FUT11_HUMAN
ID FUT11_HUMAN Reviewed; 492 AA.
AC Q495W5; Q495W7; Q8IYE4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 11;
DE EC=2.4.1.- {ECO:0000269|PubMed:19088067};
DE AltName: Full=Fucosyltransferase XI;
DE Short=Fuc-TXI;
DE Short=FucT-XI;
DE AltName: Full=Galactoside 3-L-fucosyltransferase 11;
DE Short=Fucosyltransferase 11;
GN Name=FUT11 {ECO:0000303|PubMed:19088067, ECO:0000312|HGNC:HGNC:19233};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-51.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-443.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [3]
RP FUNCTION (ISOFORMS 1 AND 2), AND PATHWAY.
RX PubMed=19088067; DOI=10.1074/jbc.m809312200;
RA Mollicone R., Moore S.E., Bovin N., Garcia-Rosasco M., Candelier J.J.,
RA Martinez-Duncker I., Oriol R.;
RT "Activity, splice variants, conserved peptide motifs, and phylogeny of two
RT new alpha1,3-fucosyltransferase families (FUT10 and FUT11).";
RL J. Biol. Chem. 284:4723-4738(2009).
CC -!- FUNCTION: [Isoform 1]: Has minor fucosyltransferase activity toward
CC biantennary N-glycan acceptors. Does not fucosylate GlcNAc residue
CC within type 2 lactosamine unit. {ECO:0000269|PubMed:19088067}.
CC -!- FUNCTION: [Isoform 2]: Has fucosyltransferase activity toward
CC biantennary N-glycan acceptors. Does not fucosylate GlcNAc residue
CC within type 2 lactosamine unit. {ECO:0000269|PubMed:19088067}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:19088067}.
CC -!- INTERACTION:
CC Q495W5; P50222: MEOX2; NbExp=3; IntAct=EBI-2907712, EBI-748397;
CC Q495W5; Q04864: REL; NbExp=3; IntAct=EBI-2907712, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q495W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q495W5-2; Sequence=VSP_027511;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 11;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_608";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC036037; AAH36037.1; -; mRNA.
DR EMBL; BC100994; AAI00995.1; -; mRNA.
DR EMBL; BC100995; AAI00996.1; -; mRNA.
DR EMBL; BC100996; AAI00997.1; -; mRNA.
DR EMBL; BC100997; AAI00998.1; -; mRNA.
DR CCDS; CCDS60558.1; -. [Q495W5-2]
DR CCDS; CCDS7333.1; -. [Q495W5-1]
DR RefSeq; NP_001271123.1; NM_001284194.1. [Q495W5-2]
DR RefSeq; NP_775811.2; NM_173540.2. [Q495W5-1]
DR AlphaFoldDB; Q495W5; -.
DR BioGRID; 128001; 128.
DR IntAct; Q495W5; 24.
DR STRING; 9606.ENSP00000361932; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q495W5; 4 sites.
DR iPTMnet; Q495W5; -.
DR PhosphoSitePlus; Q495W5; -.
DR BioMuta; FUT11; -.
DR DMDM; 121943313; -.
DR EPD; Q495W5; -.
DR jPOST; Q495W5; -.
DR MassIVE; Q495W5; -.
DR MaxQB; Q495W5; -.
DR PaxDb; Q495W5; -.
DR PeptideAtlas; Q495W5; -.
DR PRIDE; Q495W5; -.
DR ProteomicsDB; 61975; -. [Q495W5-1]
DR ProteomicsDB; 61976; -. [Q495W5-2]
DR Antibodypedia; 2883; 141 antibodies from 20 providers.
DR DNASU; 170384; -.
DR Ensembl; ENST00000372841.8; ENSP00000361932.3; ENSG00000196968.11. [Q495W5-1]
DR Ensembl; ENST00000394790.2; ENSP00000378270.1; ENSG00000196968.11. [Q495W5-2]
DR GeneID; 170384; -.
DR KEGG; hsa:170384; -.
DR MANE-Select; ENST00000372841.8; ENSP00000361932.3; NM_173540.3; NP_775811.2.
DR UCSC; uc001juz.3; human. [Q495W5-1]
DR CTD; 170384; -.
DR DisGeNET; 170384; -.
DR GeneCards; FUT11; -.
DR HGNC; HGNC:19233; FUT11.
DR HPA; ENSG00000196968; Low tissue specificity.
DR neXtProt; NX_Q495W5; -.
DR OpenTargets; ENSG00000196968; -.
DR PharmGKB; PA134914077; -.
DR VEuPathDB; HostDB:ENSG00000196968; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000158983; -.
DR HOGENOM; CLU_032075_0_1_1; -.
DR InParanoid; Q495W5; -.
DR OMA; ERIDCPR; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q495W5; -.
DR TreeFam; TF316348; -.
DR BRENDA; 2.4.1.152; 2681.
DR BRENDA; 2.4.1.65; 2681.
DR PathwayCommons; Q495W5; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q495W5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 170384; 19 hits in 1074 CRISPR screens.
DR ChiTaRS; FUT11; human.
DR GenomeRNAi; 170384; -.
DR Pharos; Q495W5; Tbio.
DR PRO; PR:Q495W5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q495W5; protein.
DR Bgee; ENSG00000196968; Expressed in sperm and 180 other tissues.
DR Genevisible; Q495W5; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0036071; P:N-glycan fucosylation; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR017176; Alpha-1_3-FUT_met.
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.
DR PIRSF; PIRSF037332; Alpha1_3FUT_met; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Alpha-(1,3)-fucosyltransferase 11"
FT /id="PRO_0000299009"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..492
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 98..103
FT /evidence="ECO:0000250"
FT DISULFID 389..392
FT /evidence="ECO:0000250"
FT VAR_SEQ 446..492
FT /note="WKEMWLQDYWQGLDQGEALTAMIHNNETEQTKFWDYLHEIFMKRQHL -> S
FT LVQVRDHCICLRFLWPHSEKGRTHNYAAVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027511"
FT VARIANT 51
FT /note="S -> A (in dbSNP:rs17853514)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034763"
SQ SEQUENCE 492 AA; 55816 MW; 19ED65D27DA6B30E CRC64;
MAAGPIRVVL VLLGVLSVCA ASGHGSVAER EAGGEAEWAE PWDGAVFRPP SALGAVGVTR
SSGTPRPGRE EAGDLPVLLW WSPGLFPHFP GDSERIECAR GACVASRNRR ALRDSRTRAL
LFYGTDFRAS AAPLPRLAHQ SWALLHEESP LNNFLLSHGP GIRLFNLTST FSRHSDYPLS
LQWLPGTAYL RRPVPPPMER AEWRRRGYAP LLYLQSHCDV PADRDRYVRE LMRHIPVDSY
GKCLQNRELP TARLQDTATA TTEDPELLAF LSRYKFHLAL ENAICNDYMT EKLWRPMHLG
AVPVYRGSPS VRDWMPNNHS VILIDDFESP QKLAEFIDFL DKNDEEYMKY LAYKQPGGIT
NQFLLDSLKH REWGVNDPLL PNYLNGFECF VCDYELARLD AEKAHAASPG DSPVFEPHIA
QPSHMDCPVP TPGFGNVEEI PENDSWKEMW LQDYWQGLDQ GEALTAMIHN NETEQTKFWD
YLHEIFMKRQ HL
