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Q99KR8

- FUCO2_MOUSE

UniProt

Q99KR8 - FUCO2_MOUSE

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Protein
Plasma alpha-L-fucosidase
Gene
Fuca2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei288 – 2881May be important for catalysis By similarity

GO - Molecular functioni

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

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. 3474.

Protein family/group databases

CAZyiGH29. Glycoside Hydrolase Family 29.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Fuca2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1914098. Fuca2.

Subcellular locationi

Secreted Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. lysosome Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 461436Plasma alpha-L-fucosidase
PRO_0000010313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi165 – 1651N-linked (GlcNAc...) Reviewed prediction
Glycosylationi233 – 2331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi371 – 3711N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ99KR8.
PaxDbiQ99KR8.
PRIDEiQ99KR8.

PTM databases

PhosphoSiteiQ99KR8.

Expressioni

Gene expression databases

ArrayExpressiQ99KR8.
BgeeiQ99KR8.
CleanExiMM_FUCA2.
GenevestigatoriQ99KR8.

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ99KR8.
SMRiQ99KR8. Positions 24-459.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3669.
GeneTreeiENSGT00440000035378.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiQ99KR8.
KOiK01206.
OMAiVGSICKH.
PhylomeDBiQ99KR8.
TreeFamiTF313034.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016286. 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]
PANTHERiPTHR10030. PTHR10030. 1 hit.
PTHR10030:SF24. PTHR10030:SF24. 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.

Q99KR8-1 [UniParc]FASTAAdd to Basket

« Hide

MRLGFLMLLP LLLLPLLRPW GVTRALSYDP TWESLDRRPL PAWFDQAKFG    50
IFIHWGVFSV PSFGSEWFWW YWQKEKKPQF VDFMNNNYAP GFKYEDFVVL 100
FTAKYFNANQ WADILQASGA KYVVFTSKHH EGFTMWGSDR SWNWNAVDEG 150
PKRDIVKELE VAVRNRTGLH FGLYYSLFEW FHPLFLEDQS SSFQKQRFPV 200
SKTLPELYEL VNRYQPEVLW SDGDGGAPDH YWNSTGFLAW LYNESPVRKT 250
VVTNDRWGVG SICKHGGYYT CSDRYNPGYL LPHKWENCMT IDKFSWGYRR 300
EAEISDYLTI EELVKKLVET VACGGNLLMN IGPTGDGTIP VIFEERLRQM 350
GTWLKVNGEA IYETHTWRSQ NDTVTPDVWY TSKPEKKLVY AIFLKWPISG 400
KLFLGQPIGS LGETEVELLG HWQPLTWTSS QPSGITVELP LLSVHQMPCK 450
WGWTLVLSNV I 461
Length:461
Mass (Da):53,645
Last modified:June 1, 2001 - v1
Checksum:i1E232FE5ED6A3C1F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32RL → PG in BAB25809. 1 Publication
Sequence conflicti140 – 1401R → H in AAH18181. 1 Publication
Sequence conflicti435 – 4351I → V in BAB22277. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23701.1.
RefSeqiNP_080075.2. NM_025799.4.
XP_006512889.1. XM_006512826.1.
XP_006512890.1. XM_006512827.1.
UniGeneiMm.26625.

Genome annotation databases

EnsembliENSMUST00000060212; ENSMUSP00000055519; ENSMUSG00000019810.
ENSMUST00000121465; ENSMUSP00000113499; ENSMUSG00000019810.
GeneIDi66848.
KEGGimmu:66848.
UCSCiuc007ekv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23701.1.
RefSeqi NP_080075.2. NM_025799.4.
XP_006512889.1. XM_006512826.1.
XP_006512890.1. XM_006512827.1.
UniGenei Mm.26625.

3D structure databases

ProteinModelPortali Q99KR8.
SMRi Q99KR8. Positions 24-459.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH29. Glycoside Hydrolase Family 29.

PTM databases

PhosphoSitei Q99KR8.

Proteomic databases

MaxQBi Q99KR8.
PaxDbi Q99KR8.
PRIDEi Q99KR8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000060212 ; ENSMUSP00000055519 ; ENSMUSG00000019810 .
ENSMUST00000121465 ; ENSMUSP00000113499 ; ENSMUSG00000019810 .
GeneIDi 66848.
KEGGi mmu:66848.
UCSCi uc007ekv.1. mouse.

Organism-specific databases

CTDi 2519.
MGIi MGI:1914098. Fuca2.

Phylogenomic databases

eggNOGi COG3669.
GeneTreei ENSGT00440000035378.
HOGENOMi HOG000029598.
HOVERGENi HBG002155.
InParanoidi Q99KR8.
KOi K01206.
OMAi VGSICKH.
PhylomeDBi Q99KR8.
TreeFami TF313034.

Enzyme and pathway databases

BRENDAi 3.2.1.51. 3474.

Miscellaneous databases

ChiTaRSi FUCA2. mouse.
NextBioi 322811.
PROi Q99KR8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99KR8.
Bgeei Q99KR8.
CleanExi MM_FUCA2.
Genevestigatori Q99KR8.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR016286. 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 ]
PANTHERi PTHR10030. PTHR10030. 1 hit.
PTHR10030:SF24. PTHR10030:SF24. 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. "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: 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.

Entry informationi

Entry nameiFUCO2_MOUSE
AccessioniPrimary (citable) accession number: Q99KR8
Secondary accession number(s): Q8VEM3, Q9D7Z8, Q9DCL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 96 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

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