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P48300 (FUCO_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:FUCA1
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Lysosome.

Involvement in disease

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 componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfucose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-fucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 465439Tissue alpha-L-fucosidase
PRO_0000010307

Sites

Site2961May be important for catalysis

Amino acid modifications

Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict14 – 152AV → LPL in AAB17403. Ref.2
Sequence conflict14 – 152AV → LPL in AAB17401. Ref.2
Sequence conflict30 – 323AAA → GPP in AAB17403. Ref.2
Sequence conflict30 – 323AAA → GPP in AAB17401. Ref.2
Sequence conflict661E → V in AAB17403. Ref.2
Sequence conflict661E → V in AAB17401. Ref.2
Sequence conflict2341K → E in AAB17403. Ref.2
Sequence conflict2571D → G in CAA63197. Ref.1
Sequence conflict2911L → H in AAB17403. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48300 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 832BA3C3510341B7

FASTA46553,757
        10         20         30         40         50         60 
MKPWAVGLGP PPPAVPLLLL LLLGAALVRA AAPPRRYTPD WQSLDSRPLP DWFDKAKFGV 

        70         80         90        100        110        120 
FVHWGEFAVP AWGSEWFWWH WKGEGLPQYE QFMSENYPPG FSYADFGPQF TARFFHPDTW 

       130        140        150        160        170        180 
ADLFQAAGAR YVVLTTKHHE GFTNWPSSVS WNWNSNDVGP HRDLVGELGR ALRKRNIRYG 

       190        200        210        220        230        240 
LYHSLLEWFH PLYLLDKKNN FKTQFFVRAK TMPELYDLVN RYEPDLIWSD GEWKCPDTYW 

       250        260        270        280        290        300 
NSTEFLSWLY NDSPVKDHVV VNDRWGQNCS CHHGGYYNCQ DKYKPESLPD LKWEMCTSID 

       310        320        330        340        350        360 
KVSWGYRRNM VMSDVASECE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLSIGK 

       370        380        390        400        410        420 
WLSINGEAIY ASKPWRVQLE KNTTSVWYTS RGMTVYAIFL RWPENGVLSL KSPVTTSTTQ 

       430        440        450        460 
ITMLGIQKDL KWSTEPEGLL IYLPQLSLFT LPVEFGWTIK LTGVE 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE.
Strain: English Springer spaniel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92671 expand/collapse EMBL AC list , X92672, X92673, X92674, X92675, X92676, X92677, X92678 Genomic DNA. Translation: CAA63362.1.
X92448 mRNA. Translation: CAA63197.1.
U29765 mRNA. Translation: AAB17403.1.
U29766 Genomic DNA. Translation: AAB17401.1.
RefSeqNP_001003250.1. NM_001003250.1.
UniGeneCfa.3785.

3D structure databases

ProteinModelPortalP48300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000019256.

Protein family/group databases

CAZyGH29. Glycoside Hydrolase Family 29.

Proteomic databases

PaxDbP48300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403929.
KEGGcfa:403929.

Organism-specific databases

CTD2517.

Phylogenomic databases

eggNOGCOG3669.
HOGENOMHOG000029598.
HOVERGENHBG002155.
InParanoidP48300.
KOK01206.

Enzyme and pathway databases

BRENDA3.2.1.51. 1154.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR016286. FUC_metazoa-typ.
IPR028755. FUCA1.
IPR013780. Glyco_hydro_13_b.
IPR000933. Glyco_hydro_29.
IPR018526. Glyco_hydro_29_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10030. PTHR10030. 1 hit.
PTHR10030:SF2. PTHR10030:SF2. 1 hit.
PfamPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSPR00741. GLHYDRLASE29.
SMARTSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00385. ALPHA_L_FUCOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20817420.

Entry information

Entry nameFUCO_CANFA
AccessionPrimary (citable) accession number: P48300
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries