FUCO_MOUSE
ID FUCO_MOUSE Reviewed; 452 AA.
AC Q99LJ1; B1AV51; Q3UAH8; Q8BN13; Q9DD22;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tissue alpha-L-fucosidase;
DE EC=3.2.1.51;
DE AltName: Full=Alpha-L-fucosidase I;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 1;
DE Short=Alpha-L-fucosidase 1;
DE Flags: Precursor;
GN Name=Fuca1; Synonyms=Fuca;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, Colon, Eye, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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:0000250}.
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 -!- 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:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC Evidence={ECO:0000250|UniProtKB:P04066};
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:0000250|UniProtKB:P04066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC Evidence={ECO:0000250|UniProtKB:P04066};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P04066}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR EMBL; AK002230; BAB21949.1; -; mRNA.
DR EMBL; AK053323; BAC35346.1; -; mRNA.
DR EMBL; AK089958; BAC41012.1; -; mRNA.
DR EMBL; AK151258; BAE30247.1; -; mRNA.
DR EMBL; AK151361; BAE30336.1; -; mRNA.
DR EMBL; AK151879; BAE30765.1; -; mRNA.
DR EMBL; AK151908; BAE30789.1; -; mRNA.
DR EMBL; AK165604; BAE38288.1; -; mRNA.
DR EMBL; AL672076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003235; AAH03235.1; -; mRNA.
DR CCDS; CCDS18794.1; -.
DR RefSeq; NP_077205.3; NM_024243.4.
DR AlphaFoldDB; Q99LJ1; -.
DR SMR; Q99LJ1; -.
DR STRING; 10090.ENSMUSP00000030434; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR GlyGen; Q99LJ1; 4 sites.
DR iPTMnet; Q99LJ1; -.
DR PhosphoSitePlus; Q99LJ1; -.
DR EPD; Q99LJ1; -.
DR jPOST; Q99LJ1; -.
DR MaxQB; Q99LJ1; -.
DR PaxDb; Q99LJ1; -.
DR PRIDE; Q99LJ1; -.
DR ProteomicsDB; 271642; -.
DR Antibodypedia; 30233; 306 antibodies from 29 providers.
DR DNASU; 71665; -.
DR Ensembl; ENSMUST00000030434; ENSMUSP00000030434; ENSMUSG00000028673.
DR GeneID; 71665; -.
DR KEGG; mmu:71665; -.
DR UCSC; uc008vhi.2; mouse.
DR CTD; 2517; -.
DR MGI; MGI:95593; Fuca1.
DR VEuPathDB; HostDB:ENSMUSG00000028673; -.
DR eggNOG; KOG3340; Eukaryota.
DR GeneTree; ENSGT00440000035378; -.
DR HOGENOM; CLU_002934_1_1_1; -.
DR InParanoid; Q99LJ1; -.
DR OMA; LPEHKWE; -.
DR OrthoDB; 929780at2759; -.
DR PhylomeDB; Q99LJ1; -.
DR TreeFam; TF313034; -.
DR BRENDA; 3.2.1.51; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SABIO-RK; Q99LJ1; -.
DR BioGRID-ORCS; 71665; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fuca1; mouse.
DR PRO; PR:Q99LJ1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99LJ1; protein.
DR Bgee; ENSMUSG00000028673; Expressed in prostate gland ventral lobe and 257 other tissues.
DR Genevisible; Q99LJ1; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0015928; F:fucosidase activity; ISO:MGI.
DR GO; GO:0006004; P:fucose metabolic process; ISO:MGI.
DR GO; GO:0016139; P:glycoside catabolic process; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR028755; FUCA1.
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 PANTHER; PTHR10030:SF2; PTHR10030:SF2; 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 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..452
FT /note="Tissue alpha-L-fucosidase"
FT /id="PRO_0000010310"
FT SITE 282
FT /note="May be important for catalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 379
FT /note="A -> T (in Ref. 1; BAC41012)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="L -> F (in Ref. 1; BAB21949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 52281 MW; 41B319A040152B2C CRC64;
MLLLLLLLLV AAAQAVALAP RRFTPDWQSL DSRPLPSWFD EAKFGVFVHW GVFSVPAWGS
EWFWWHWQGD RMPAYQRFMT ENYPPGFSYA DFAPQFTARF FHPDQWAELF QAAGAKYVVL
TTKHHEGFTN WPSPVSWNWN SKDVGPHRDL VGELGAAVRK RNIRYGLYHS LLEWFHPLYL
LDKKNGFKTQ HFVRAKTMPE LYDLVNSYKP DLIWSDGEWE CPDTYWNSTS FLAWLYNDSP
VKDEVIVNDR WGQNCSCHHG GYYNCQDKYK PQSLPDHKWE MCTSMDRASW GYRKDMTMST
IAKENEIIEE LVQTVSLGGN YLLNIGPTKD GLIVPIFQER LLAVGKWLQI NGEAIYASKP
WRVQSEKNKT VVWYTTKNAT VYATFLYWPE NGIVNLKSPK TTSATKITML GLEGDLSWTQ
DPLEGVLISL PQLPPTVLPV EFAWTLKLTK VN
