ID   OFT20_BRANA             Reviewed;         555 AA.
AC   A0A0B5GR44;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 2.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=O-fucosyltransferase 20 {ECO:0000305};
DE            Short=O-FucT-20 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=BnAt2G(1) {ECO:0000303|Ref.1};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:AJF23778.1};
GN   Name=OFUT20 {ECO:0000305};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-555, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=cv. Topas;
RA   Halliday J.;
RT   "Molecular analysis and functional elucidation of a novel plant O-
RT   fucosyltransferase in Arabidopsis thaliana and Brassica napus.";
RL   Thesis (2016), University of Guelph, Canada.
CC   -!- FUNCTION: May play a role in the biosynthesis of matrix polysaccharides
CC       and contribute to the biomechanics and development of the plant cell
CC       wall. {ECO:0000269|Ref.1}.
CC   -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|Ref.1};
CC       Single-pass type II membrane protein {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in embryogenic microspore and in
CC       vegetative tissues. {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: Increased number of lateral roots and wider stem
CC       diameter. Altered cell wall composition with an increased level of de-
CC       esterified pectins. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AJF23778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; KM875557; AJF23778.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5GR44; -.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11299; O-FucT_plant; 1.
DR   InterPro; IPR024709; FucosylTrfase_pln.
DR   InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR   Pfam; PF10250; O-FucT; 1.
DR   PIRSF; PIRSF009360; UCP009360; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..555
FT                   /note="O-fucosyltransferase 20"
FT                   /id="PRO_0000442101"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        59..79
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305|Ref.1"
FT   TOPO_DOM        80..555
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          110..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         330..332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H488"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        89
FT                   /note="Y -> H (in Ref. 1; AJF23778)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   555 AA;  62553 MW;  9D7CE255BE7177FD CRC64;
     MALPKNGGNS SSTKKKVSYI SVPSQIINSL SSSSLQSLLV SPKKSSRCTN RFSYRNPRIW
     FLTLFLVSLF GMLKLGLNVD PISLPFSRYP CSTGSFDEHH AVSHLAFASK NDTQSSSSSE
     HRKNETLPTE GDFWKQPDGL GFKPCLGFSR QYRKDSNSIL KNRWKYLLVV VAGGMNQQRN
     QIVDAVIMAR ILGASLVVPV LQVNVIWGDE SEFADIFDLE HFKNVLADDV HIVSSLPSTH
     VMTRPAEEKR TPLHASPQWI RAHYLKRINR ERVLLLRGLD SRLSNDLPSD LQKLRCKVAS
     QALRFSPRIL ELGNKLASRM LSEGQYLSLH LRMEKDVWVR TGSLPGLTPE YDEIVNSERQ
     RHPELLTGRS NMTYNERKLA GLCPLTALEV TRLLKALEAP KDARIYWAGG EPLGGKEALE
     PLTKEFPHLY NKHDLALPGE LEPFAKKASV MAAIDYIVCE KSDVFIPSHG GNMGHALQGQ
     RAYAGHKKYI TPNKRHMLPY FMNASLPESE FNRIVKDFHR ESLGQPELRT GRGGKDVTKH
     PVSECMCSDR RQQQQ