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P48300

- FUCO_CANFA

UniProt

P48300 - FUCO_CANFA

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Protein

Tissue alpha-L-fucosidase

Gene

FUCA1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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
Sitei296 – 2961May be important for catalysis

GO - Molecular functioni

  1. alpha-L-fucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. fucose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.51. 1154.

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
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 465439Tissue alpha-L-fucosidasePRO_0000010307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP48300.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000019256.

Structurei

3D structure databases

ProteinModelPortaliP48300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 29 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3669.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiP48300.
KOiK01206.

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.

P48300-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPWAVGLGP PPPAVPLLLL LLLGAALVRA AAPPRRYTPD WQSLDSRPLP
60 70 80 90 100
DWFDKAKFGV FVHWGEFAVP AWGSEWFWWH WKGEGLPQYE QFMSENYPPG
110 120 130 140 150
FSYADFGPQF TARFFHPDTW ADLFQAAGAR YVVLTTKHHE GFTNWPSSVS
160 170 180 190 200
WNWNSNDVGP HRDLVGELGR ALRKRNIRYG LYHSLLEWFH PLYLLDKKNN
210 220 230 240 250
FKTQFFVRAK TMPELYDLVN RYEPDLIWSD GEWKCPDTYW NSTEFLSWLY
260 270 280 290 300
NDSPVKDHVV VNDRWGQNCS CHHGGYYNCQ DKYKPESLPD LKWEMCTSID
310 320 330 340 350
KVSWGYRRNM VMSDVASECE IISELVQTVS LGGNYLLNIG PTKDGLIVPI
360 370 380 390 400
FQERLLSIGK WLSINGEAIY ASKPWRVQLE KNTTSVWYTS RGMTVYAIFL
410 420 430 440 450
RWPENGVLSL KSPVTTSTTQ ITMLGIQKDL KWSTEPEGLL IYLPQLSLFT
460
LPVEFGWTIK LTGVE
Length:465
Mass (Da):53,757
Last modified:February 1, 1996 - v1
Checksum:i832BA3C3510341B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152AV → LPL in AAB17403. (PubMed:8661697)Curated
Sequence conflicti14 – 152AV → LPL in AAB17401. (PubMed:8661697)Curated
Sequence conflicti30 – 323AAA → GPP in AAB17403. (PubMed:8661697)Curated
Sequence conflicti30 – 323AAA → GPP in AAB17401. (PubMed:8661697)Curated
Sequence conflicti66 – 661E → V in AAB17403. (PubMed:8661697)Curated
Sequence conflicti66 – 661E → V in AAB17401. (PubMed:8661697)Curated
Sequence conflicti234 – 2341K → E in AAB17403. (PubMed:8661697)Curated
Sequence conflicti257 – 2571D → G in CAA63197. (PubMed:8730282)Curated
Sequence conflicti291 – 2911L → H in AAB17403. (PubMed:8661697)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92671
, 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.
RefSeqiNP_001003250.1. NM_001003250.1.
UniGeneiCfa.3785.

Genome annotation databases

GeneIDi403929.
KEGGicfa:403929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92671
, 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 .
RefSeqi NP_001003250.1. NM_001003250.1.
UniGenei Cfa.3785.

3D structure databases

ProteinModelPortali P48300.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000019256.

Protein family/group databases

CAZyi GH29. Glycoside Hydrolase Family 29.

Proteomic databases

PaxDbi P48300.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403929.
KEGGi cfa:403929.

Organism-specific databases

CTDi 2517.

Phylogenomic databases

eggNOGi COG3669.
HOGENOMi HOG000029598.
HOVERGENi HBG002155.
InParanoidi P48300.
KOi K01206.

Enzyme and pathway databases

BRENDAi 3.2.1.51. 1154.

Miscellaneous databases

NextBioi 20817420.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR016286. 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 ]
PANTHERi PTHR10030. PTHR10030. 1 hit.
PTHR10030:SF2. PTHR10030:SF2. 1 hit.
Pfami PF01120. Alpha_L_fucos. 1 hit.
[Graphical view ]
PIRSFi PIRSF001092. Alpha-L-fucosidase. 1 hit.
PRINTSi PR00741. GLHYDRLASE29.
SMARTi SM00812. Alpha_L_fucos. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00385. ALPHA_L_FUCOSIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiFUCO_CANFA
AccessioniPrimary (citable) accession number: P48300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 93 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, 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