FUT11_ARATH
ID FUT11_ARATH Reviewed; 501 AA.
AC Q9LJK1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glycoprotein 3-alpha-L-fucosyltransferase A;
DE EC=2.4.1.214 {ECO:0000269|PubMed:11420147, ECO:0000269|PubMed:11696361, ECO:0000269|PubMed:21515584};
DE AltName: Full=Core alpha-(1,3)-fucosyltransferase;
DE AltName: Full=Fuc-T C3;
DE AltName: Full=FucT1;
DE AltName: Full=FucTA;
DE AltName: Full=Fucosyltransferase 11;
DE Short=AtFUT11;
GN Name=FUT11; OrderedLocusNames=At3g19280; ORFNames=MVI11.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=11420147; DOI=10.1016/s0304-4165(01)00151-9;
RA Wilson I.B., Rendic D., Freilinger A., Dumic J., Altmann F., Mucha J.,
RA Muller S., Hauser M.T.;
RT "Cloning and expression of cDNAs encoding alpha1,3-fucosyltransferase
RT homologues from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1527:88-96(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=11696361; DOI=10.1016/s0014-5793(01)02999-4;
RA Bakker H., Schijlen E., de Vries T., Schiphorst W.E., Jordi W., Lommen A.,
RA Bosch D., van Die I.;
RT "Plant members of the alpha1-->3/4-fucosyltransferase gene family encode an
RT alpha1-->4-fucosyltransferase, potentially involved in Lewis(a)
RT biosynthesis, and two core alpha1-->3-fucosyltransferases.";
RL FEBS Lett. 507:307-312(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 26-287.
RC STRAIN=cv. Wassilewskija;
RA Kiefer-Meyer M.-C., Faye L., Gomord V.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, GLYCOSYLATION AT ASN-337; ASN-420
RP AND ASN-481, AND MUTAGENESIS OF SER-218; ASN-219; ARG-226; TYR-243;
RP SER-253; ASN-337; THR-339; THR-422 AND SER-483.
RX PubMed=21515584; DOI=10.1093/glycob/cwr056;
RA Both P., Sobczak L., Breton C., Hann S., Noebauer K., Paschinger K.,
RA Kozmon S., Mucha J., Wilson I.B.;
RT "Distantly related plant and nematode core alpha1,3-fucosyltransferases
RT display similar trends in structure-function relationships.";
RL Glycobiology 21:1401-1415(2011).
CC -!- FUNCTION: Involved in cell wall synthesis (Probable). Preferentially
CC catalyzes the addition of fucose in alpha 1-3 linkage to the first
CC GlcNAc residue next to the peptide chains in N-glycans
CC (PubMed:11420147, PubMed:11696361, PubMed:21515584).
CC {ECO:0000269|PubMed:11420147, ECO:0000269|PubMed:11696361,
CC ECO:0000269|PubMed:21515584, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP +
CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC [(1->4)-alpha-L-Fuc]-beta-D-GlcNAc}-L-asparaginyl-[protein];
CC Xref=Rhea:RHEA:24444, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13529,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137182; EC=2.4.1.214;
CC Evidence={ECO:0000269|PubMed:11420147, ECO:0000269|PubMed:11696361,
CC ECO:0000269|PubMed:21515584};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21515584};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21515584};
CC Note=Can also use Co(2+), Ca(2+) or Ni(2+) in vitro.
CC {ECO:0000269|PubMed:21515584};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+) and Zn(2+).
CC {ECO:0000269|PubMed:21515584}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for GDP-fucose (at pH 6.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:21515584};
CC KM=15 uM for NST-GlcNAc-beta-1-2Man-alpha-1-6(GlcNAc-beta-1-2Man-
CC alpha-1-3)Man-beta-1-4GlcNAc-beta-1-4GlcNAc (GnGn) (at pH 6.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:21515584};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- DOMAIN: The C-terminus (388-501) is important for catalytic activity or
CC for enzyme stability. The N-terminus (1-89) appears to be dispensable
CC for enzymatic activity. {ECO:0000269|PubMed:21515584}.
CC -!- PTM: Glycosylation may be important for enzymatic activity.
CC {ECO:0000269|PubMed:21515584}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ404860; CAC38048.1; -; mRNA.
DR EMBL; AJ345084; CAC78979.1; -; mRNA.
DR EMBL; AP000419; BAB02969.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76217.1; -; Genomic_DNA.
DR EMBL; AF277228; AAM68912.1; -; mRNA.
DR EMBL; AF277229; AAM68913.1; -; mRNA.
DR RefSeq; NP_188559.1; NM_112815.4.
DR AlphaFoldDB; Q9LJK1; -.
DR BioGRID; 6795; 1.
DR STRING; 3702.AT3G19280.1; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR iPTMnet; Q9LJK1; -.
DR PaxDb; Q9LJK1; -.
DR PRIDE; Q9LJK1; -.
DR ProteomicsDB; 230439; -.
DR EnsemblPlants; AT3G19280.1; AT3G19280.1; AT3G19280.
DR GeneID; 821462; -.
DR Gramene; AT3G19280.1; AT3G19280.1; AT3G19280.
DR KEGG; ath:AT3G19280; -.
DR Araport; AT3G19280; -.
DR TAIR; locus:2094078; AT3G19280.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_040484_0_0_1; -.
DR InParanoid; Q9LJK1; -.
DR OMA; FLHIKQM; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q9LJK1; -.
DR BioCyc; ARA:AT3G19280-MON; -.
DR BioCyc; MetaCyc:AT3G19280-MON; -.
DR BRENDA; 2.4.1.214; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LJK1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJK1; baseline and differential.
DR Genevisible; Q9LJK1; AT.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:TAIR.
DR GO; GO:0018392; F:glycoprotein 3-alpha-L-fucosyltransferase activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; TAS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:TAIR.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Magnesium; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..501
FT /note="Glycoprotein 3-alpha-L-fucosyltransferase A"
FT /id="PRO_0000221124"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..501
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 218
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000269|PubMed:21515584"
FT SITE 219
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000269|PubMed:21515584"
FT SITE 226
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000269|PubMed:21515584"
FT SITE 243
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000269|PubMed:21515584"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:21515584"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:21515584"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:21515584"
FT MUTAGEN 218
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 219
FT /note="N->A: Loss of catalytic activity associated with a
FT 3-fold decrease in affinity for GDP-fucose."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 226
FT /note="R->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 243
FT /note="Y->A: 90 percent decrease in catalytic activity
FT associated with a 2.4-fold decrease in affinity for GDP-
FT fucose."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 253
FT /note="S->A: 65 percent decrease in catalytic activity with
FT no decrease in affinity for GDP-fucose."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 337
FT /note="N->A: 80 percent decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 339
FT /note="T->A: 90 percent decrease in catalytic activity
FT associated with a 3.6-fold decrease in affinity for GDP-
FT fucose. 95 percent decrease in catalytic activity; when
FT associated with A-422 and A-483."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 422
FT /note="T->A: 65 percent decrease in catalytic activity. 95
FT percent decrease in catalytic activity; when associated
FT with A-339 and A-483."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 483
FT /note="S->A: 70 percent decrease in catalytic activity. 95
FT percent decrease in catalytic activity; when associated
FT with A-339 and A-422."
FT /evidence="ECO:0000269|PubMed:21515584"
FT CONFLICT 210
FT /note="K -> E (in Ref. 5; AAM68912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56205 MW; 2CEAC85CD1A3DA5B CRC64;
MGVFSNLRGP KIGLTHEELP VVANGSTSSS SSPSSFKRKV STFLPICVAL VVIIEIGFLC
RLDNASLVDT LTHFFTKSSS DLKVGSGIEK CQEWLERVDS VTYSRDFTKD PIFISGSNKD
FKSCSVDCVM GFTSDKKPDA AFGLSHQPGT LSIIRSMESA QYYQENNLAQ ARRKGYDIVM
TTSLSSDVPV GYFSWAEYDI MAPVQPKTEK ALAAAFISNC AARNFRLQAL EALMKTNVKI
DSYGGCHRNR DGSVEKVEAL KHYKFSLAFE NTNEEDYVTE KFFQSLVAGS VPVVVGAPNI
EEFAPSPDSF LHIKQMDDVK AVAKKMKYLA DNPDAYNQTL RWKHEGPSDS FKALIDMAAV
HSSCRLCIFV ATRIREQEEK SPEFKRRPCK CTRGSETVYH LYVRERGRFD MESIFLKDGN
LTLEALESAV LAKFMSLRYE PIWKKERPAS LRGDGKLRVH GIYPIGLTQR QALYNFKFEG
NSSLSTHIQR NPCPKFEVVF V
