FUTC_CAEEL
ID FUTC_CAEEL Reviewed; 400 AA.
AC G5EFP5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase fut-3 {ECO:0000303|PubMed:17369288};
DE EC=2.4.1.65 {ECO:0000269|PubMed:17369288};
DE AltName: Full=Fucosyltransferase fut-3 {ECO:0000305};
GN Name=fut-3 {ECO:0000312|WormBase:F59E12.13};
GN Synonyms=CEFT-4 {ECO:0000303|PubMed:17369288};
GN ORFNames=F59E12.13 {ECO:0000312|WormBase:F59E12.13};
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:CAG32978.1}
RP NUCLEOTIDE SEQUENCE [MRNA], 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, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
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).
CC -!- FUNCTION: Catalyzes the addition of fucose in alpha 1-3 linkage. Unlike
CC fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-
CC 1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man-
CC alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-
CC beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2-
CC Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-
CC beta-1-Asn (GnM3F6) acceptors. {ECO:0000269|PubMed:17369288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-
CC fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304;
CC EC=2.4.1.65; Evidence={ECO:0000269|PubMed:17369288};
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 Ni(2+) and to a lesser extent by
CC Mn(2+) and Cu(2+). {ECO:0000269|PubMed:17369288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 23 degrees Celsius. Vey low activity at 37
CC degrees Celsius. {ECO:0000269|PubMed:17369288};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:17369288}.
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17369288}.
CC -!- DISRUPTION PHENOTYPE: No obvious defect in N-glycan composition.
CC {ECO:0000269|PubMed:15364955}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000255|RuleBase:RU003832}.
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DR EMBL; AJ745072; CAG32978.1; -; mRNA.
DR EMBL; BX284602; CCD64979.1; -; Genomic_DNA.
DR PIR; T15270; T15270.
DR RefSeq; NP_495106.1; NM_062705.7.
DR AlphaFoldDB; G5EFP5; -.
DR IntAct; G5EFP5; 1.
DR STRING; 6239.F59E12.13.1; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR EPD; G5EFP5; -.
DR PaxDb; G5EFP5; -.
DR PeptideAtlas; G5EFP5; -.
DR EnsemblMetazoa; F59E12.13.1; F59E12.13.1; WBGene00006402.
DR EnsemblMetazoa; F59E12.13.2; F59E12.13.2; WBGene00006402.
DR GeneID; 173958; -.
DR KEGG; cel:CELE_F59E12.13; -.
DR CTD; 173958; -.
DR WormBase; F59E12.13; CE29413; WBGene00006402; fut-3.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00970000195924; -.
DR HOGENOM; CLU_032075_3_0_1; -.
DR InParanoid; G5EFP5; -.
DR OMA; TVAPWNA; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; G5EFP5; -.
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:G5EFP5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006402; Expressed in germ line (C elegans) and 4 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:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IMP: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..400
FT /note="Alpha-(1,3)-fucosyltransferase fut-3"
FT /id="PRO_0000438293"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..400
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 400 AA; 45744 MW; C94BC3C1C101C517 CRC64;
MRVRPASVYR YLLLGVCALL GIYTVYSIIG YDDGSHVPIH RPQRHLYLTV SQDRIGSRFG
KLAPKRILYW TTIFGATVPS TALSDCPGLT DRCVIDTNRH QLDSADAVVF HAADISKFPL
PVSRKPDQIF VFNSMETPDN SGRFAVPDGF FNWTSTHLYS SDAIHKYGTF LIPTQIAESR
GFKVQSYYVQ PKRLVKTMKG IFGLISNCHT KSKRELALQE LGKHINVTIG GKCASDDRLK
SICPAGVECI DVFEQYPFYI AIENTVCNDY VTEKIWSRIT VPSIPIVMRR RVYQNILPPK
SFIAMDDYKN PSEMANHLRS LEANSTAYGE YFEWRQKGLW TSAPWNAPGY RNGLCRVCEL
LWKAKDNETE VYKSYDNIWK WFDNESQCET DEFVRSWLSG
