P48300 (FUCO_CANFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 77.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tissue alpha-L-fucosidase EC=3.2.1.51 Alternative name(s): Alpha-L-fucosidase I Alpha-L-fucoside fucohydrolase 1 Short name=Alpha-L-fucosidase 1 | ||
| Gene names |
| ||
| Organism | Canis familiaris (Dog) (Canis lupus familiaris) | ||
| Taxonomic identifier | 9615 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis |
Protein attributes
| Sequence length | 465 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. |
| Catalytic activity | An alpha-L-fucoside + H2O = L-fucose + an alcohol. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Involvement in disease | Note=Defects in FUCA1 are the cause of fucosidosis. It is a lysosomal storage disease characterized by accumulation of fucose-containing glycolipids and glycoproteins in various tissues. Ref.1 Ref.2 |
| Sequence similarities | Belongs to the glycosyl hydrolase 29 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Lysosome |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fucose metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alpha-L-fucosidase activity Inferred from electronic annotation. Source: EC cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Potential | ||||||
| Chain | 27 – 465 | 439 | Tissue alpha-L-fucosidase | PRO_0000010307 | |||||
Sites | |||||||||
| Site | 296 | 1 | May be important for catalysis | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 241 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 268 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 382 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 14 – 15 | 2 | AV → LPL in AAB17403. Ref.2 | ||||||
| Sequence conflict | 14 – 15 | 2 | AV → LPL in AAB17401. Ref.2 | ||||||
| Sequence conflict | 30 – 32 | 3 | AAA → GPP in AAB17403. Ref.2 | ||||||
| Sequence conflict | 30 – 32 | 3 | AAA → GPP in AAB17401. Ref.2 | ||||||
| Sequence conflict | 66 | 1 | E → V in AAB17403. Ref.2 | ||||||
| Sequence conflict | 66 | 1 | E → V in AAB17401. Ref.2 | ||||||
| Sequence conflict | 234 | 1 | K → E in AAB17403. Ref.2 | ||||||
| Sequence conflict | 257 | 1 | D → G in CAA63197. Ref.1 | ||||||
| Sequence conflict | 291 | 1 | L → H in AAB17403. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The molecular defect underlying canine fucosidosis." Skelly B.J., Sargan D.R., Herrtage M.E., Winchester B.G. J. Med. Genet. 33:284-288(1996) [PubMed: 8730282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE. Strain: English Springer spaniel. Tissue: Blood and Liver. |
| [2] | "Isolation of the canine alpha-L-fucosidase cDNA and definition of the fucosidosis mutation in English Springer Spaniels." Occhiodoro T., Anson D.S. Mamm. Genome 7:271-274(1996) [PubMed: 8661697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE. Strain: English Springer spaniel. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X92671 X92678 Genomic DNA. Translation: CAA63362.1.X92448 mRNA. Translation: CAA63197.1. U29765 mRNA. Translation: AAB17403.1. U29766 Genomic DNA. Translation: AAB17401.1. |
| RefSeq | NP_001003250.1. NM_001003250.1. |
| UniGene | Cfa.3785. |
3D structure databases | |
| ProteinModelPortal | P48300. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P48300. |
Protein family/group databases | |
| CAZy | GH29. Glycoside Hydrolase Family 29. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 403929. |
| KEGG | cfa:403929. |
Organism-specific databases | |
| CTD | 2517. |
Phylogenomic databases | |
| eggNOG | maNOG11538. |
| GeneTree | ENSGT00440000035378. |
| HOVERGEN | HBG002155. |
| InParanoid | P48300. |
| OrthoDB | EOG4BRWKH. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.51. 1154. |
Family and domain databases | |
| InterPro | IPR000933. Glyco_hydro_29. IPR018526. Glyco_hydro_29_CS. IPR016286. Glyco_hydro_29_sub. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| KO | K01206. |
| PANTHER | PTHR10030. Glyco_hydro_29. 1 hit. |
| Pfam | PF01120. Alpha_L_fucos. 1 hit. [Graphical view] |
| PIRSF | PIRSF001092. Alpha-L-fucosidase. 1 hit. |
| PRINTS | PR00741. GLHYDRLASE29. |
| SMART | SM00812. Alpha_L_fucos. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00385. ALPHA_L_FUCOSIDASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FUCO_CANFA | ||||||||
| Accession | Primary (citable) accession number: P48300 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with