FUT10_MOUSE
ID FUT10_MOUSE Reviewed; 481 AA.
AC Q5F2L2; Q8C457; Q8K0S3; Q8R247;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 10;
DE EC=2.4.1.- {ECO:0000269|PubMed:23986452};
DE AltName: Full=Fucosyltransferase X;
DE Short=Fuc-TX;
DE Short=FucT-X;
DE AltName: Full=Galactoside 3-L-fucosyltransferase 10;
DE Short=Fucosyltransferase 10;
GN Name=Fut10 {ECO:0000303|PubMed:23986452, ECO:0000312|MGI:MGI:2384748};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Martinez-Duncker I., Oriol R., Mollicone R.;
RT "Phylogeny of fucosyltransferases.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Spinal cord;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 FUNCTION, PATHWAY, AND DEVELOPMENTAL STAGE.
RX PubMed=23986452; DOI=10.1074/jbc.m113.469403;
RA Kumar A., Torii T., Ishino Y., Muraoka D., Yoshimura T., Togayachi A.,
RA Narimatsu H., Ikenaka K., Hitoshi S.;
RT "The Lewis X-related alpha1,3-fucosyltransferase, Fut10, is required for
RT the maintenance of stem cell populations.";
RL J. Biol. Chem. 288:28859-28868(2013).
CC -!- FUNCTION: Predominantly fucosylates the innermost N-acetyl glucosamine
CC (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to
CC generate core alpha(1->3)-fucose epitope within the chitobiose unit of
CC biantennary N-glycans, providing for a recognition signal to reorient
CC aberrantly folded glycoproteins for degradation (By similarity).
CC Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that
CC regulate neuron stem cell self-renewal during brain development
CC (PubMed:23986452). {ECO:0000250|UniProtKB:Q6P4F1,
CC ECO:0000269|PubMed:23986452}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:23986452}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6P4F1}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6P4F1};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Fut10A;
CC IsoId=Q5F2L2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F2L2-2; Sequence=VSP_027509;
CC Name=3;
CC IsoId=Q5F2L2-3; Sequence=VSP_027507, VSP_027508;
CC -!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in liver
CC and thymus. {ECO:0000269|PubMed:12370785}.
CC -!- DEVELOPMENTAL STAGE: Expressed by Lewis X-positive neural precursor
CC cells in the ventricular and subventricular zones of 15.5 dpc embryonic
CC brain. {ECO:0000269|PubMed:23986452}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 10;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_617";
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DR EMBL; AJ880009; CAI53944.1; -; mRNA.
DR EMBL; AK083041; BAC38741.1; -; mRNA.
DR EMBL; AK147136; BAE27706.1; -; mRNA.
DR EMBL; AK169153; BAE40932.1; -; mRNA.
DR EMBL; BC022579; AAH22579.1; -; mRNA.
DR EMBL; BC030474; AAH30474.1; -; mRNA.
DR EMBL; BC062113; AAH62113.1; -; mRNA.
DR CCDS; CCDS22223.1; -. [Q5F2L2-1]
DR CCDS; CCDS52536.1; -. [Q5F2L2-2]
DR CCDS; CCDS72111.1; -. [Q5F2L2-3]
DR RefSeq; NP_001012535.1; NM_001012517.5. [Q5F2L2-1]
DR RefSeq; NP_001273351.1; NM_001286422.1. [Q5F2L2-1]
DR RefSeq; NP_001273353.1; NM_001286424.1. [Q5F2L2-2]
DR RefSeq; NP_001273354.1; NM_001286425.1. [Q5F2L2-3]
DR RefSeq; NP_598922.1; NM_134161.3. [Q5F2L2-2]
DR AlphaFoldDB; Q5F2L2; -.
DR STRING; 10090.ENSMUSP00000069816; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q5F2L2; 4 sites.
DR iPTMnet; Q5F2L2; -.
DR PhosphoSitePlus; Q5F2L2; -.
DR PaxDb; Q5F2L2; -.
DR PeptideAtlas; Q5F2L2; -.
DR PRIDE; Q5F2L2; -.
DR ProteomicsDB; 271647; -. [Q5F2L2-1]
DR ProteomicsDB; 271648; -. [Q5F2L2-2]
DR ProteomicsDB; 271649; -. [Q5F2L2-3]
DR Antibodypedia; 23343; 177 antibodies from 24 providers.
DR DNASU; 171167; -.
DR Ensembl; ENSMUST00000066173; ENSMUSP00000069816; ENSMUSG00000046152. [Q5F2L2-1]
DR Ensembl; ENSMUST00000110527; ENSMUSP00000106156; ENSMUSG00000046152. [Q5F2L2-3]
DR Ensembl; ENSMUST00000161502; ENSMUSP00000125265; ENSMUSG00000046152. [Q5F2L2-1]
DR Ensembl; ENSMUST00000161788; ENSMUSP00000124437; ENSMUSG00000046152. [Q5F2L2-2]
DR GeneID; 171167; -.
DR KEGG; mmu:171167; -.
DR UCSC; uc009ljj.2; mouse. [Q5F2L2-2]
DR UCSC; uc009ljk.2; mouse. [Q5F2L2-1]
DR UCSC; uc012gby.2; mouse. [Q5F2L2-3]
DR CTD; 84750; -.
DR MGI; MGI:2384748; Fut10.
DR VEuPathDB; HostDB:ENSMUSG00000046152; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000160287; -.
DR HOGENOM; CLU_032075_0_2_1; -.
DR InParanoid; Q5F2L2; -.
DR OMA; FTAQEFW; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q5F2L2; -.
DR TreeFam; TF316348; -.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 171167; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fut10; mouse.
DR PRO; PR:Q5F2L2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q5F2L2; protein.
DR Bgee; ENSMUSG00000046152; Expressed in embryonic post-anal tail and 151 other tissues.
DR Genevisible; Q5F2L2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:MGI.
DR GO; GO:0008417; F:fucosyltransferase activity; ISO:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0036071; P:N-glycan fucosylation; IDA:UniProtKB.
DR GO; GO:0036445; P:neuronal stem cell division; IMP:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
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 Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Alpha-(1,3)-fucosyltransferase 10"
FT /id="PRO_0000299003"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 127..136
FT /note="TDFNIDSLPL -> LTTQTMEGRC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027507"
FT VAR_SEQ 137..481
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027508"
FT VAR_SEQ 405..481
FT /note="GLPPKQWKADVSHLHCPEPALFTFSSPASPALRGRSLRELWLPSFQQSKKEA
FT QALRWLVDRNQNFSSEEFWALVFKD -> VSEWKSGGWHGPSLCVVLVFLLWWLPATGL
FT YS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027509"
FT CONFLICT 335
FT /note="S -> N (in Ref. 3; AAH22579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55707 MW; 4CEC3DB4469F754D CRC64;
MVRFQRRKLL ASCLCVTATV FLMVTLQVVV ELGKFERKKL KDSNVQDGHR DVEGEPKHLE
PFPEKEALAL AGRTKVDAGS YPIVLWWSPL TGETGRLGQC GADACFFTIN RTFQHHPMTR
AFLFYGTDFN IDSLPLPREA HHDWALFHEE SPKNNYKLFH KPVITLFNHT ATFSRHSHLP
LTTQYLEGVD VLKSLRYLVP LQAKNNLRQK LAPLVYVQSD CDPPSDRDSY VRELMAYIEV
DSYGECLQNR DLPQQLKNPA SMDADAFYRV IAQYKFILAF ENAVCDDYIT EKFWRPLKLG
VVPVYYGSPT IADWLPSNRS AILVSEFSHP RELASFIRRL DYDDGLYETY VEWKLKGKIS
NQRLLTALNE REWGVQDINQ DNYIDSFECM VCRRVWANSR LQEQGLPPKQ WKADVSHLHC
PEPALFTFSS PASPALRGRS LRELWLPSFQ QSKKEAQALR WLVDRNQNFS SEEFWALVFK
D
