Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99KR8 (FUCO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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:
Plasma alpha-L-fucosidase

EC=3.2.1.51
Alternative name(s):
Alpha-L-fucoside fucohydrolase 2
Short name=Alpha-L-fucosidase 2
Gene names
Name:Fuca2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length461 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

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 29 family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

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 – 2525 Potential
Chain26 – 461436Plasma alpha-L-fucosidase
PRO_0000010313

Sites

Site2881May be important for catalysis By similarity

Amino acid modifications

Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2 – 32RL → PG in BAB25809. Ref.1
Sequence conflict1401R → H in AAH18181. Ref.2
Sequence conflict4351I → V in BAB22277. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99KR8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1E232FE5ED6A3C1F

FASTA46153,645
        10         20         30         40         50         60 
MRLGFLMLLP LLLLPLLRPW GVTRALSYDP TWESLDRRPL PAWFDQAKFG IFIHWGVFSV 

        70         80         90        100        110        120 
PSFGSEWFWW YWQKEKKPQF VDFMNNNYAP GFKYEDFVVL FTAKYFNANQ WADILQASGA 

       130        140        150        160        170        180 
KYVVFTSKHH EGFTMWGSDR SWNWNAVDEG PKRDIVKELE VAVRNRTGLH FGLYYSLFEW 

       190        200        210        220        230        240 
FHPLFLEDQS SSFQKQRFPV SKTLPELYEL VNRYQPEVLW SDGDGGAPDH YWNSTGFLAW 

       250        260        270        280        290        300 
LYNESPVRKT VVTNDRWGVG SICKHGGYYT CSDRYNPGYL LPHKWENCMT IDKFSWGYRR 

       310        320        330        340        350        360 
EAEISDYLTI EELVKKLVET VACGGNLLMN IGPTGDGTIP VIFEERLRQM GTWLKVNGEA 

       370        380        390        400        410        420 
IYETHTWRSQ NDTVTPDVWY TSKPEKKLVY AIFLKWPISG KLFLGQPIGS LGETEVELLG 

       430        440        450        460 
HWQPLTWTSS QPSGITVELP LLSVHQMPCK WGWTLVLSNV I 

« 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: C57BL/6J.
Tissue: Kidney, Ovary, Stomach, Urinary bladder and Uterus.
[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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002675 mRNA. Translation: BAB22277.1.
AK008653 mRNA. Translation: BAB25809.1.
AK030320 mRNA. Translation: BAC26899.1.
AK035607 mRNA. Translation: BAC29123.1.
BC004039 mRNA. Translation: AAH04039.1.
BC018181 mRNA. Translation: AAH18181.1.
RefSeqNP_080075.2. NM_025799.4.
XP_006512889.1. XM_006512826.1.
XP_006512890.1. XM_006512827.1.
UniGeneMm.26625.

3D structure databases

ProteinModelPortalQ99KR8.
SMRQ99KR8. Positions 27-460.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH29. Glycoside Hydrolase Family 29.

PTM databases

PhosphoSiteQ99KR8.

Proteomic databases

PaxDbQ99KR8.
PRIDEQ99KR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060212; ENSMUSP00000055519; ENSMUSG00000019810.
ENSMUST00000121465; ENSMUSP00000113499; ENSMUSG00000019810.
GeneID66848.
KEGGmmu:66848.
UCSCuc007ekv.1. mouse.

Organism-specific databases

CTD2519.
MGIMGI:1914098. Fuca2.

Phylogenomic databases

eggNOGCOG3669.
GeneTreeENSGT00440000035378.
HOGENOMHOG000029598.
HOVERGENHBG002155.
InParanoidQ99KR8.
KOK01206.
OMAQFTAEFF.
PhylomeDBQ99KR8.
TreeFamTF313034.

Enzyme and pathway databases

BRENDA3.2.1.51. 3474.

Gene expression databases

ArrayExpressQ99KR8.
BgeeQ99KR8.
CleanExMM_FUCA2.
GenevestigatorQ99KR8.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR016286. FUC_metazoa-typ.
IPR028756. FUCA2.
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:SF6. PTHR10030:SF6. 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

ChiTaRSFUCA2. mouse.
NextBio322811.
PROQ99KR8.
SOURCESearch...

Entry information

Entry nameFUCO2_MOUSE
AccessionPrimary (citable) accession number: Q99KR8
Secondary accession number(s): Q8VEM3, Q9D7Z8, Q9DCL7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 93 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