ID A0A3Q2XAU7_HAPBU Unreviewed; 583 AA.
AC A0A3Q2XAU7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase {ECO:0000256|ARBA:ARBA00018201, ECO:0000256|PIRNR:PIRNR000472};
DE EC=2.4.1.68 {ECO:0000256|ARBA:ARBA00012660, ECO:0000256|PIRNR:PIRNR000472};
GN Name=FUT8 {ECO:0000313|Ensembl:ENSHBUP00000032435.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000032435.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000032435.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the
CC first GlcNAc residue, next to the peptide chains in N-glycans.
CC {ECO:0000256|ARBA:ARBA00002882, ECO:0000256|PIRNR:PIRNR000472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP +
CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC [alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein];
CC Xref=Rhea:RHEA:12985, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13532,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137207; EC=2.4.1.68;
CC Evidence={ECO:0000256|ARBA:ARBA00034431,
CC ECO:0000256|PIRNR:PIRNR000472};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|PIRNR:PIRNR000472}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004447}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC {ECO:0000256|PIRNR:PIRNR000472, ECO:0000256|PROSITE-ProRule:PRU00992}.
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DR RefSeq; XP_005921577.1; XM_005921515.2.
DR AlphaFoldDB; A0A3Q2XAU7; -.
DR STRING; 8153.ENSHBUP00000032435; -.
DR Ensembl; ENSHBUT00000025344.1; ENSHBUP00000032435.1; ENSHBUG00000018737.1.
DR GeneID; 102300482; -.
DR CTD; 100331714; -.
DR GeneTree; ENSGT00530000063737; -.
DR OMA; YHDIDEY; -.
DR OrthoDB; 2876062at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd11300; Fut8_like; 1.
DR CDD; cd11792; SH3_Fut8; 1.
DR Gene3D; 3.40.50.11350; -; 1.
DR Gene3D; 1.10.287.1060; ESAT-6-like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR015827; Fut8.
DR InterPro; IPR045573; Fut8_N_cat.
DR InterPro; IPR035653; Fut8_SH3.
DR InterPro; IPR027350; GT23_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13132; ALPHA- 1,6 -FUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR13132:SF29; ALPHA-(1,6)-FUCOSYLTRANSFERASE; 1.
DR Pfam; PF19745; FUT8_N_cat; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000472; Alpha1_6FUT_euk; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51659; GT23; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000472-52};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR000472};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR000472};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000472};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000472};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 207..494
FT /note="GT23"
FT /evidence="ECO:0000259|PROSITE:PS51659"
FT DOMAIN 503..564
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 366..367
FT /note="Important for donor substrate binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-50,
FT ECO:0000256|PROSITE-ProRule:PRU00992"
FT COILED 43..104
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 300..306
FT /note="SH3-binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-51"
FT DISULFID 205..267
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT DISULFID 213..231
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT DISULFID 219..223
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT DISULFID 466..473
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
SQ SEQUENCE 583 AA; 67001 MW; EDF6A03402DE942B CRC64;
MRPWAGSWRW ITLVLLAWGT LLFYIGGHLV RDSEHPERSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGQADAGSLA AGRLRSLEDQ LTRAKQKIHS FQKLTGDGPG PTQEELRRRV
ENGVKEFWYF VRSEVKKLAN VEPSERQKYA DTLLQDLGHQ ERSIMTDLYY LSQADGIGEW
RMKEAKDLSD LVQNRITYLQ NPPDCSKARK LVCNINKGCG YGCQLHHVVY CFMIAYGTQR
TLILESHNWR YAPGGWETVF LPVSNTCTDR SGATTGHWSG EAHDKDVQVV ELPIVDSLHP
RPPYLPLAIP EDLAPRLQRL HGDPSVWWVS QFVKYLVRPQ AWLEKEIQQT TAKLGFKHPI
IGVHVRRTDK VGTEAAFHPI EEYMLHVEEQ FQHLARRVHV DKKRVYLATD DPSLLQEAKT
KYPDYEFISD NSISWSAGLH NRYTENSLRG VILDIHFLSQ TDFLVCTFSS QVCRVAYEIM
QTLHPDASSF FYSLDDIYYF GGQNAHNQIA VYPHQPRNSE DIPLEPGDVI GVAGNHWDGY
SKGINRKLGR TGLYPSYKVR EKIETVKYPT YPEADKLLNS QNK
//
