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Q8L7W8

- FUCO2_ARATH

UniProt

Q8L7W8 - FUCO2_ARATH

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Protein

Alpha-L-fucosidase 2

Gene

FUC95A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes alpha-1,2-linked fucose. Also active on fucosylated xyloglucan oligosaccharides. No activity with 3-fucosyllactose, p-nitrophenyl-alpha-I-fucopyranoside, lacto-N-fucopentaose II, lacto-N-fucopentaose III or alpha 1,6-fucosylated chitopentaose. Involved in apoplastic xyloglucan metabolism.2 Publications

Catalytic activityi

An alpha-L-fucoside + H2O = L-fucose + an alcohol.1 Publication

Kineticsi

  1. KM=0.65 mM for 2-fucosyllactose1 Publication
  2. KM=1.5 mM for polymeric xyloglucan1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

GO - Molecular functioni

  1. 1,2-alpha-L-fucosidase activity Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciARA:AT4G34260-MONOMER.

Protein family/group databases

CAZyiGH95. Glycoside Hydrolase Family 95.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-fucosidase 2 (EC:3.2.1.51)
Alternative name(s):
Alpha-1,2-fucosidase 2
Alpha-L-fucosidase 95A
Short name:
AtFuc95A
Alpha-L-fucoside fucohydrolase 2
Protein ALTERED XYLOGLUCAN 8
Gene namesi
Name:FUC95A
Synonyms:AXY8
Ordered Locus Names:At4g34260
ORF Names:F10M10.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34260.

Subcellular locationi

Secretedextracellular spaceapoplast 1 Publication

GO - Cellular componenti

  1. apoplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Higher abundance of fucosylated oligosaccharides and presence of unusual oligosaccharides.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi511 – 5111C → Y in axy8-4; Loss of activity. 1 Publication
Mutagenesisi562 – 5621P → L in axy8-3; Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 843816Alpha-L-fucosidase 2PRO_0000289877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi605 – 6051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8L7W8.
PRIDEiQ8L7W8.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression in vascular tissues, leaf trichomes, root elongation zone and emerging lateral roots.1 Publication

Gene expression databases

GenevestigatoriQ8L7W8.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G34260.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8L7W8.
SMRiQ8L7W8. Positions 56-806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 95 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG04067.
HOGENOMiHOG000161832.
InParanoidiQ8L7W8.
KOiK15923.
OMAiCKYTINI.
PhylomeDBiQ8L7W8.

Family and domain databases

Gene3Di2.70.98.50. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR016518. Alpha-L-fucosidase.
IPR027414. GH_fam_N_dom.
[Graphical view]
PfamiPF14498. Glyco_hyd_65N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF007663. UCP007663. 1 hit.
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8L7W8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEKSSFFVH FSCLLLLLTI IITCGEGVRN PVRPRSSERR ALMDGQDLSR
60 70 80 90 100
PLKLTFGGPS RNWTDAIPIG NGRLGATIWG GVSSEILNIN EDTIWTGVPA
110 120 130 140 150
DYTNQKAPEA LAEVRRLVDE RNYAEATSEA VKLSGQPSDV YQIVGDLNLE
160 170 180 190 200
FDSSHRKYTQ ASYRRELDLE TAVAKVSYSV GAVDFSREFF ASNPDQVIIA
210 220 230 240 250
KIYASKPGSL SFKVSFDSEL HHHSETNPKA NQILMRGSCR PKRLPVNLKK
260 270 280 290 300
SINATNIPYD DHKGLQFASI LEVRVSNGGS VSSLGGKKLS VEKADWAVLL
310 320 330 340 350
LAASSNFDGP FTMPVDSKID PAKECVNRIS SVQKYSYSDL YARHLGDYQK
360 370 380 390 400
LFNRVSLHLS GSSTNETVQQ ATSTAERVRS FKTDQDPSLV ELLFQYGRYL
410 420 430 440 450
LISSSRPGTQ VANLQGIWNR DIQPPWDGAP HLNINLQMNY WHSLPGNIRE
460 470 480 490 500
CQEPLFDYMS ALAINGRKTA QVNYGASGWV AHQVSDIWAK TSPDRGEAVW
510 520 530 540 550
ALWPMGGAWL CTHAWEHYTY TMDKEFLKKK GYPLLEGCTS FLLDWLIKGK
560 570 580 590 600
DGFLQTNPST SPEHMFTAPI GKPASVSYSS TMDIAIIKEV FADIVSASEI
610 620 630 640 650
LGKTNDTLIG KVIAAQAKLP PTRISKDGSI REWAEDFEDP EVHHRHVSHL
660 670 680 690 700
FGLFPGHTIT VEKSPELAKA VEATLKKRGE EGPGWSTTWK AALWARLHNS
710 720 730 740 750
EHAYRMVTHI FDLVDPLNER NYEGGLYSNM FTAHPPFQID ANFGFAAAVA
760 770 780 790 800
EMLVQSTTKD LYLLPALPAD KWPNGIVNGL RARGGVTVSI KWMEGNLVEF
810 820 830 840
GLWSEQIVST RIVYRGISAA AELLPGKVFT FDKDLRCIRT DKL
Length:843
Mass (Da):93,725
Last modified:October 1, 2002 - v1
Checksum:i2EF1315DF98A1365
GO

Sequence cautioni

The sequence CAB36703.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB80143.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035521 Genomic DNA. Translation: CAB36703.1. Sequence problems.
AL161585 Genomic DNA. Translation: CAB80143.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86349.1.
AY125494 mRNA. Translation: AAM78086.1.
BT002722 mRNA. Translation: AAO11638.1.
PIRiT04772.
RefSeqiNP_195152.2. NM_119590.3.
UniGeneiAt.45833.

Genome annotation databases

EnsemblPlantsiAT4G34260.1; AT4G34260.1; AT4G34260.
GeneIDi829575.
KEGGiath:AT4G34260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035521 Genomic DNA. Translation: CAB36703.1 . Sequence problems.
AL161585 Genomic DNA. Translation: CAB80143.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE86349.1 .
AY125494 mRNA. Translation: AAM78086.1 .
BT002722 mRNA. Translation: AAO11638.1 .
PIRi T04772.
RefSeqi NP_195152.2. NM_119590.3.
UniGenei At.45833.

3D structure databases

ProteinModelPortali Q8L7W8.
SMRi Q8L7W8. Positions 56-806.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G34260.1-P.

Protein family/group databases

CAZyi GH95. Glycoside Hydrolase Family 95.

Proteomic databases

PaxDbi Q8L7W8.
PRIDEi Q8L7W8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G34260.1 ; AT4G34260.1 ; AT4G34260 .
GeneIDi 829575.
KEGGi ath:AT4G34260.

Organism-specific databases

TAIRi AT4G34260.

Phylogenomic databases

eggNOGi NOG04067.
HOGENOMi HOG000161832.
InParanoidi Q8L7W8.
KOi K15923.
OMAi CKYTINI.
PhylomeDBi Q8L7W8.

Enzyme and pathway databases

BioCyci ARA:AT4G34260-MONOMER.

Gene expression databases

Genevestigatori Q8L7W8.

Family and domain databases

Gene3Di 2.70.98.50. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR016518. Alpha-L-fucosidase.
IPR027414. GH_fam_N_dom.
[Graphical view ]
Pfami PF14498. Glyco_hyd_65N_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF007663. UCP007663. 1 hit.
SUPFAMi SSF48208. SSF48208. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Molecular cloning and characterization of Bifidobacterium bifidum 1,2-alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95)."
    Katayama T., Sakuma A., Kimura T., Makimura Y., Hiratake J., Sakata K., Yamanoi T., Kumagai H., Yamamoto K.
    J. Bacteriol. 186:4885-4893(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "Identification of an Arabidopsis gene encoding a GH95 alpha1,2-fucosidase active on xyloglucan oligo- and polysaccharides."
    Leonard R., Pabst M., Bondili J.S., Chambat G., Veit C., Strasser R., Altmann F.
    Phytochemistry 69:1983-1988(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "AXY8 encodes an alpha-fucosidase, underscoring the importance of apoplastic metabolism on the fine structure of Arabidopsis cell wall polysaccharides."
    Gunl M., Neumetzler L., Kraemer F., de Souza A., Schultink A., Pena M., York W.S., Pauly M.
    Plant Cell 23:4025-4040(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-511 AND PRO-562, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiFUCO2_ARATH
AccessioniPrimary (citable) accession number: Q8L7W8
Secondary accession number(s): Q9SYZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2002
Last modified: October 1, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3