FUT3_ARATH
ID FUT3_ARATH Reviewed; 521 AA.
AC Q9CA71; Q67XV8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fucosyltransferase 3;
DE Short=AtFUT3;
DE EC=2.4.1.-;
GN Name=FUT3; OrderedLocusNames=At1g74420; ORFNames=F1M20.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-521.
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).
CC -!- FUNCTION: May be involved in cell wall biosynthesis. May act as a
CC fucosyltransferase.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CA71-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC siliques and seedlings.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 37 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL50622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC011765; AAG52352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35589.1; -; Genomic_DNA.
DR EMBL; AK175419; BAD43182.1; -; mRNA.
DR EMBL; AK176710; BAD44473.1; -; mRNA.
DR EMBL; AF417473; AAL50622.1; ALT_INIT; mRNA.
DR RefSeq; NP_177582.3; NM_106102.4. [Q9CA71-1]
DR AlphaFoldDB; Q9CA71; -.
DR SMR; Q9CA71; -.
DR STRING; 3702.AT1G74420.2; -.
DR CAZy; GT37; Glycosyltransferase Family 37.
DR PaxDb; Q9CA71; -.
DR PRIDE; Q9CA71; -.
DR ProteomicsDB; 230564; -. [Q9CA71-1]
DR EnsemblPlants; AT1G74420.1; AT1G74420.1; AT1G74420. [Q9CA71-1]
DR GeneID; 843783; -.
DR Gramene; AT1G74420.1; AT1G74420.1; AT1G74420. [Q9CA71-1]
DR KEGG; ath:AT1G74420; -.
DR Araport; AT1G74420; -.
DR eggNOG; ENOG502QTTA; Eukaryota.
DR HOGENOM; CLU_001992_2_1_1; -.
DR InParanoid; Q9CA71; -.
DR OMA; LYRKEST; -.
DR PhylomeDB; Q9CA71; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9CA71; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA71; baseline and differential.
DR Genevisible; Q9CA71; AT.
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:0008417; F:fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004938; XG_FTase.
DR PANTHER; PTHR31889; PTHR31889; 1.
DR Pfam; PF03254; XG_FTase; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..521
FT /note="Fucosyltransferase 3"
FT /id="PRO_0000193912"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..521
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 58989 MW; D2AB9A0FD84CAFFC CRC64;
MKRGKKNSDA GDRLTNSDTR TGSSELNAMM KPSLSSMKTM GLLLAVLMVA SVMFSLSVVL
RDPPSDDVIE TEAASRVLQS RLHQDGGLSE KKAQLGNINL VPSFDKESCL SRYEASLYRK
ESPFKQSSYL DYRLQRYEDL HRRCGPFTRS YNLTLDKLKS GDRSDGEVSG CRYVIWLNSN
GDLGNRMLSL ASAFLYALLT NRFLLVELGV DMADLFCEPF PNTTWFLPPE FPLNSHFNEQ
SLLRNSGNPM VAYRHVVRDS SDQQKLFFCE DSQVLLEETP WLILKADSFF LPSLFSVSSF
KQELQMLFPE KDTAFHFLSQ YLFHPTNVVW GLITRYYNAY LAKADQRIGI YIGVSESGNE
QFQHLIDQIL ACGTRHKLLP EVDKQRNLPS SQVLNRKSKA VFISSSSPGY FKSIRDVYWE
NPTVMGEIIS VHKPSYKDYQ KTPRNMESKR AWAEIYLLSC SDALVVTGLW SSLVEVAHGL
GGLKPWVLNK AENGTAHEPY CVKARSIEPC SQATLFHGCK D
