FUT11_MOUSE
ID FUT11_MOUSE Reviewed; 489 AA.
AC Q8BHC9; Q9CXS9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11698403; DOI=10.1074/jbc.m107927200;
RA Roos C., Kolmer M., Mattila P., Renkonen R.;
RT "Composition of Drosophila melanogaster proteome involved in fucosylated
RT glycan metabolism.";
RL J. Biol. Chem. 277:3168-3175(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Head, Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=12370785; DOI=10.1007/s00335-001-2152-5;
RA Baboval T., Smith F.I.;
RT "Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression
RT studies in the mouse.";
RL Mamm. Genome 13:538-541(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
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 -!- TISSUE SPECIFICITY: Widely expressed. Expressed at slightly higher
CC level in heart, kidney and lung. {ECO:0000269|PubMed:12370785}.
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_mou_618";
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DR EMBL; AJ542393; CAD62573.1; -; mRNA.
DR EMBL; AK014029; BAB29123.1; -; mRNA.
DR EMBL; AK030310; BAC26892.1; -; mRNA.
DR EMBL; AK046461; BAC32740.1; -; mRNA.
DR EMBL; BC145735; AAI45736.1; -; mRNA.
DR CCDS; CCDS26851.1; -.
DR RefSeq; NP_082704.1; NM_028428.2.
DR AlphaFoldDB; Q8BHC9; -.
DR BioGRID; 215746; 12.
DR STRING; 10090.ENSMUSP00000040370; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR CarbonylDB; Q8BHC9; -.
DR GlyConnect; 2118; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8BHC9; 2 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q8BHC9; -.
DR PhosphoSitePlus; Q8BHC9; -.
DR EPD; Q8BHC9; -.
DR MaxQB; Q8BHC9; -.
DR PaxDb; Q8BHC9; -.
DR PRIDE; Q8BHC9; -.
DR ProteomicsDB; 273015; -.
DR Antibodypedia; 2883; 141 antibodies from 20 providers.
DR DNASU; 73068; -.
DR Ensembl; ENSMUST00000048016; ENSMUSP00000040370; ENSMUSG00000039357.
DR GeneID; 73068; -.
DR KEGG; mmu:73068; -.
DR UCSC; uc007skk.1; mouse.
DR CTD; 170384; -.
DR MGI; MGI:1920318; Fut11.
DR VEuPathDB; HostDB:ENSMUSG00000039357; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000158983; -.
DR HOGENOM; CLU_032075_0_1_1; -.
DR InParanoid; Q8BHC9; -.
DR OMA; ERIDCPR; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q8BHC9; -.
DR TreeFam; TF316348; -.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 73068; 6 hits in 71 CRISPR screens.
DR PRO; PR:Q8BHC9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BHC9; protein.
DR Bgee; ENSMUSG00000039357; Expressed in lumbar dorsal root ganglion and 225 other tissues.
DR ExpressionAtlas; Q8BHC9; baseline and differential.
DR Genevisible; Q8BHC9; MM.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..489
FT /note="Alpha-(1,3)-fucosyltransferase 11"
FT /id="PRO_0000299010"
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..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..99
FT /evidence="ECO:0000250"
FT DISULFID 385..388
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="A -> V (in Ref. 2; BAB29123)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="G -> R (in Ref. 2; BAB29123)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="G -> S (in Ref. 2; BAB29123)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="G -> R (in Ref. 2; BAB29123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55533 MW; 313E8EB8AE3A1345 CRC64;
MAARCTEAVL AALGVLSVCS ASSSGSEASG EAEREEPWDG AVFRPPAALG AVGIARGPGS
PPPGNREAVD LPVLLWWSPG LFPHFPGDSE RIQCAHGACV ASRDRRARAD PRTRALLFYG
TDFRAADAPL PRLAHQSWAL LHEESPLNNF LLSHGPGIRL FNLTATFSRH SDYPLPLQWL
PGAAYLRRPA PPPRERAEWR RRGYAPLLYL QSHCDVPSDR DRYVRELMRY IPVDSYGKCL
QNREPPTVRL QDTATATTED PELMAFLSRY KFHLALENAI CNDYMTEKLW RPMHLGAVPV
YRGSPSVRDW MPNNHSVILI DDFESPQKLA EFIDFLDKND DEYMKYLAYK QPGGITNQFL
LDNLEHREWG VNDPMLPNYL NGFECFVCDH ELARLNAEKA HASSHGDIPV PEPRIAQSSH
MNCPVPTPGF GKVEEIPEND SWKEMWLQDY WQGLYQGEAL TAMIHNNETQ QRKFWDYVHE
IFMKRNKNL
