Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tissue alpha-L-fucosidase

Gene

Fuca1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

An alpha-L-fucoside + H2O = L-fucose + an alcohol.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei292 – 2921May be important for catalysis

GO - Molecular functioni

  • alpha-L-fucosidase activity Source: UniProtKB
  • carbohydrate binding Source: RGD
  • fucosidase activity Source: RGD

GO - Biological processi

  • fucose metabolic process Source: UniProtKB
  • glycoside catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.51. 5301.
SABIO-RKP17164.

Protein family/group databases

CAZyiGH29. Glycoside Hydrolase Family 29.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Fuca1
Synonyms:Fuca
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2636. Fuca1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • lysosome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 462434Tissue alpha-L-fucosidasePRO_0000010311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP17164.
PRIDEiP17164.

Expressioni

Gene expression databases

GenevisibleiP17164. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP17164. 1 interaction.
STRINGi10116.ENSRNOP00000012455.

Structurei

3D structure databases

ProteinModelPortaliP17164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 29 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3669.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiP17164.
KOiK01206.
OrthoDBiEOG7DC249.
PhylomeDBiP17164.
TreeFamiTF313034.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR016286. 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]
PANTHERiPTHR10030. PTHR10030. 1 hit.
PTHR10030:SF2. PTHR10030:SF2. 1 hit.
PfamiPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFiPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSiPR00741. GLHYDRLASE29.
SMARTiSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00385. ALPHA_L_FUCOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWDLKSEWWA VGFGLLLLLA ASAQAGGLAP HHYTPDWPSL DSRPLPRWFD
60 70 80 90 100
EAKFGLFVHW GVYSVPAWGS EWFWWHWQGE QSSAYVRFMK ENYPPGFSYA
110 120 130 140 150
DFAPQFTARF FHPEEWADLF QAAGAKYVVL TAKHHEGFTN WPSAVSWNWN
160 170 180 190 200
SKDVGPHRDL VGELGAAVRK RNIRYGLYHS LFEWFHPLYL LDKKNGLKTQ
210 220 230 240 250
HFVSTKTMPE LYDLVNRYKP DLIWSDGEWE CPDSYWNSTE FLAWLYNESP
260 270 280 290 300
VKDQVVVNDR WGQNCSCRHG GYYNCEDKYR PHSLPDHKWE MCTSVDKASW
310 320 330 340 350
GYRRDMSMST IVDENEIIEE LVQTISLGGN YLLNIGPNKD GVIVPIFQER
360 370 380 390 400
LLAVGKWLQI NGEAIYASKP WRVQSERNKT VVWYTTKDSA VYATFLHWPE
410 420 430 440 450
DGVVNLQSPK MTSATKITML GMEGELHWTQ DPLEGVLITL PQLPPGTFPV
460
ESAWTLKLTK VN
Length:462
Mass (Da):53,487
Last modified:August 1, 1990 - v1
Checksum:iB9B06B62E6019C15
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31D → E in AAH81844 (PubMed:15489334).Curated
Sequence conflicti377 – 3771R → K in AAH81844 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16145 mRNA. Translation: CAA34268.1.
BC081844 mRNA. Translation: AAH81844.1.
PIRiS07074. S10235.
RefSeqiNP_036694.2. NM_012562.2.
UniGeneiRn.3469.

Genome annotation databases

GeneIDi24375.
KEGGirno:24375.
UCSCiRGD:2636. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16145 mRNA. Translation: CAA34268.1.
BC081844 mRNA. Translation: AAH81844.1.
PIRiS07074. S10235.
RefSeqiNP_036694.2. NM_012562.2.
UniGeneiRn.3469.

3D structure databases

ProteinModelPortaliP17164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17164. 1 interaction.
STRINGi10116.ENSRNOP00000012455.

Chemistry

BindingDBiP17164.
ChEMBLiCHEMBL2710.

Protein family/group databases

CAZyiGH29. Glycoside Hydrolase Family 29.

Proteomic databases

PaxDbiP17164.
PRIDEiP17164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24375.
KEGGirno:24375.
UCSCiRGD:2636. rat.

Organism-specific databases

CTDi2517.
RGDi2636. Fuca1.

Phylogenomic databases

eggNOGiCOG3669.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiP17164.
KOiK01206.
OrthoDBiEOG7DC249.
PhylomeDBiP17164.
TreeFamiTF313034.

Enzyme and pathway databases

BRENDAi3.2.1.51. 5301.
SABIO-RKP17164.

Miscellaneous databases

NextBioi603125.
PROiP17164.

Gene expression databases

GenevisibleiP17164. RN.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR016286. 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]
PANTHERiPTHR10030. PTHR10030. 1 hit.
PTHR10030:SF2. PTHR10030:SF2. 1 hit.
PfamiPF01120. Alpha_L_fucos. 1 hit.
[Graphical view]
PIRSFiPIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSiPR00741. GLHYDRLASE29.
SMARTiSM00812. Alpha_L_fucos. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00385. ALPHA_L_FUCOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase."
    Fisher K.J., Aronson N.N. Jr.
    Biochem. J. 264:695-701(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40; 90-124 AND 307-372.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiFUCO_RAT
AccessioniPrimary (citable) accession number: P17164
Secondary accession number(s): Q642C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 24, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.