ID FUCO_HUMAN Reviewed; 466 AA. AC P04066; B2RBG3; Q14334; Q14335; Q3LID0; Q8NAC2; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 4. DT 24-JAN-2024, entry version 224. DE RecName: Full=Tissue alpha-L-fucosidase {ECO:0000305}; DE EC=3.2.1.51 {ECO:0000305|PubMed:9741689}; 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 {ECO:0000312|HGNC:HGNC:4006}; ORFNames=Nbla10230; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT FUCA1D ASP-65, AND VARIANT RP ARG-286. RX PubMed=8504303; DOI=10.1093/hmg/2.4.423; RA Seo H.-C., Willems P.J., Kretz K.A., Martin B.M., O'Brien J.S.; RT "Fucosidosis: four new mutations and a new polymorphism."; RL Hum. Mol. Genet. 2:423-429(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Neuroblastoma; RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5; RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., RA Hirato J., Nakagawara A.; RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the RT genesis and biology of neuroblastoma."; RL Cancer Lett. 197:63-68(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-286. RC TISSUE=Spleen, and Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-466, AND VARIANT SER-269. RX PubMed=2803312; DOI=10.1016/0006-291x(89)91739-7; RA Occhiodoro T., Beckmann K.R., Morris C.P., Hopwood J.J.; RT "Human alpha-L-fucosidase: complete coding sequence from cDNA clones."; RL Biochem. Biophys. Res. Commun. 164:439-445(1989). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-92. RC TISSUE=Placenta; RX PubMed=2174090; DOI=10.1007/bf01799583; RA Fukushima H., Nishimoto J., Okada S.; RT "Sequencing and expression of a full-length cDNA for human alpha-L- RT fucosidase."; RL J. Inherit. Metab. Dis. 13:761-765(1990). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-427. RX PubMed=2983333; DOI=10.1073/pnas.82.4.1262; RA Fukushima H., de Wet J.R., O'Brien J.S.; RT "Molecular cloning of a cDNA for human alpha-L-fucosidase."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1262-1265(1985). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-426. RX PubMed=6096099; DOI=10.1089/dna.1.1984.3.437; RA de Wet J.R., Fukushima H., Dewji N.N., Wilcox E., O'Brien J.S., RA Helinski D.R.; RT "Chromogenic immunodetection of human serum albumin and alpha-L-fucosidase RT clones in a human hepatoma cDNA expression library."; RL DNA 3:437-447(1984). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-426, AND VARIANT SER-269. RX PubMed=2894306; DOI=10.1159/000469189; RA O'Brien J.S., Willems P.J., Fukushima H., de Wet J.R., Darby J.K., RA Dicioccio R.A., Fowler M.L., Shows T.B.; RT "Molecular biology of the alpha-6L-fucosidase gene and fucosidosis."; RL Enzyme 38:45-53(1987). RN [11] RP STRUCTURE OF CARBOHYDRATES. RA Beem E.P., Lisman J.J.W., van Steijn G.J., van der Wal C.J., RA Trippelvitz L.A.W., Overdijk B., van Halbeek H., Mutsaers J.H.G.M., RA Vliegenthart J.F.G.; RT "Structural analysis of the carbohydrate moieties of alpha-L-fucosidase RT from human liver."; RL Glycoconj. J. 4:33-42(1987). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=9741689; RA Asfaw B., Schindler D., Ledvinova J., Cerny B., Smid F., Conzelmann E.; RT "Degradation of blood group A glycolipid A-6-2 by normal and mutant human RT skin fibroblasts."; RL J. Lipid Res. 39:1768-1780(1998). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241 AND ASN-382. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP VARIANT ARG-286. RX PubMed=8399358; DOI=10.1016/0925-4439(93)90065-9; RA Yang M., Allen H., Dicioccio R.A.; RT "Pedigree analysis of alpha-L-fucosidase gene mutations in a fucosidosis RT family."; RL Biochim. Biophys. Acta 1182:245-249(1993). RN [19] RP VARIANT FUCA1D LEU-68. RX PubMed=7874128; RA Seo H.-C., Yang M., Tonlorenzi R., Willems P.J., Kim A.H., Filocamo M., RA Gatti R., Dicioccio R.A., O'Brien J.S.; RT "A missense mutation (S63L) in alpha-L-fucosidase is responsible for RT fucosidosis in an Italian patient."; RL Hum. Mol. Genet. 3:2065-2066(1994). RN [20] RP VARIANT ARG-286. RX PubMed=7815431; DOI=10.1136/jmg.31.8.659-a; RA Cragg H., Winchester B., Seo H.-C., O'Brien J.S., Swallow D.; RT "Molecular basis of the common electrophoretic polymorphism (Fu1/Fu2) in RT human alpha-L-fucosidase."; RL J. Med. Genet. 31:659-660(1994). RN [21] RP VARIANT FUCA1D ARG-410. RX PubMed=9762612; DOI=10.1023/a:1005405222252; RA Fleming C.J., Sinclair D.U., White E.J., Winchester B., Whiteford M.L., RA Connor J.M.; RT "A fucosidosis patient with relative longevity and a missense mutation in RT exon 7 of the alpha-fucosidase gene."; RL J. Inherit. Metab. Dis. 21:688-689(1998). RN [22] RP REVIEW ON VARIANTS. RX PubMed=10094192; DOI=10.1038/sj.ejhg.5200272; RA Willems P.J., Seo H.-C., Coucke P., Tonlorenzi R., O'Brien J.S.; RT "Spectrum of mutations in fucosidosis."; RL Eur. J. Hum. Genet. 7:60-67(1999). RN [23] RP VARIANTS SER-269 AND ARG-286. RX PubMed=12408193; DOI=10.1023/a:1020116220624; RA Ip P., Goh W., Chan K.W., Cheung P.T.; RT "A novel FUCA1 mutation causing fucosidosis in a Chinese boy."; RL J. Inherit. Metab. Dis. 25:415-416(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:0000269|PubMed:9741689}. 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12289; CC Evidence={ECO:0000305}; 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:0000269|PubMed:9741689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225; CC Evidence={ECO:0000269|PubMed:9741689}; 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:0000269|PubMed:9741689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309; CC Evidence={ECO:0000269|PubMed:9741689}; CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P04066; Q99828: CIB1; NbExp=3; IntAct=EBI-2512153, EBI-372594; CC P04066; Q9BTT4: MED10; NbExp=3; IntAct=EBI-2512153, EBI-394354; CC P04066; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-2512153, EBI-947187; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9741689}. CC -!- POLYMORPHISM: There are two common alleles of FUCA1; FUCA1*1; also CC known as Fu1; has Arg-281 and FUCA1*2; also known as Fu2; has Gln-281. CC -!- DISEASE: Fucosidosis (FUCA1D) [MIM:230000]: An autosomal recessive CC lysosomal storage disease characterized by accumulation of fucose- CC containing glycolipids and glycoproteins in various tissues. Clinical CC signs include facial dysmorphism, dysostosis multiplex, moderate CC hepatomegaly, severe intellectual deficit, deafness, and according to CC age, angiokeratomas. {ECO:0000269|PubMed:7874128, CC ECO:0000269|PubMed:8504303, ECO:0000269|PubMed:9762612}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35519.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAA52481.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH17338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG37210.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA25646.1; Type=Miscellaneous discrepancy; Note=Translation of X01390 sequence produces a larger peptide than that shown in CAA25646.1.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M80815; AAA52481.1; ALT_INIT; Genomic_DNA. DR EMBL; M80809; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; M80810; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; M80811; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; M80812; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; M80813; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; M80814; AAA52481.1; JOINED; Genomic_DNA. DR EMBL; AB074175; BAE45738.1; -; mRNA. DR EMBL; AK092914; BAC04002.1; -; mRNA. DR EMBL; AK314649; BAG37210.1; ALT_INIT; mRNA. DR EMBL; AL590728; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017338; AAH17338.1; ALT_INIT; mRNA. DR EMBL; M29877; AAA35519.1; ALT_INIT; mRNA. DR EMBL; M10355; AAA52482.1; -; mRNA. DR EMBL; X01390; CAA25646.1; ALT_SEQ; mRNA. DR CCDS; CCDS244.2; -. DR PIR; A33427; HWHUFA. DR RefSeq; NP_000138.2; NM_000147.4. DR PDB; 7PLS; EM; 2.49 A; A/B/C/D=32-466. DR PDB; 7PM4; EM; 2.49 A; A/B/C/D=32-466. DR PDBsum; 7PLS; -. DR PDBsum; 7PM4; -. DR AlphaFoldDB; P04066; -. DR EMDB; EMD-13499; -. DR EMDB; EMD-13520; -. DR SMR; P04066; -. DR BioGRID; 108793; 39. DR IntAct; P04066; 17. DR MINT; P04066; -. DR STRING; 9606.ENSP00000363603; -. DR BindingDB; P04066; -. DR ChEMBL; CHEMBL4176; -. DR SwissLipids; SLP:000001407; -. DR CAZy; GH29; Glycoside Hydrolase Family 29. DR GlyConnect; 1810; 6 N-Linked glycans (2 sites). DR GlyCosmos; P04066; 4 sites, 8 glycans. DR GlyGen; P04066; 5 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P04066; -. DR MetOSite; P04066; -. DR PhosphoSitePlus; P04066; -. DR SwissPalm; P04066; -. DR BioMuta; FUCA1; -. DR DMDM; 156631012; -. DR CPTAC; CPTAC-2215; -. DR EPD; P04066; -. DR jPOST; P04066; -. DR MassIVE; P04066; -. DR MaxQB; P04066; -. DR PaxDb; 9606-ENSP00000363603; -. DR PeptideAtlas; P04066; -. DR ProteomicsDB; 51645; -. DR Pumba; P04066; -. DR Antibodypedia; 30233; 337 antibodies from 29 providers. DR DNASU; 2517; -. DR Ensembl; ENST00000374479.4; ENSP00000363603.3; ENSG00000179163.12. DR GeneID; 2517; -. DR KEGG; hsa:2517; -. DR MANE-Select; ENST00000374479.4; ENSP00000363603.3; NM_000147.5; NP_000138.2. DR UCSC; uc001bie.5; human. DR AGR; HGNC:4006; -. DR CTD; 2517; -. DR DisGeNET; 2517; -. DR GeneCards; FUCA1; -. DR HGNC; HGNC:4006; FUCA1. DR HPA; ENSG00000179163; Low tissue specificity. DR MalaCards; FUCA1; -. DR MIM; 230000; phenotype. DR MIM; 612280; gene. DR neXtProt; NX_P04066; -. DR OpenTargets; ENSG00000179163; -. DR Orphanet; 349; Fucosidosis. DR PharmGKB; PA28422; -. DR VEuPathDB; HostDB:ENSG00000179163; -. DR eggNOG; KOG3340; Eukaryota. DR GeneTree; ENSGT00440000035378; -. DR HOGENOM; CLU_002934_1_1_1; -. DR InParanoid; P04066; -. DR OMA; LPEHKWE; -. DR OrthoDB; 2955544at2759; -. DR PhylomeDB; P04066; -. DR TreeFam; TF313034; -. DR BRENDA; 3.2.1.51; 2681. DR PathwayCommons; P04066; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway. DR SABIO-RK; P04066; -. DR SignaLink; P04066; -. DR BioGRID-ORCS; 2517; 15 hits in 1160 CRISPR screens. DR ChiTaRS; FUCA1; human. DR GeneWiki; Fucosidase; -. DR GenomeRNAi; 2517; -. DR Pharos; P04066; Tchem. DR PRO; PR:P04066; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P04066; Protein. DR Bgee; ENSG00000179163; Expressed in mucosa of sigmoid colon and 205 other cell types or tissues. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IBA:GO_Central. DR GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:UniProtKB. DR GO; GO:0006004; P:fucose metabolic process; IDA:UniProtKB. DR GO; GO:0019377; P:glycolipid catabolic process; ISS:BHF-UCL. DR GO; GO:0006027; P:glycosaminoglycan catabolic process; NAS:UniProtKB. DR GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB. 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:SF2; TISSUE 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. DR Genevisible; P04066; HS. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Glycoprotein; Glycosidase; Hydrolase; KW Lipid metabolism; Lysosome; Phosphoprotein; Reference proteome; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..466 FT /note="Tissue alpha-L-fucosidase" FT /id="PRO_0000010308" FT SITE 296 FT /note="May be important for catalysis" FT MOD_RES 170 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 268 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VARIANT 2 FT /note="R -> W (in dbSNP:rs2070955)" FT /id="VAR_049106" FT VARIANT 10 FT /note="P -> R (in dbSNP:rs2070956)" FT /id="VAR_016233" FT VARIANT 65 FT /note="G -> D (in FUCA1D; loss of activity; FT dbSNP:rs1353778985)" FT /evidence="ECO:0000269|PubMed:8504303" FT /id="VAR_002442" FT VARIANT 68 FT /note="S -> L (in FUCA1D)" FT /evidence="ECO:0000269|PubMed:7874128" FT /id="VAR_002443" FT VARIANT 146 FT /note="P -> L (in dbSNP:rs2228424)" FT /id="VAR_049107" FT VARIANT 260 FT /note="V -> I (in dbSNP:rs665)" FT /id="VAR_049108" FT VARIANT 269 FT /note="C -> S (in dbSNP:rs1126512)" FT /evidence="ECO:0000269|PubMed:12408193, FT ECO:0000269|PubMed:2803312, ECO:0000269|PubMed:2894306" FT /id="VAR_016234" FT VARIANT 286 FT /note="Q -> R (in allele FUCA1*2; dbSNP:rs13551)" FT /evidence="ECO:0000269|PubMed:12408193, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:7815431, FT ECO:0000269|PubMed:8399358, ECO:0000269|PubMed:8504303" FT /id="VAR_002444" FT VARIANT 410 FT /note="L -> R (in FUCA1D; less than 1% of residual FT activity; dbSNP:rs80358199)" FT /evidence="ECO:0000269|PubMed:9762612" FT /id="VAR_016235" FT CONFLICT 54..56 FT /note="DEA -> NEV (in Ref. 3; BAC04002)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="S -> T (in Ref. 7; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 76..77 FT /note="WF -> FL (in Ref. 8; AAA52482 and 9; CAA25646)" FT /evidence="ECO:0000305" FT CONFLICT 93..114 FT /note="Missing (in Ref. 3; BAC04002)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="A -> T (in Ref. 3; BAC04002)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="A -> G (in Ref. 3; BAC04002)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="N -> D (in Ref. 3; BAC04002)" FT /evidence="ECO:0000305" FT CONFLICT 427 FT /note="Q -> P (in Ref. 8; AAA52482)" FT /evidence="ECO:0000305" FT HELIX 41..44 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 51..56 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 77..81 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 87..96 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 103..109 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 117..126 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 130..137 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:7PLS" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 164..174 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 178..185 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 191..198 FT /evidence="ECO:0007829|PDB:7PLS" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 205..209 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 211..220 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 242..251 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:7PLS" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 293..300 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 318..330 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 349..365 FT /evidence="ECO:0007829|PDB:7PLS" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:7PLS" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 381..391 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 394..401 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 406..412 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 414..421 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 436..438 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 440..443 FT /evidence="ECO:0007829|PDB:7PLS" FT STRAND 458..466 FT /evidence="ECO:0007829|PDB:7PLS" SQ SEQUENCE 466 AA; 53689 MW; D9A38ECC7BADCBBB CRC64; MRAPGMRSRP AGPALLLLLL FLGAAESVRR AQPPRRYTPD WPSLDSRPLP AWFDEAKFGV FIHWGVFSVP AWGSEWFWWH WQGEGRPQYQ RFMRDNYPPG FSYADFGPQF TARFFHPEEW ADLFQAAGAK YVVLTTKHHE GFTNWPSPVS WNWNSKDVGP HRDLVGELGT ALRKRNIRYG LYHSLLEWFH PLYLLDKKNG FKTQHFVSAK TMPELYDLVN SYKPDLIWSD GEWECPDTYW NSTNFLSWLY NDSPVKDEVV VNDRWGQNCS CHHGGYYNCE DKFKPQSLPD HKWEMCTSID KFSWGYRRDM ALSDVTEESE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLAVGK WLSINGEAIY ASKPWRVQWE KNTTSVWYTS KGSAVYAIFL HWPENGVLNL ESPITTSTTK ITMLGIQGDL KWSTDPDKGL FISLPQLPPS AVPAEFAWTI KLTGVK //