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Protein

Tissue alpha-L-fucosidase

Gene

Fuca1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei282 – 2821May be important for catalysisPROSITE-ProRule annotation

GO - Molecular functioni

  1. alpha-L-fucosidase activity Source: MGI
  2. fucose binding Source: GO_Central

GO - Biological processi

  1. fucose metabolic process Source: MGI
  2. glycoside catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.51. 3474.
SABIO-RKQ99LJ1.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:95593. Fuca1.

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. lysosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 452435Tissue alpha-L-fucosidasePRO_0000010310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ99LJ1.
PaxDbiQ99LJ1.
PRIDEiQ99LJ1.

PTM databases

PhosphoSiteiQ99LJ1.

Expressioni

Gene expression databases

BgeeiQ99LJ1.
GenevestigatoriQ99LJ1.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030434.

Structurei

3D structure databases

ProteinModelPortaliQ99LJ1.
SMRiQ99LJ1. Positions 22-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 29 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3669.
GeneTreeiENSGT00440000035378.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiQ99LJ1.
KOiK01206.
OMAiNGFKTQH.
OrthoDBiEOG7DC249.
PhylomeDBiQ99LJ1.
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.

Q99LJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLLLLLLV AAAQAVALAP RRFTPDWQSL DSRPLPSWFD EAKFGVFVHW
60 70 80 90 100
GVFSVPAWGS EWFWWHWQGD RMPAYQRFMT ENYPPGFSYA DFAPQFTARF
110 120 130 140 150
FHPDQWAELF QAAGAKYVVL TTKHHEGFTN WPSPVSWNWN SKDVGPHRDL
160 170 180 190 200
VGELGAAVRK RNIRYGLYHS LLEWFHPLYL LDKKNGFKTQ HFVRAKTMPE
210 220 230 240 250
LYDLVNSYKP DLIWSDGEWE CPDTYWNSTS FLAWLYNDSP VKDEVIVNDR
260 270 280 290 300
WGQNCSCHHG GYYNCQDKYK PQSLPDHKWE MCTSMDRASW GYRKDMTMST
310 320 330 340 350
IAKENEIIEE LVQTVSLGGN YLLNIGPTKD GLIVPIFQER LLAVGKWLQI
360 370 380 390 400
NGEAIYASKP WRVQSEKNKT VVWYTTKNAT VYATFLYWPE NGIVNLKSPK
410 420 430 440 450
TTSATKITML GLEGDLSWTQ DPLEGVLISL PQLPPTVLPV EFAWTLKLTK

VN
Length:452
Mass (Da):52,281
Last modified:June 1, 2001 - v1
Checksum:i41B319A040152B2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti379 – 3791A → T in BAC41012. (PubMed:16141072)Curated
Sequence conflicti396 – 3961L → F in BAB21949. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002230 mRNA. Translation: BAB21949.1.
AK053323 mRNA. Translation: BAC35346.1.
AK089958 mRNA. Translation: BAC41012.1.
AK151258 mRNA. Translation: BAE30247.1.
AK151361 mRNA. Translation: BAE30336.1.
AK151879 mRNA. Translation: BAE30765.1.
AK151908 mRNA. Translation: BAE30789.1.
AK165604 mRNA. Translation: BAE38288.1.
AL672076 Genomic DNA. Translation: CAM15900.1.
BC003235 mRNA. Translation: AAH03235.1.
CCDSiCCDS18794.1.
RefSeqiNP_077205.3. NM_024243.4.
UniGeneiMm.439940.

Genome annotation databases

EnsembliENSMUST00000030434; ENSMUSP00000030434; ENSMUSG00000028673.
GeneIDi71665.
KEGGimmu:71665.
UCSCiuc008vhi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002230 mRNA. Translation: BAB21949.1.
AK053323 mRNA. Translation: BAC35346.1.
AK089958 mRNA. Translation: BAC41012.1.
AK151258 mRNA. Translation: BAE30247.1.
AK151361 mRNA. Translation: BAE30336.1.
AK151879 mRNA. Translation: BAE30765.1.
AK151908 mRNA. Translation: BAE30789.1.
AK165604 mRNA. Translation: BAE38288.1.
AL672076 Genomic DNA. Translation: CAM15900.1.
BC003235 mRNA. Translation: AAH03235.1.
CCDSiCCDS18794.1.
RefSeqiNP_077205.3. NM_024243.4.
UniGeneiMm.439940.

3D structure databases

ProteinModelPortaliQ99LJ1.
SMRiQ99LJ1. Positions 22-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030434.

Protein family/group databases

CAZyiGH29. Glycoside Hydrolase Family 29.

PTM databases

PhosphoSiteiQ99LJ1.

Proteomic databases

MaxQBiQ99LJ1.
PaxDbiQ99LJ1.
PRIDEiQ99LJ1.

Protocols and materials databases

DNASUi71665.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030434; ENSMUSP00000030434; ENSMUSG00000028673.
GeneIDi71665.
KEGGimmu:71665.
UCSCiuc008vhi.2. mouse.

Organism-specific databases

CTDi2517.
MGIiMGI:95593. Fuca1.

Phylogenomic databases

eggNOGiCOG3669.
GeneTreeiENSGT00440000035378.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiQ99LJ1.
KOiK01206.
OMAiNGFKTQH.
OrthoDBiEOG7DC249.
PhylomeDBiQ99LJ1.
TreeFamiTF313034.

Enzyme and pathway databases

BRENDAi3.2.1.51. 3474.
SABIO-RKQ99LJ1.

Miscellaneous databases

ChiTaRSiFuca1. mouse.
NextBioi334183.
PROiQ99LJ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LJ1.
GenevestigatoriQ99LJ1.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and C57BL/6J.
    Tissue: Bone marrow, Colon, Eye and Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiFUCO_MOUSE
AccessioniPrimary (citable) accession number: Q99LJ1
Secondary accession number(s): B1AV51
, Q3UAH8, Q8BN13, Q9DD22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 106 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.