FUTA_CAEEL
ID FUTA_CAEEL Reviewed; 433 AA.
AC G5EDR5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase fut-1 {ECO:0000303|PubMed:9675224};
DE EC=2.4.1.214 {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224};
DE AltName: Full=Fucosyltransferase fut-1 {ECO:0000305};
GN Name=fut-1 {ECO:0000312|WormBase:K08F8.3};
GN Synonyms=CEFT-1 {ECO:0000303|PubMed:9675224};
GN ORFNames=K08F8.3 {ECO:0000312|WormBase:K08F8.3};
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:CAG32977.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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, AND PATHWAY.
RX PubMed=9675224; DOI=10.1093/glycob/8.9.905;
RA DeBose-Boyd R.A., Nyame A.K., Cummings R.D.;
RT "Molecular cloning and characterization of an alpha1,3 fucosyltransferase,
RT CEFT-1, from Caenorhabditis elegans.";
RL Glycobiology 8:905-917(1998).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY, DEVELOPMENTAL
RP 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).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, GLYCOSYLATION, AND MUTAGENESIS OF
RP ASN-194; SER-243; ASP-303; THR-361 AND 424-GLY--ASP-433.
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: Preferentially catalyzes the addition of fucose in alpha 1-3
CC linkage to the first GlcNAc residue (with or without alpha 1,6-linked
CC fucose), next to the peptide chains in N-glycans (PubMed:15364955,
CC PubMed:9675224, PubMed:17369288, PubMed:21515584). Unlike in mammals,
CC does not require the prior action of N-acetylglucosaminyltransferase I
CC to generate complex N-glycans (PubMed:15364955).
CC {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288,
CC ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224}.
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:15364955, ECO:0000269|PubMed:17369288,
CC ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584};
CC Note=Can also use Co(2+) or Ca(2+) in vitro.
CC {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+) or Zn(2+) and to a lesser
CC extent Ni(2+) ions. {ECO:0000269|PubMed:17369288,
CC ECO:0000269|PubMed:21515584}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for GDP-fucose (at pH 7.5 and 23 degrees Celsius)
CC {ECO:0000269|PubMed:21515584};
CC KM=400 uM for Man-alpha-1-6(Man-alpha-1-3)Man-alpha-1-6(Man-alpha-1-
CC 3)Man-beta-1-4GlcNAc-beta-1-4GlcNAc (at pH 7.5 and 23 degrees
CC Celsius) {ECO:0000269|PubMed:21515584};
CC Temperature dependence:
CC Optimum temperature is 23 degrees Celsius. No detectable activity at
CC 37 degrees Celsius. {ECO:0000269|PubMed:17369288};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288,
CC ECO:0000269|PubMed:9675224}.
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 -!- TISSUE SPECIFICITY: Expressed in the pharyngeal-intestinal (PI) and
CC anal valves. Expressed in ASG neurons and in one or two neurons in the
CC retrovesicular ganglion and two neurons posterior to the PI valve and
CC PHA and PHB neurons in the tail. {ECO:0000269|PubMed:17369288}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adult.
CC {ECO:0000269|PubMed:17369288}.
CC -!- DOMAIN: The C-terminus (424-433) is important for catalytic activity or
CC for enzyme stability. The N-terminus (1-78) appears to be dispensable
CC for enzymatic activity. {ECO:0000269|PubMed:21515584}.
CC -!- PTM: N-glycosylated (PubMed:17369288, PubMed:21515584). Glycosylation
CC is important for enzymatic activity (PubMed:21515584).
CC {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000255|RuleBase:RU003832}.
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DR EMBL; AJ745071; CAG32977.1; -; mRNA.
DR EMBL; BX284602; CAA91285.2; -; Genomic_DNA.
DR PIR; T23491; T23491.
DR RefSeq; NP_495862.2; NM_063461.5.
DR AlphaFoldDB; G5EDR5; -.
DR STRING; 6239.K08F8.3.1; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR EPD; G5EDR5; -.
DR PaxDb; G5EDR5; -.
DR PeptideAtlas; G5EDR5; -.
DR PRIDE; G5EDR5; -.
DR EnsemblMetazoa; K08F8.3.1; K08F8.3.1; WBGene00001505.
DR EnsemblMetazoa; K08F8.3.2; K08F8.3.2; WBGene00001505.
DR GeneID; 174400; -.
DR CTD; 174400; -.
DR WormBase; K08F8.3; CE32907; WBGene00001505; fut-1.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000175840; -.
DR HOGENOM; CLU_032075_8_0_1; -.
DR InParanoid; G5EDR5; -.
DR OMA; YLMFACC; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; G5EDR5; -.
DR BRENDA; 2.4.1.214; 1045.
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:G5EDR5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001505; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:WormBase.
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:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; IGI:UniProtKB.
DR GO; GO:0018392; F:glycoprotein 3-alpha-L-fucosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:WormBase.
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; Magnesium; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..433
FT /note="Alpha-(1,3)-fucosyltransferase fut-1"
FT /id="PRO_0000438178"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..433
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT SITE 243
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000269|PubMed:21515584"
FT SITE 267
FT /note="May be important for donor substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LJK1"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 194
FT /note="N->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 243
FT /note="S->A: 85 percent decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 303
FT /note="D->E: 80 percent decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 361
FT /note="T->A: 80 percent decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:21515584"
FT MUTAGEN 424..433
FT /note="Missing: Loss of catalytic activity and reduced
FT protein stability."
FT /evidence="ECO:0000269|PubMed:21515584"
SQ SEQUENCE 433 AA; 50004 MW; 6F18FEFE3100245B CRC64;
MTARSIKLFF ARWKYLMFAC CITYLLVIYA PISKSEQKDW KEGEIELSND HELDVPILQK
EELKPQQRPS FEENVPKKKT FNFNPVGKEP FDVEEVLTSS DIKLEERMTA TVIPGQKRLI
LSWNAGHSQD NLQGCPDWNC EFTQVRARAP DADAVLIAHM DNDFVPKPNQ YVVYFSQESP
ANSGIQIPRP DYINMTLGFR HDTPAGSPYG YTVKLGAKSR KTGQVVDANL VNGKAKGAAW
FVSHCQTNSK REDFVKKLQK HLQIDIYGGC GPMKCARGDS KCDTMLDTDY HFYVTFENSI
CEDYVTEKLW KSGYQNTIIP LVLKRKLVEP FVPPNSFIAI DDFKSVKEMG DYLNYLMNNK
TAYMEYFEWR HDYKVVFLDG SHHDVLERPW GFCQVCRMAW TEPRQKVLIP NWDAYWRQTC
EKDGTLVDSI PLD
