FUTB2_CAEEL
ID FUTB2_CAEEL Reviewed; 402 AA.
AC A5Z2X3; G5EFK3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Galactoside 2-alpha-L-fucosyltransferase {ECO:0000312|EMBL:CAN99658.1};
DE EC=2.4.1.- {ECO:0000269|PubMed:18252778};
DE AltName: Full=Alpha-(1,2)-L-fucosyltransferase {ECO:0000303|PubMed:18252778};
DE AltName: Full=CE2FT-2 {ECO:0000303|PubMed:18252778};
GN ORFNames=F08A8.5 {ECO:0000312|WormBase:F08A8.5b};
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:ABK20307.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND GLYCOSYLATION.
RX PubMed=18252778; DOI=10.1093/glycob/cwn007;
RA Zheng Q., Van Die I., Cummings R.D.;
RT "A novel alpha1,2-fucosyltransferase (CE2FT-2) in Caenorhabditis elegans
RT generates H-type 3 glycan structures.";
RL Glycobiology 18:290-302(2008).
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).
CC -!- FUNCTION: Selectively catalyzes the addition of fucose in alpha 1-2
CC linkage to Gal-beta-(1->3)-GalNAc-alpha-R, Gal-beta-(1->3)-(GlcNAc-
CC beta-(1->6))-GalNAc-alpha-R and Gal-beta-(1->3)-GalNAc acceptors but
CC not Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc in vitro.
CC {ECO:0000269|PubMed:18252778}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for Gal-beta-1-3GalNAc-alpha-O-pNP at 25 degrees Celsius
CC {ECO:0000269|PubMed:18252778};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: May form oligomers. {ECO:0000269|PubMed:18252778}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F08A8.5b};
CC IsoId=A5Z2X3-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F08A8.5a};
CC IsoId=A5Z2X3-2; Sequence=VSP_058619;
CC -!- TISSUE SPECIFICITY: Expression is restricted to pharyngeal neurons and
CC gland cells. {ECO:0000269|PubMed:18252778}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adult.
CC {ECO:0000269|PubMed:18252778}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18252778}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; EF015633; ABK20307.1; -; mRNA.
DR EMBL; BX284601; CAB16868.1; -; Genomic_DNA.
DR EMBL; BX284601; CAN99658.1; -; Genomic_DNA.
DR PIR; T20572; T20572.
DR RefSeq; NP_001122446.1; NM_001128974.1. [A5Z2X3-1]
DR RefSeq; NP_493265.1; NM_060864.1. [A5Z2X3-2]
DR AlphaFoldDB; A5Z2X3; -.
DR STRING; 6239.F08A8.5b; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR PaxDb; A5Z2X3; -.
DR EnsemblMetazoa; F08A8.5a.1; F08A8.5a.1; WBGene00008568. [A5Z2X3-2]
DR EnsemblMetazoa; F08A8.5b.1; F08A8.5b.1; WBGene00008568. [A5Z2X3-1]
DR GeneID; 184168; -.
DR KEGG; cel:CELE_F08A8.5; -.
DR UCSC; F08A8.5b; c. elegans. [A5Z2X3-1]
DR CTD; 184168; -.
DR WormBase; F08A8.5a; CE17637; WBGene00008568; -. [A5Z2X3-2]
DR WormBase; F08A8.5b; CE41218; WBGene00008568; -. [A5Z2X3-1]
DR eggNOG; ENOG502T8JY; Eukaryota.
DR GeneTree; ENSGT00530000064380; -.
DR InParanoid; A5Z2X3; -.
DR OMA; PEWIKLK; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; A5Z2X3; -.
DR SABIO-RK; A5Z2X3; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:A5Z2X3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008568; Expressed in pharyngeal muscle cell (C elegans) and 2 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043413; P:macromolecule glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..402
FT /note="Galactoside 2-alpha-L-fucosyltransferase"
FT /id="PRO_0000438177"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..402
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 52..70
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058619"
SQ SEQUENCE 402 AA; 46619 MW; C19BBC8957CA2231 CRC64;
MRYNSNYLMY FCLVLGIFAN IYVIIKITLG SSHILEYFQK NSNLSPKCEI NVNNLLSFIE
NRHFLDLEQK NSQKSQPNYE KTLQLMLFAF PSGGLGNKLF EIISLHGIAT SLQRKAVINA
TNPSFIETLN RNIQPLFPKL ADQFTLRIIP DSLVTHQQTN WGRCCVYDDP SRFLNRSDQN
LILDGHYFQS FKYFHHIRPQ VREWLAPSKL QAMRAEILLP AKFRDDFLIC THVRRGDFQY
DGLHRPSDAT FTRAATDFLV DLYRKSHERV NVVVLGNDIH FAYTVFEDRV AHFTFLQKPV
NNSYDYSLPQ ISPSYTAILT PTLTPEIDLA FSRLFCDVTL ITAPSSTFGW WLSYLAKRTA
TTYYRDILES KDGVAGEMHP EDFYPPEWIK LKTDLNGKIS KY
