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Q99LJ1 (FUCO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:Fuca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length452 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 By similarity.

Catalytic activity

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Lysosome By similarity.

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 Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-L-fucosidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

fucose binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 452435Tissue alpha-L-fucosidase
PRO_0000010310

Sites

Site2821May be important for catalysis By similarity

Amino acid modifications

Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3791A → T in BAC41012. Ref.1
Sequence conflict3961L → F in BAB21949. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99LJ1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 41B319A040152B2C

FASTA45252,281
        10         20         30         40         50         60 
MLLLLLLLLV AAAQAVALAP RRFTPDWQSL DSRPLPSWFD EAKFGVFVHW GVFSVPAWGS 

        70         80         90        100        110        120 
EWFWWHWQGD RMPAYQRFMT ENYPPGFSYA DFAPQFTARF FHPDQWAELF QAAGAKYVVL 

       130        140        150        160        170        180 
TTKHHEGFTN WPSPVSWNWN SKDVGPHRDL VGELGAAVRK RNIRYGLYHS LLEWFHPLYL 

       190        200        210        220        230        240 
LDKKNGFKTQ HFVRAKTMPE LYDLVNSYKP DLIWSDGEWE CPDTYWNSTS FLAWLYNDSP 

       250        260        270        280        290        300 
VKDEVIVNDR WGQNCSCHHG GYYNCQDKYK PQSLPDHKWE MCTSMDRASW GYRKDMTMST 

       310        320        330        340        350        360 
IAKENEIIEE LVQTVSLGGN YLLNIGPTKD GLIVPIFQER LLAVGKWLQI NGEAIYASKP 

       370        380        390        400        410        420 
WRVQSEKNKT VVWYTTKNAT VYATFLYWPE NGIVNLKSPK TTSATKITML GLEGDLSWTQ 

       430        440        450 
DPLEGVLISL PQLPPTVLPV EFAWTLKLTK VN 

« Hide

References

[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS18794.1.
RefSeqNP_077205.3. NM_024243.4.
UniGeneMm.439940.

3D structure databases

ProteinModelPortalQ99LJ1.
SMRQ99LJ1. Positions 22-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000030434.

Protein family/group databases

CAZyGH29. Glycoside Hydrolase Family 29.

PTM databases

PhosphoSiteQ99LJ1.

Proteomic databases

MaxQBQ99LJ1.
PaxDbQ99LJ1.
PRIDEQ99LJ1.

Protocols and materials databases

DNASU71665.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030434; ENSMUSP00000030434; ENSMUSG00000028673.
GeneID71665.
KEGGmmu:71665.
UCSCuc008vhi.2. mouse.

Organism-specific databases

CTD2517.
MGIMGI:95593. Fuca1.

Phylogenomic databases

eggNOGCOG3669.
GeneTreeENSGT00440000035378.
HOGENOMHOG000029598.
HOVERGENHBG002155.
InParanoidB1AV51.
KOK01206.
OMAIFLHWPD.
OrthoDBEOG7DC249.
PhylomeDBQ99LJ1.
TreeFamTF313034.

Enzyme and pathway databases

BRENDA3.2.1.51. 3474.
SABIO-RKQ99LJ1.

Gene expression databases

BgeeQ99LJ1.
GenevestigatorQ99LJ1.

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

ChiTaRSFUCA1. mouse.
NextBio334183.
PROQ99LJ1.
SOURCESearch...

Entry information

Entry nameFUCO_MOUSE
AccessionPrimary (citable) accession number: Q99LJ1
Secondary accession number(s): B1AV51 expand/collapse secondary AC list , Q3UAH8, Q8BN13, Q9DD22
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 101 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries