FUT4_MOUSE
ID FUT4_MOUSE Reviewed; 433 AA.
AC Q11127;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 4;
DE AltName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase;
DE EC=2.4.1.152 {ECO:0000269|PubMed:11485743};
DE AltName: Full=Fucosyltransferase 4;
DE AltName: Full=Fucosyltransferase IV;
DE Short=Fuc-TIV;
DE Short=FucT-IV;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=Fut4; Synonyms=Elft;
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 [GENOMIC DNA].
RX PubMed=7559635; DOI=10.1074/jbc.270.42.25047;
RA Gersten K.M., Natsuka S., Trinchera M., Petryniak B., Kelly R.J.,
RA Hiraiwa N., Jenkins N.A., Gilbert D.J., Copeland N.G., Lowe J.B.;
RT "Molecular cloning, expression, chromosomal assignment, and tissue-specific
RT expression of a murine alpha-(1,3)-fucosyltransferase locus corresponding
RT to the human ELAM-1 ligand fucosyl transferase.";
RL J. Biol. Chem. 270:25047-25056(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT).
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8882722; DOI=10.1093/oxfordjournals.jbchem.a021239;
RA Ozawa M., Muramatsu T.;
RT "Molecular cloning and expression of a mouse alpha-1,3 fucosyltransferase
RT gene that shows homology with the human alpha-1,3 fucosyltransferase IV
RT gene.";
RL J. Biochem. 119:302-308(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=11485743; DOI=10.1016/s1074-7613(01)00166-2;
RA Homeister J.W., Thall A.D., Petryniak B., Maly P., Rogers C.E., Smith P.L.,
RA Kelly R.J., Gersten K.M., Askari S.W., Cheng G., Smithson G., Marks R.M.,
RA Misra A.K., Hindsgaul O., von Andrian U.H., Lowe J.B.;
RT "The alpha(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative
RT control over selectin-dependent leukocyte recruitment and lymphocyte
RT homing.";
RL Immunity 15:115-126(2001).
CC -!- FUNCTION: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred
CC from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2
CC lactosamine (LacNAc, Gal-beta(1->4)GlcNAc) glycan attached to N- or O-
CC linked glycoproteins (PubMed:11485743). Robustly fucosylates
CC nonsialylated distal LacNAc unit of the polylactosamine chain to form
CC Lewis X antigen (CD15), a glycan determinant known to mediate important
CC cellular functions in development and immunity. Fucosylates with lower
CC efficiency sialylated LacNAc acceptors to form sialyl Lewis X and 6-
CC sulfo sialyl Lewis X determinants that serve as recognition epitopes
CC for C-type lectins (PubMed:11485743). Together with FUT7 contributes to
CC SELE, SELL and SELP selectin ligand biosynthesis and selectin-dependent
CC lymphocyte homing, leukocyte migration and blood leukocyte homeostasis
CC (PubMed:11485743). In a cell type specific manner, may also fucosylate
CC the internal LacNAc unit of the polylactosamine chain to form VIM-2
CC antigen that serves as recognition epitope for SELE (By similarity).
CC {ECO:0000250|UniProtKB:P22083, ECO:0000269|PubMed:11485743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC EC=2.4.1.152; Evidence={ECO:0000269|PubMed:11485743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000269|PubMed:11485743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000269|PubMed:11485743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000269|PubMed:11485743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP +
CC H(+); Xref=Rhea:RHEA:68044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145343, ChEBI:CHEBI:176900;
CC Evidence={ECO:0000250|UniProtKB:P22083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045;
CC Evidence={ECO:0000250|UniProtKB:P22083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000269|PubMed:11485743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000269|PubMed:11485743};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11485743}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q11127-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q11127-2; Sequence=VSP_001778;
CC -!- TISSUE SPECIFICITY: Highest expression in stomach and colon. It is also
CC expressed in the lung, testis, uterus, small intestine and to a lesser
CC extent in spleen, and ovary. Present in trace amounts in brain, thymus,
CC heart, smooth muscle, kidney and bone marrow. Not found in liver,
CC salivary gland and pancreas.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate. No
CC visible phenotype; likely due to the redundancy with FUT7. Simultaneous
CC knockdown of FUT4 and FUT7 results in leukocytosis characterized by an
CC 18.4 fold increase in blood neutrophils and significant increases in
CC blood monocytes, eosinophils, and lymphocytes numbers.
CC {ECO:0000269|PubMed:11485743}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_613";
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DR EMBL; U33457; AAC52269.1; -; Genomic_DNA.
DR EMBL; D63380; BAA09697.1; -; Genomic_DNA.
DR EMBL; D63379; BAA09696.1; -; mRNA.
DR CCDS; CCDS22825.1; -. [Q11127-1]
DR PIR; A57596; A57596.
DR RefSeq; NP_034372.1; NM_010242.3. [Q11127-1]
DR AlphaFoldDB; Q11127; -.
DR IntAct; Q11127; 1.
DR STRING; 10090.ENSMUSP00000053027; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q11127; 2 sites.
DR iPTMnet; Q11127; -.
DR PhosphoSitePlus; Q11127; -.
DR PaxDb; Q11127; -.
DR PRIDE; Q11127; -.
DR ProteomicsDB; 271811; -. [Q11127-1]
DR ProteomicsDB; 271812; -. [Q11127-2]
DR Antibodypedia; 3496; 1963 antibodies from 46 providers.
DR DNASU; 14345; -.
DR Ensembl; ENSMUST00000061498; ENSMUSP00000053027; ENSMUSG00000049307. [Q11127-1]
DR GeneID; 14345; -.
DR KEGG; mmu:14345; -.
DR UCSC; uc009oew.1; mouse. [Q11127-1]
DR CTD; 2526; -.
DR MGI; MGI:95594; Fut4.
DR VEuPathDB; HostDB:ENSMUSG00000049307; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000162506; -.
DR HOGENOM; CLU_032075_4_0_1; -.
DR InParanoid; Q11127; -.
DR OMA; ANYERFM; -.
DR PhylomeDB; Q11127; -.
DR TreeFam; TF316348; -.
DR BRENDA; 2.4.1.152; 3474.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14345; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fut4; mouse.
DR PRO; PR:Q11127; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q11127; protein.
DR Bgee; ENSMUSG00000049307; Expressed in left colon and 119 other tissues.
DR ExpressionAtlas; Q11127; baseline and differential.
DR Genevisible; Q11127; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
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:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; IMP:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:1903037; P:regulation of leukocyte cell-cell adhesion; ISS:UniProtKB.
DR Gene3D; 3.40.50.11660; -; 1.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Inflammatory response; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..433
FT /note="Alpha-(1,3)-fucosyltransferase 4"
FT /id="PRO_0000221101"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..433
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8882722"
FT /id="VSP_001778"
FT CONFLICT 252
FT /note="Q -> P (in Ref. 2; BAA09697)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> Q (in Ref. 2; BAA09697)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="V -> E (in Ref. 2; BAA09697)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="R -> Q (in Ref. 2; BAA09697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 49481 MW; 2401822F02B5D021 CRC64;
MAPARQELQH ESRCRPSRTV DAWRAAVATR GRHMETPGYR RRTRCGGWGL PRSVSSLAAV
GLLCTALTTF ICWGQLPPLP WASPAPQRLV GVLLWWEPFR GRGGYPKSPP DCSLRFNISG
CRLLTDRAAY GEAQAVLFHH RDLVKELHDW PPPWGARERT DKALVLRVFD DQEGAVTLTG
KALETVGSRP PGQRWVWMNF ESPSHTPGLR GLAKDLFNWT LSYRTDSDVF VPYGFLYSRS
DPTEQPSGLG PQLARKRGLV AWVVSNWNEH QARVRYYHQL SRHVSVDVFG RTGPGRPVPA
IGLLHTVARY KFYLAFENSR HVDYITEKLW RNAFLAGAVP VVLGPDRANY ERFVPRGAFI
HVDDFPNAAS LAAYLLFLDR NVAVYRRYFR WRRSFAVHIT SFWDEQWCRT CQAVQTSGDQ
PKSIHNLADW FQR
