SICKHGGYYT CSDRYNPGYL LPHKWENCMT IDKFSWGYRR
     EAEISDYLTI EELVKKLVET VACGGNLLMN IGPTGDGTIP VIFEERLRQM GTWLKVNGEA
     IYETHTWRSQ NDTVTPDVWY TSKPEKKLVY AIFLKWPISG KLFLGQPIGS LGETEVELLG
     HWQPLTWTSS QPSGITVELP LLSVHQMPCK WGWTLVLSNV I
//