FUT10_RAT
ID FUT10_RAT Reviewed; 483 AA.
AC Q5F2L1; Q5F2N5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 10;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q5F2L2, ECO:0000250|UniProtKB:Q6P4F1};
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;
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Wistar;
RA Martinez-Duncker I., Oriol R., Mollicone R.;
RT "Phylogeny of fucosyltransferases.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q5F2L2,
CC ECO:0000250|UniProtKB:Q6P4F1}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q6P4F1}.
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=2;
CC Name=1; Synonyms=Fut10A;
CC IsoId=Q5F2L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F2L1-2; Sequence=VSP_027510;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ880010; CAI53945.1; -; mRNA.
DR EMBL; AJ879584; CAI52074.1; -; mRNA.
DR RefSeq; NP_001012360.1; NM_001012360.1. [Q5F2L1-2]
DR AlphaFoldDB; Q5F2L1; -.
DR SMR; Q5F2L1; -.
DR STRING; 10116.ENSRNOP00000065788; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q5F2L1; 4 sites.
DR PaxDb; Q5F2L1; -.
DR GeneID; 497619; -.
DR KEGG; rno:497619; -.
DR CTD; 84750; -.
DR RGD; 1359164; Fut10.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q5F2L1; -.
DR PhylomeDB; Q5F2L1; -.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5F2L1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0046920; F:alpha-(1->3)-fucosyltransferase activity; ISO:RGD.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0036071; P:N-glycan fucosylation; ISS:UniProtKB.
DR GO; GO:0036445; P:neuronal stem cell division; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:RGD.
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..483
FT /note="Alpha-(1,3)-fucosyltransferase 10"
FT /id="PRO_0000299004"
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..483
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 405..483
FT /note="GLPPKQWKADVSHLHCPEPTLFAFSSPASPALRGRSLRELWLPSFQQSKKEA
FT QALRWLVDRNQNFSSEEFWALVFKDSF -> VSGWKSGGGRGLSLGVVLVFLLWLLPAT
FT VLHS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027510"
SQ SEQUENCE 483 AA; 56025 MW; B31AA416A6CB2D4B CRC64;
MVRIPRRKLL PSCLCMTATV FLMVTVQVLV ELGKFERKKF KNSDLQDGQK DVEGDPKHLN
PLPKKDALAL SGRNKVDAGS YPIVLWWSPL TGETGRLGQC GADACFFTIN RTFQHHPMTK
AFLFYGTDFN IDSLPLPRKA HHDWALFHEE SPKNNYKLFH KPVITLFNHT ATFSRHSDLP
LTTQYLESVE VLKSLRYLVP LQSKNNLRQK LAPLVYVQSD CDPPSDRDSY VRELMAYIEV
DSYGECLQNK HLPQQLKNPA SMDADAFYRV LAQYKFILAF ENAVCDDYIT EKFWRPLKLG
VVPVYYGSPT IADWLPSNRS AILVSEFSHP RELASFIRRL DYDDGLYETY VEWKLKGEIS
NQRLLTALRE REWGVQDINQ DNYIDTFECM VCRRVWANRR LQEQGLPPKQ WKADVSHLHC
PEPTLFAFSS PASPALRGRS LRELWLPSFQ QSKKEAQALR WLVDRNQNFS SEEFWALVFK
DSF
