ID A0A3Q3X5C2_MOLML Unreviewed; 546 AA.
AC A0A3Q3X5C2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000020479.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000020479.1}
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 AlphaFoldDB; A0A3Q3X5C2; -.
DR STRING; 94237.ENSMMOP00000020479; -.
DR Ensembl; ENSMMOT00000020819.1; ENSMMOP00000020479.1; ENSMMOG00000015572.1.
DR OMA; TYCAITA; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000261620; 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; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000472; Alpha1_6FUT_euk; 2.
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 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:UP000261620};
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 170..457
FT /note="GT23"
FT /evidence="ECO:0000259|PROSITE:PS51659"
FT DOMAIN 466..527
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 329..330
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 263..269
FT /note="SH3-binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR000472-51"
SQ SEQUENCE 546 AA; 62758 MW; 4EEA724B33D8CF88 CRC64;
MRPWAGSWRW ITLVLLAWGT LLFYIGGHLV RDSEHPERSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGQAEAGSLA AGRLRSLEEE LTRAKQKIHS FQKLTGDGKH EELRRRVENG
VKEFWYFVRS EVKKLANVEP GEGQKYADAL LQDLGHQERC AYSQAIKKIK AKKLVCNINK
GCGYGCQLHH VVYCFMIAYG TQRTLILESH NWRYAPGGWE TVFLPVSNTC TDRSGASTGH
WSGEAHDKDV QVVELPIVDS LHPRPPYLPL AIPEDLAPRL HRLHGDPSVW WVSQFVKYLV
RPQAWLEKEI QQTMAKLGFK HPIIGVHVRR TDKVGTEAAF HPIEEYMQHV EEQFQLLARR
VHVDKKRVYL ATDDPSLLQE AKTKYPDYEF ISDNSISWSA GLHNRYTENS LRGVILDIHF
LSQTDFLVCT FSSQVCRVAY ELMQMLHPDA SSFFYSLDDI YYFGGQNAHN QIAIYHHQPR
NNEDIPLEPG DVIGVAGNHW DGYSKGVNRK LGRTGLYPSY KVKEKIETVK YPTYPEADKL
LTSQKK
//
