FUT4_PANTR
ID FUT4_PANTR Reviewed; 530 AA.
AC Q659K9;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
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;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 126-530.
RA Martinez-Duncker I., Oriol R., Mollicone R.;
RT "Phylogeny of fucosyltransferases.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ831840; CAH41983.1; -; mRNA.
DR RefSeq; NP_001008985.2; NM_001008985.2.
DR AlphaFoldDB; Q659K9; -.
DR STRING; 9598.ENSPTRP00000047698; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; Q659K9; -.
DR Ensembl; ENSPTRT00000055239; ENSPTRP00000047698; ENSPTRG00000028425.
DR GeneID; 449507; -.
DR KEGG; ptr:449507; -.
DR CTD; 2526; -.
DR VGNC; VGNC:3125; FUT4.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000162506; -.
DR HOGENOM; CLU_032075_4_0_1; -.
DR InParanoid; Q659K9; -.
DR OMA; ANYERFM; -.
DR OrthoDB; 551308at2759; -.
DR TreeFam; TF316348; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000028425; Expressed in lymph node and 17 other tissues.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
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; ISS: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; 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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Inflammatory response;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..530
FT /note="Alpha-(1,3)-fucosyltransferase 4"
FT /id="PRO_0000221102"
FT TOPO_DOM 1..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..172
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..530
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 59183 MW; 9EDB5428FAA420AE CRC64;
MRRLWGAARK PSGAGWEKEW AEAPQEAPGA WSGRLGPGRS GRKGRAVPGW ASWPAHLALA
ARPARHLGGA GQGPRPLDSG TAPFHSRASG ERQRRLEPQL QHESRCRSST PADAWRAEAA
LPVRAMGAPW GSPTAAAGGR RRWRRGRGLP WTVCVLAAAG LTCTALITYA CWGQLPPLPW
ASPTPSRPVG VLLWWEPFAG RHSAPRPPPD CRLRFNISGC RLLTDRASYG EAQAVLFHHR
DLVKGPPDWP PPWGVQAHTA EEVDLRVLDY EEAAAAAEAL ATSSPRPPGQ RWVWMNFESP
SHSPGLRSLA SNLFNWTLSY RADSDVFVPY GYLYPRSHPG DPPSGLAPPL SRKQGLVAWV
VSHWDERQAR VRYYHQLSQH VTVDVFGRGG PGQPVPEIGL LHTVARYKFY LAFENSQHLD
YITEKLWRNA LLAGAVPVVL GPDRANYERF VPRGAFIHVD DFPSASSLAS YLLFLDRNPA
VYRRYFHWRR SYAVHITSFW DEPWCRVCQA VQRAGDRPKS IRNLASWFER
