FUT4_RAT
ID FUT4_RAT Reviewed; 433 AA.
AC Q62994;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
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:0000250|UniProtKB:P22083, ECO:0000250|UniProtKB:Q11127};
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=Rfuc-t;
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 [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=9111142; DOI=10.1023/a:1018550023637;
RA Sajdel-Sulkowska E.M., Smith F.I., Wiederschain G., McCluer R.H.;
RT "Cloning of a rat alpha1,3-fucosyltransferase gene: a member of the
RT fucosyltransferase IV family.";
RL Glycoconj. J. 14:249-258(1997).
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. Robustly fucosylates nonsialylated distal LacNAc
CC unit of the polylactosamine chain to form Lewis X antigen (CD15), a
CC glycan determinant known to mediate important cellular functions in
CC development and immunity. Fucosylates with lower efficiency sialylated
CC LacNAc acceptors to form sialyl Lewis X and 6-sulfo sialyl Lewis X
CC determinants that serve as recognition epitopes for C-type lectins.
CC Together with FUT7 contributes to SELE, SELL and SELP selectin ligand
CC biosynthesis and selectin-dependent lymphocyte homing, leukocyte
CC migration and blood leukocyte homeostasis (By similarity). In a cell
CC type specific manner, may also fucosylate the internal LacNAc unit of
CC the polylactosamine chain to form VIM-2 antigen that serves as
CC recognition epitope for SELE (By similarity).
CC {ECO:0000250|UniProtKB:P22083, ECO:0000250|UniProtKB:Q11127}.
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:0000250|UniProtKB:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
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:0000250|UniProtKB:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
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:0000250|UniProtKB:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11127}.
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=Q62994-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q62994-2; Sequence=VSP_001779;
CC -!- TISSUE SPECIFICITY: In adult, highest expression in spleen, testis,
CC brain, lung, kidney and skeletal muscle and to a lesser extent in liver
CC and heart.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; U58860; AAB97609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q62994; -.
DR STRING; 10116.ENSRNOP00000012176; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q62994; 2 sites.
DR PaxDb; Q62994; -.
DR UCSC; RGD:619954; rat. [Q62994-1]
DR RGD; 619954; Fut4.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q62994; -.
DR PhylomeDB; Q62994; -.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q62994; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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:RGD.
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; ISS:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; ISS: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 2: Evidence at transcript 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_0000221103"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..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 REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000305"
FT /id="VSP_001779"
SQ SEQUENCE 433 AA; 48779 MW; 75B0E569B72FD2F8 CRC64;
MAPAGRKLQH ESRCRPSRPV DAWRAAATTR GRCMGTPGAR RTARRGGWGL PRTSSGLAAA
GLLCTALTAC LCWGQLPPLP WASPAPQRPV SVLLWWEPFG GRGGHSKPPP DCSLRFNISG
CRLLTDRAAY GEAQAVLFHH RDLVKGPPDW PPPWGAQERT DEALELRVFD DQEGAVMLAR
EALETTGSRP PGQRWVWMNF ESPSHTPGLR GLAKDLFNWT LSYRTDSDIF VPYGFLYPRS
HPAEQPSGLG PPLARKRGLV AWVVSHWNER QARVRYYHQL RRHVSVDVFG RAGPGQPVPA
VGLLHTVARY KFYLAFENSQ HVDYNTEKLW RNAFLAGAVP VLLGPDRANY EGFVPRGSFI
HVDDFPSAAS LAAYLLFLDR NVAVYRRYFH WRRSYAVHIT SFWDEPWCQT CRAVQTSGDQ
PKSIHNLADW FQR
