FUTE_CAEEL
ID FUTE_CAEEL Reviewed; 392 AA.
AC G5EEE1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase fut-6 {ECO:0000303|PubMed:17369288};
DE EC=2.4.1.- {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284};
GN Name=fut-6 {ECO:0000312|WormBase:T05A7.5};
GN Synonyms=CEFT-3 {ECO:0000303|PubMed:17369288};
GN ORFNames=T05A7.5 {ECO:0000312|WormBase:T05A7.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAG32980.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15364955; DOI=10.1074/jbc.m408978200;
RA Paschinger K., Rendic D., Lochnit G., Jantsch V., Wilson I.B.H.;
RT "Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 279:49588-49598(2004).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17369288; DOI=10.1093/glycob/cwm023;
RA Nguyen K., van Die I., Grundahl K.M., Kawar Z.S., Cummings R.D.;
RT "Molecular cloning and characterization of the Caenorhabditis elegans
RT alpha1,3-fucosyltransferase family.";
RL Glycobiology 17:586-599(2007).
RN [4] {ECO:0000305}
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=23754284; DOI=10.1074/jbc.m113.479147;
RA Yan S., Serna S., Reichardt N.C., Paschinger K., Wilson I.B.;
RT "Array-assisted characterization of a fucosyltransferase required for the
RT biosynthesis of complex core modifications of nematode N-glycans.";
RL J. Biol. Chem. 288:21015-21028(2013).
RN [5] {ECO:0000305}
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=26538210; DOI=10.1021/acs.jproteome.5b00746;
RA Yan S., Jin C., Wilson I.B., Paschinger K.;
RT "Comparisons of Caenorhabditis fucosyltransferase mutants reveal a
RT multiplicity of isomeric N-Glycan structures.";
RL J. Proteome Res. 14:5291-5305(2015).
RN [6] {ECO:0000305}
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=26002521; DOI=10.1074/mcp.m115.049817;
RA Yan S., Brecker L., Jin C., Titz A., Dragosits M., Karlsson N.G.,
RA Jantsch V., Wilson I.B., Paschinger K.;
RT "Bisecting Galactose as a Feature of N-Glycans of Wild-type and Mutant
RT Caenorhabditis elegans.";
RL Mol. Cell. Proteomics 14:2111-2125(2015).
CC -!- FUNCTION: Involved in the fucosylation of N-glycans (PubMed:15364955,
CC PubMed:17369288, PubMed:23754284, PubMed:26538210, PubMed:26002521).
CC Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to
CC the distal GlcNAc residue in N-glycans (PubMed:23754284). Catalyzes the
CC transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-
CC beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288).
CC Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose
CC to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-
CC beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-
CC beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-
CC Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-
CC 1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288).
CC {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288,
CC ECO:0000269|PubMed:23754284, ECO:0000269|PubMed:26002521,
CC ECO:0000269|PubMed:26538210}.
CC -!- COFACTOR:
CC Note=Unlike other alpha-(1,3)-fucosyltransferases, appears not to
CC require a divalent metal cation as cofactor.
CC {ECO:0000269|PubMed:17369288};
CC -!- ACTIVITY REGULATION: Inhibited by divalent metal cations.
CC {ECO:0000269|PubMed:17369288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 23 degrees Celsius. Very low activity at 37
CC degrees Celsius. {ECO:0000269|PubMed:17369288};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284,
CC ECO:0000269|PubMed:26002521, ECO:0000269|PubMed:26538210}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein
CC {ECO:0000255|RuleBase:RU003832}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and adult.
CC {ECO:0000269|PubMed:17369288}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:17369288). Loss of
CC several tetra-fucosylated N-glycans (PubMed:15364955). Loss of
CC tetra- and tri-fucosylated N-glycans in a fut-8 or fut-1 mutant
CC background (PubMed:26538210). fut-1, fut-6 and fut-8 triple mutants
CC lack all N-glycan core fucose with only one fucose present in the
CC bisecting galactose, thus resulting in the loss of tetra-, tri- and bi-
CC fucosylated N-glycans (PubMed:26002521). {ECO:0000269|PubMed:15364955,
CC ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:26002521,
CC ECO:0000269|PubMed:26538210}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000255|RuleBase:RU003832}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ745074; CAG32980.1; -; mRNA.
DR EMBL; BX284602; CCD69223.1; -; Genomic_DNA.
DR PIR; T16799; T16799.
DR RefSeq; NP_494823.2; NM_062422.7.
DR AlphaFoldDB; G5EEE1; -.
DR STRING; 6239.T05A7.5; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR EPD; G5EEE1; -.
DR PaxDb; G5EEE1; -.
DR PeptideAtlas; G5EEE1; -.
DR PRIDE; G5EEE1; -.
DR EnsemblMetazoa; T05A7.5.1; T05A7.5.1; WBGene00020222.
DR GeneID; 188084; -.
DR KEGG; cel:CELE_T05A7.5; -.
DR CTD; 188084; -.
DR WormBase; T05A7.5; CE32206; WBGene00020222; fut-6.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_032075_3_0_1; -.
DR InParanoid; G5EEE1; -.
DR OMA; SNVYPQA; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; G5EEE1; -.
DR Reactome; R-CEL-9037629; Lewis blood group biosynthesis.
DR Reactome; R-CEL-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR PRO; PR:G5EEE1; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020222; Expressed in adult organism and 3 other tissues.
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:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; IGI:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..392
FT /note="Alpha-(1,3)-fucosyltransferase fut-6"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438422"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..392
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 392 AA; 45226 MW; 8B2E9B7D969D3E43 CRC64;
MSQIGGATCT WRYLGRFVTL GIYASVALFV WYTLVPTRSK HKDSIAINNN NADPATALIP
VHTKNVVIYA ATKFFGHPIT TERFLATCPD VQNYCRITQE ESEFDNADAV LFHNADYRGS
TDKFKKMKSQ RKPGVPYVLW SLESPTNDMF RPDSHMINWT MTYRTDSDVW APYGTIVKLK
NPVEVDLNAI WEGKTKTATW LASNCITQNH RFDLIKKIID NGFEIDIWGN CGKQVSQCAG
VDNQESPCVL ELIKPYKFYI SMENSNCKDY VTEKFWKALN DRMTIPIVLA RKYYKDLGVP
DSAYIAVDDY ATLDEFLAHV KKVNKEKDLF LSYHQWRKEW KVIIGSGFSG WCTLCNKLQD
KDYILKNPKS YKDVAWWHSF EMCNNQIASK YL
