ID   FUT1_PEA                Reviewed;         565 AA.
AC   Q9M5Q1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Galactoside 2-alpha-L-fucosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=PsFT1;
DE   AltName: Full=Xyloglucan alpha-(1,2)-fucosyltransferase;
GN   Name=FT1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Alaska;
RX   PubMed=10747946; DOI=10.1074/jbc.m000677200;
RA   Faik A., Bar-Peled M., DeRocher A.E., Zeng W., Perrin R.M., Wilkerson C.,
RA   Raikhel N.V., Keegstra K.;
RT   "Biochemical characterization and molecular cloning of an alpha-1,2-
RT   fucosyltransferase that catalyzes the last step of cell wall xyloglucan
RT   biosynthesis in Pea.";
RL   J. Biol. Chem. 275:15082-15089(2000).
CC   -!- FUNCTION: Involved in cell wall biosynthesis. Adds the terminal fucosyl
CC       residue on xyloglucan side chains. {ECO:0000269|PubMed:10747946}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
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 37 family.
CC       {ECO:0000305}.
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DR   EMBL; AF223643; AAF62896.1; -; mRNA.
DR   AlphaFoldDB; Q9M5Q1; -.
DR   SMR; Q9M5Q1; -.
DR   CAZy; GT37; Glycosyltransferase Family 37.
DR   PRIDE; Q9M5Q1; -.
DR   UniPathway; UPA00378; -.
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:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004938; XG_FTase.
DR   PANTHER; PTHR31889; PTHR31889; 1.
DR   Pfam; PF03254; XG_FTase; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..565
FT                   /note="Galactoside 2-alpha-L-fucosyltransferase"
FT                   /id="PRO_0000193910"
FT   TOPO_DOM        1..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..565
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   565 AA;  64029 MW;  5E6AAA2BED20594B CRC64;
     MNMLIKRVIA IKNPRGDDNN NNKLSDLETL TDKCTTCPLT LMRVMAFFVV SFMLFSVLFS
     LSVVLRDPPS DAAISSTTTL FQLNQGLGSD DFDSVELLND KLLGGLLADG FDEKSCLSRY
     QSAIFGKGLS GKPSSYLISR LRKYEARHKQ CGPYTESYNK TVKELGSGQF SESVDCKYVV
     WISFSGLGNR ILTLVSAFLY ALLTDRVLLV DPGVDMTDLF CEPFPDASWF VPPDFPLNSH
     LNNFNQESNQ CHGKILKTKS ITNSTVPSFV YLHLAHDYDD HDKLFFCDEE QLFLQNVPLL
     IMKTDNYFIP SLFLMPSFEQ ELNDLFPKKE KVFHFLGRYL LHPTNNVWGL VVRYYDAYLA
     KVDERIGIQI RVFDTDPGPF QHVLDQVLAC TLKESILPDV NREQNINSSS GTPKSKAVLI
     TSLSSGYFEK VRDMYWEFPT ETGEVVGIYQ PSHEGYQQTQ KQFHNQKAWA EMYLLSLTDV
     LVTSSWSTFG YVAQGLGGLK PWILYKPENR TAPNPPCQRA MSMEPCFHAP PFYDCKAKRG
     TDTGALVPHV RHCEDMSWGL KLVDN