ID   FUT11_RAT               Reviewed;         494 AA.
AC   Q68FV3; Q8CG40;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Alpha-(1,3)-fucosyltransferase 11;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:Q495W5};
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Candelier J.-J., Martinez-Duncker I., Oriol R., Mollicone R.;
RT   "Cloning, expression and genomic organization of a new human alpha3-
RT   fucosyltransferase (FUT11).";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- FUNCTION: Has fucosyltransferase activity toward biantennary N-glycan
CC       acceptors. Does not fucosylate GlcNAc residue within type 2 lactosamine
CC       unit. {ECO:0000250|UniProtKB:Q495W5}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q495W5}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ535753; CAD59737.1; -; mRNA.
DR   EMBL; BC079316; AAH79316.1; -; mRNA.
DR   RefSeq; NP_775430.2; NM_173308.2.
DR   AlphaFoldDB; Q68FV3; -.
DR   SMR; Q68FV3; -.
DR   STRING; 10116.ENSRNOP00000012300; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   GlyGen; Q68FV3; 1 site.
DR   PhosphoSitePlus; Q68FV3; -.
DR   PaxDb; Q68FV3; -.
DR   PRIDE; Q68FV3; -.
DR   Ensembl; ENSRNOT00000012300; ENSRNOP00000012300; ENSRNOG00000009274.
DR   GeneID; 286971; -.
DR   KEGG; rno:286971; -.
DR   UCSC; RGD:628731; rat.
DR   CTD; 170384; -.
DR   RGD; 628731; Fut11.
DR   eggNOG; KOG2619; Eukaryota.
DR   GeneTree; ENSGT00940000158983; -.
DR   HOGENOM; CLU_032075_0_1_1; -.
DR   InParanoid; Q68FV3; -.
DR   OMA; ERIDCPR; -.
DR   OrthoDB; 551308at2759; -.
DR   PhylomeDB; Q68FV3; -.
DR   TreeFam; TF316348; -.
DR   Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q68FV3; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000009274; Expressed in ovary and 18 other tissues.
DR   Genevisible; Q68FV3; RN.
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; ISS:UniProtKB.
DR   GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR   GO; GO:0036071; P:N-glycan fucosylation; ISS: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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="Alpha-(1,3)-fucosyltransferase 11"
FT                   /id="PRO_0000299011"
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..494
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        99..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        390..393
FT                   /evidence="ECO:0000250"
FT   CONFLICT        41..42
FT                   /note="EP -> A (in Ref. 1; CAD59737)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281..283
FT                   /note="MEN -> LEK (in Ref. 1; CAD59737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  56000 MW;  6EA3AB50641272D4 CRC64;
     MAARYTEAVL AALGVLSVCS ASSSSGSGAS GKAGGEAEWA EPWDGAVFRP PAALGAVGMT
     RGLGSPPPGN AETVDLPVLL WWSPGLFPHF PGDSERIECA LGACVASRDR RARADPRTRA
     LLFYGTDFRA ADAPLPRLAH QSWALLHEES PLNNFLLSHG PGIRLFNLTA TFSRHSDYPL
     PLQWLPGAAY LRRPAPPLRE RAEWRRRGYA PLLYLQSHCD VPSDRDRYVR ELMRYIPVDS
     YGKCLQNREP PTVRLQDTAT ATTEDPELMA FLSRYKFHLA MENAICNDYM TEKLWRPMHL
     GAVPVYRGSP SVRDWMPNNH SVILIDDFES PQKLAEFIDF LDKNDEEYMK YLAYKQPGGI
     TNQFLLDNLE HREWGVNDPM LPNYLNGFEC FVCDHELARL DAEKAHESSP RDIPVLEPHI
     AQLSHMDCPV PTPGFGKVEE IPENDSWKEM WLQDYWQGLY QGEALTAMIH NNETQQSKFW
     DYVHEIFMKR NKNL