FUTB1_CAEEL
ID FUTB1_CAEEL Reviewed; 355 AA.
AC P91200;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Galactoside 2-alpha-L-fucosyltransferase {ECO:0000312|EMBL:CCD68841.1};
DE EC=2.4.1.- {ECO:0000269|PubMed:12163507};
DE AltName: Full=Alpha-(1,2)-fucosyltransferase fut-2 {ECO:0000303|PubMed:12163507};
DE AltName: Full=Fucosyltransferase fut-2 {ECO:0000312|WormBase:EGAP9.2};
GN Name=fut-2 {ECO:0000312|WormBase:EGAP9.2};
GN Synonyms=CE2FT-1 {ECO:0000303|PubMed:12163507};
GN ORFNames=EGAP9.2 {ECO:0000312|WormBase:EGAP9.2};
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|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 [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12163507; DOI=10.1074/jbc.m207487200;
RA Zheng Q., Van Die I., Cummings R.D.;
RT "Molecular cloning and characterization of a novel alpha 1,2-
RT fucosyltransferase (CE2FT-1) from Caenorhabditis elegans.";
RL J. Biol. Chem. 277:39823-39832(2002).
CC -!- FUNCTION: Selectively catalyzes the addition of fucose in alpha 1-2
CC linkage to Gal-beta-(1->4)-Xyl-beta-R, Gal-beta-(1->6)-GlcNAc-R, Gal-
CC beta-(1->3)-Gal-beta-(1->4)-Glc and Gal-beta-(1->3)-Gal-beta-(1->4)-
CC Xyl-R acceptors but not Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-
CC (1->4)-Glc. Unlike in mammals, unable to fucosylate Gal-beta-(1->4)-
CC Glc-beta-R. {ECO:0000269|PubMed:12163507}.
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305|PubMed:12163507}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:12163507}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the 20 intestinal cells
CC in larvae and adult. {ECO:0000269|PubMed:12163507}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adult.
CC {ECO:0000269|PubMed:12163507}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD68841.1; -; Genomic_DNA.
DR PIR; T34405; T34405.
DR RefSeq; NP_504671.1; NM_072270.1.
DR AlphaFoldDB; P91200; -.
DR STRING; 6239.EGAP9.2; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR EPD; P91200; -.
DR PaxDb; P91200; -.
DR PeptideAtlas; P91200; -.
DR EnsemblMetazoa; EGAP9.2.1; EGAP9.2.1; WBGene00001506.
DR GeneID; 184050; -.
DR KEGG; cel:CELE_EGAP9.2; -.
DR UCSC; EGAP9.2; c. elegans.
DR CTD; 184050; -.
DR WormBase; EGAP9.2; CE09151; WBGene00001506; fut-2.
DR eggNOG; ENOG502SGEF; Eukaryota.
DR GeneTree; ENSGT00530000064380; -.
DR HOGENOM; CLU_785801_0_0_1; -.
DR InParanoid; P91200; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; P91200; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P91200; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001506; Expressed in embryo 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:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:WormBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043413; P:macromolecule glycosylation; IDA:WormBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002516; Glyco_trans_11.
DR Pfam; PF01531; Glyco_transf_11; 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..355
FT /note="Galactoside 2-alpha-L-fucosyltransferase"
FT /id="PRO_0000438176"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..355
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 355 AA; 41538 MW; 9DB8C0909A40DA76 CRC64;
MRNVKGLFSY MTKTKSFYIS IIVIIFIIFI VNRMGPRNYN YKQIGTEINC VKHKVDEQRY
LLFPMITILY KYGLGNQLFE VFSLLGSAQT LNRTAIFNAD DDILQSKLDL LQKQVPQVAA
RIISIPIEIA ESTRYLFLPA CCHYQFPSLF SCERSKFLVI DGQYFQSFKY FSAIDSLIRK
LLKPPIDEEI ILKKMIGRKD ELRFKNCVHI RRGDYVNDFD HAETSSYFTI RAIDYVHTLH
PGLVYLISDD PKWVRKQIAE HLDYHDDVKI METPINAAIR DLYFSQAHCD SVLITAPSST
FGWWIGYMSK NQSNVYYRDI QETDDMVKYK MVEEDFFPPT WKKLGMSRNG SIISK
