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Protein

Plasma alpha-L-fucosidase

Gene

Fuca2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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
Sitei288 – 2881May 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
  3. regulation of entry of bacterium into host cell Source: MGI
  4. response to bacterium Source: MGI
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 Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 461436Plasma alpha-L-fucosidasePRO_0000010313Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ99KR8.
PaxDbiQ99KR8.
PRIDEiQ99KR8.

PTM databases

PhosphoSiteiQ99KR8.

Expressioni

Gene expression databases

BgeeiQ99KR8.
CleanExiMM_FUCA2.
ExpressionAtlasiQ99KR8. baseline and differential.
GenevestigatoriQ99KR8.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ99KR8.
SMRiQ99KR8. Positions 28-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 29 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3669.
GeneTreeiENSGT00440000035378.
HOGENOMiHOG000029598.
HOVERGENiHBG002155.
InParanoidiQ99KR8.
KOiK01206.
OMAiQFTAEFF.
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

        10         20         30         40         50
MRLGFLMLLP LLLLPLLRPW GVTRALSYDP TWESLDRRPL PAWFDQAKFG
60 70 80 90 100
IFIHWGVFSV PSFGSEWFWW YWQKEKKPQF VDFMNNNYAP GFKYEDFVVL
110 120 130 140 150
FTAKYFNANQ WADILQASGA KYVVFTSKHH EGFTMWGSDR SWNWNAVDEG
160 170 180 190 200
PKRDIVKELE VAVRNRTGLH FGLYYSLFEW FHPLFLEDQS SSFQKQRFPV
210 220 230 240 250
SKTLPELYEL VNRYQPEVLW SDGDGGAPDH YWNSTGFLAW LYNESPVRKT
260 270 280 290 300
VVTNDRWGVG SICKHGGYYT CSDRYNPGYL LPHKWENCMT IDKFSWGYRR
310 320 330 340 350
EAEISDYLTI EELVKKLVET VACGGNLLMN IGPTGDGTIP VIFEERLRQM
360 370 380 390 400
GTWLKVNGEA IYETHTWRSQ NDTVTPDVWY TSKPEKKLVY AIFLKWPISG
410 420 430 440 450
KLFLGQPIGS LGETEVELLG HWQPLTWTSS QPSGITVELP LLSVHQMPCK
460
WGWTLVLSNV I
Length:461
Mass (Da):53,645
Last modified:June 1, 2001 - v1
Checksum:i1E232FE5ED6A3C1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32RL → PG in BAB25809 (PubMed:16141072).Curated
Sequence conflicti140 – 1401R → H in AAH18181 (PubMed:15489334).Curated
Sequence conflicti435 – 4351I → V in BAB22277 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ99KR8.
SMRiQ99KR8. Positions 28-404.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH29. Glycoside Hydrolase Family 29.

PTM databases

PhosphoSiteiQ99KR8.

Proteomic databases

MaxQBiQ99KR8.
PaxDbiQ99KR8.
PRIDEiQ99KR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2519.
MGIiMGI:1914098. Fuca2.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.2.1.51. 3474.

Miscellaneous databases

ChiTaRSiFuca2. mouse.
NextBioi322811.
PROiQ99KR8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KR8.
CleanExiMM_FUCA2.
ExpressionAtlasiQ99KR8. baseline and differential.
GenevestigatoriQ99KR8.

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]
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: 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: February 4, 2015
This is version 101 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.