FUTD_CAEEL
ID FUTD_CAEEL Reviewed; 378 AA.
AC G5EE06;
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-5 {ECO:0000303|PubMed:17369288};
DE EC=2.4.1.65 {ECO:0000269|PubMed:17369288};
DE AltName: Full=Fucosyltransferase fut-5 {ECO:0000305};
GN Name=fut-5 {ECO:0000312|WormBase:T05A7.10};
GN Synonyms=CEFT-2 {ECO:0000303|PubMed:17369288};
GN ORFNames=T05A7.10 {ECO:0000312|WormBase:T05A7.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAG32979.1};
RN [1] {ECO:0000312|EMBL:CAG32979.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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 to
CC GalNAc-beta-1->4-GlcNAc-beta-1->3-Gal-beta-1->4-Glc (LDNT)acceptor.
CC Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-
CC Man-beta-1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-
CC (Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-
CC GlcNAc-beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-
CC beta-1->2-Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-
CC 1->6)-GlcNAc-beta-1-Asn (GnM3F6) acceptors.
CC {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 Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17369288};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+) and Ni(2+), and to a lesser
CC extent by EDTA, Mn(2+) and Mg(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 -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000255|RuleBase:RU003832}.
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DR EMBL; AJ745073; CAG32979.1; -; mRNA.
DR EMBL; BX284602; CCD69228.1; -; Genomic_DNA.
DR RefSeq; NP_001022310.1; NM_001027139.1.
DR AlphaFoldDB; G5EE06; -.
DR STRING; 6239.T05A7.10; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; G5EE06; -.
DR PRIDE; G5EE06; -.
DR EnsemblMetazoa; T05A7.10.1; T05A7.10.1; WBGene00043986.
DR GeneID; 3565968; -.
DR KEGG; cel:CELE_T05A7.10; -.
DR CTD; 3565968; -.
DR WormBase; T05A7.10; CE37986; WBGene00043986; fut-5.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00970000196480; -.
DR HOGENOM; CLU_032075_3_0_1; -.
DR InParanoid; G5EE06; -.
DR OMA; NGRWSYV; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; G5EE06; -.
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:G5EE06; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00043986; Expressed in adult organism and 1 other tissue.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Calcium; Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Alpha-(1,3)-fucosyltransferase fut-5"
FT /id="PRO_0000438294"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..378
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 378 AA; 44346 MW; 7A8D75BE0C693BF5 CRC64;
MKHNTLRAVF QFSFFIGICT FIMIAGYSYQ INYNQRMGIF YGGNITFKKV PKVVIYTATP
FFDVPIENSI LRDCSEKIKN SCTVTSNNKT FPIADAIVFH SRDINETKLS FFNKNRRYDI
PYIMMAMENP FFAGLTVYHN FFNWTMTYRT DSDIFHPYGA FVKSYVPAEV NYSEIWNSKT
KETLWMVSNG NAQNKRKELV EKLIKKGMSI DLYGQLYKKE PAECPRRRGP PGCDVKFHSP
YKFAIAFENS NCKDYVTEKF WKKAGIYKTV PIVMSRKIYR DLGIPDSMYI AVDDYPNLEE
FVHHIQNVTS NEEEYMKYHK WRKQFKIVDT NEGNIGFCQL CQKLAGYKRK LVPHKVYENL
NSWHSTSTCD NSFATRFL
