FUT1_ARATH
ID FUT1_ARATH Reviewed; 558 AA.
AC Q9SWH5; O81052;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Galactoside 2-alpha-L-fucosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Xyloglucan alpha-(1,2)-fucosyltransferase;
DE Short=AtFUT1;
GN Name=FUT1; Synonyms=FT1, MUR2; OrderedLocusNames=At2g03220;
GN ORFNames=T18E12.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10373113; DOI=10.1126/science.284.5422.1976;
RA Perrin R.M., DeRocher A.E., Bar-Peled M., Zeng W., Norambuena L.,
RA Orellana A., Raikhel N.V., Keegstra K.;
RT "Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall
RT biosynthesis.";
RL Science 284:1976-1979(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11743104; DOI=10.1104/pp.010596;
RA Sarria R., Wagner T.A., O'Neill M.A., Faik A., Wilkerson C.G., Keegstra K.,
RA Raikhel N.V.;
RT "Characterization of a family of Arabidopsis genes related to xyloglucan
RT fucosyltransferase1.";
RL Plant Physiol. 127:1595-1606(2001).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-550.
RX PubMed=11854459; DOI=10.1073/pnas.052450699;
RA Vanzin G.F., Madson M., Carpita N.C., Raikhel N.V., Keegstra K.,
RA Reiter W.D.;
RT "The mur2 mutant of Arabidopsis thaliana lacks fucosylated xyloglucan
RT because of a lesion in fucosyltransferase AtFUT1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3340-3345(2002).
RN [7]
RP FUNCTION.
RX PubMed=14730072; DOI=10.1104/pp.103.027508;
RA Pena M.J., Ryden P., Madson M., Smith A.C., Carpita N.C.;
RT "The galactose residues of xyloglucan are essential to maintain mechanical
RT strength of the primary cell walls in Arabidopsis during growth.";
RL Plant Physiol. 134:443-451(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21143678; DOI=10.1111/j.1365-313x.2010.04388.x;
RA Chevalier L., Bernard S., Ramdani Y., Lamour R., Bardor M., Lerouge P.,
RA Follet-Gueye M.L., Driouich A.;
RT "Subcompartment localization of the side chain xyloglucan-synthesizing
RT enzymes within Golgi stacks of tobacco suspension-cultured cells.";
RL Plant J. 64:977-989(2010).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH MUR3; XLT2; XXT2 AND XXT5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25392066; DOI=10.1093/pcp/pcu161;
RA Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
RT "Protein-protein interactions among xyloglucan-synthesizing enzymes and
RT formation of Golgi-localized multiprotein complexes.";
RL Plant Cell Physiol. 56:255-267(2015).
CC -!- FUNCTION: Involved in cell wall biosynthesis. Is both necessary and
CC sufficient for the addition of the terminal fucosyl residue on
CC xyloglucan side chains, but is not involved in the fucosylation of
CC other cell wall components (PubMed:10373113, PubMed:11743104,
CC PubMed:11854459, PubMed:14730072). Associates with other xyloglucan-
CC synthesizing enzymes to form multiprotein complexes for xyloglucan
CC synthesis in the Golgi (PubMed:25392066). {ECO:0000269|PubMed:10373113,
CC ECO:0000269|PubMed:11743104, ECO:0000269|PubMed:11854459,
CC ECO:0000269|PubMed:14730072, ECO:0000269|PubMed:25392066}.
CC -!- SUBUNIT: Homodimer (PubMed:25392066). Interacts with MUR3, XLT2, XXT2
CC and XXT5 (PubMed:25392066). {ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:21143678}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21143678}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:25392066}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:25392066}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000269|PubMed:21143678}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC siliques and seedlings. {ECO:0000269|PubMed:11743104}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 37 family.
CC {ECO:0000305}.
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DR EMBL; AF154111; AAD41092.1; -; mRNA.
DR EMBL; AC005313; AAC34480.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05676.1; -; Genomic_DNA.
DR EMBL; AY139993; AAM98135.1; -; mRNA.
DR EMBL; BT002477; AAO00837.1; -; mRNA.
DR EMBL; BT003401; AAO30064.1; -; mRNA.
DR PIR; T02704; T02704.
DR RefSeq; NP_178421.1; NM_126373.3.
DR PDB; 5KOE; X-ray; 1.79 A; A/B/C/D=84-558.
DR PDB; 5KOP; X-ray; 2.10 A; A/B/C/D=69-558.
DR PDB; 5KOR; X-ray; 2.20 A; A/B/C/D=69-558.
DR PDB; 5KWK; X-ray; 1.90 A; A/B=84-558.
DR PDB; 5KX6; X-ray; 2.20 A; A/B=84-558.
DR PDBsum; 5KOE; -.
DR PDBsum; 5KOP; -.
DR PDBsum; 5KOR; -.
DR PDBsum; 5KWK; -.
DR PDBsum; 5KX6; -.
DR AlphaFoldDB; Q9SWH5; -.
DR SMR; Q9SWH5; -.
DR BioGRID; 253; 7.
DR IntAct; Q9SWH5; 1.
DR STRING; 3702.AT2G03220.1; -.
DR CAZy; GT37; Glycosyltransferase Family 37.
DR PaxDb; Q9SWH5; -.
DR PRIDE; Q9SWH5; -.
DR ProteomicsDB; 247381; -.
DR EnsemblPlants; AT2G03220.1; AT2G03220.1; AT2G03220.
DR GeneID; 814851; -.
DR Gramene; AT2G03220.1; AT2G03220.1; AT2G03220.
DR KEGG; ath:AT2G03220; -.
DR Araport; AT2G03220; -.
DR TAIR; locus:2056886; AT2G03220.
DR eggNOG; ENOG502QTTA; Eukaryota.
DR HOGENOM; CLU_001992_2_1_1; -.
DR InParanoid; Q9SWH5; -.
DR OMA; NKAIHSN; -.
DR OrthoDB; 364119at2759; -.
DR PhylomeDB; Q9SWH5; -.
DR BioCyc; ARA:AT2G03220-MON; -.
DR BioCyc; MetaCyc:AT2G03220-MON; -.
DR BRENDA; 2.4.1.344; 399.
DR BRENDA; 2.4.1.69; 399.
DR PRO; PR:Q9SWH5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SWH5; baseline and differential.
DR Genevisible; Q9SWH5; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
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:0008417; F:fucosyltransferase activity; ISS:TAIR.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IDA:TAIR.
DR InterPro; IPR004938; XG_FTase.
DR PANTHER; PTHR31889; PTHR31889; 1.
DR Pfam; PF03254; XG_FTase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..558
FT /note="Galactoside 2-alpha-L-fucosyltransferase"
FT /id="PRO_0000193909"
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..558
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 550
FT /note="D->N: In mur2; loss of activity and lack of
FT fucosylated xylogulcan."
FT /evidence="ECO:0000269|PubMed:11854459"
FT CONFLICT 270
FT /note="V -> F (in Ref. 1; AAD41092)"
FT /evidence="ECO:0000305"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5KOP"
FT TURN 96..101
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5KOP"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:5KOE"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:5KOE"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5KWK"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:5KOE"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5KWK"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:5KX6"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5KWK"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:5KOE"
FT HELIX 483..492
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5KWK"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:5KOE"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:5KOE"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:5KOE"
SQ SEQUENCE 558 AA; 63452 MW; 1BF0E372231A8ADF CRC64;
MDQNSYRRRS SPIRTTTGGS KSVNFSELLQ MKYLSSGTMK LTRTFTTCLI VFSVLVAFSM
IFHQHPSDSN RIMGFAEARV LDAGVFPNVT NINSDKLLGG LLASGFDEDS CLSRYQSVHY
RKPSPYKPSS YLISKLRNYE KLHKRCGPGT ESYKKALKQL DQEHIDGDGE CKYVVWISFS
GLGNRILSLA SVFLYALLTD RVLLVDRGKD MDDLFCEPFL GMSWLLPLDF PMTDQFDGLN
QESSRCYGYM VKNQVIDTEG TLSHLYLHLV HDYGDHDKMF FCEGDQTFIG KVPWLIVKTD
NYFVPSLWLI PGFDDELNKL FPQKATVFHH LGRYLFHPTN QVWGLVTRYY EAYLSHADEK
IGIQVRVFDE DPGPFQHVMD QISSCTQKEK LLPEVDTLVE RSRHVNTPKH KAVLVTSLNA
GYAENLKSMY WEYPTSTGEI IGVHQPSQEG YQQTEKKMHN GKALAEMYLL SLTDNLVTSA
WSTFGYVAQG LGGLKPWILY RPENRTTPDP SCGRAMSMEP CFHSPPFYDC KAKTGIDTGT
LVPHVRHCED ISWGLKLV
