OFUT2_ARATH
ID OFUT2_ARATH Reviewed; 590 AA.
AC F4IAL1; O65380; Q5BQ14;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=O-fucosyltransferase 2 {ECO:0000305};
DE Short=O-FucT-2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=OFUT2 {ECO:0000305};
GN OrderedLocusNames=At1g11990 {ECO:0000312|Araport:AT1G11990};
GN ORFNames=F12F1.14 {ECO:0000312|EMBL:AAC17628.1};
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 Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Xiao Y., Underwood B.A., Moskal W., Redman J., Wang W., Monaghan E.,
RA Wu H.C., Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND REVIEW.
RX PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL Front. Plant Sci. 3:59-59(2012).
RN [6]
RP GENE FAMILY.
RX PubMed=22916179; DOI=10.1371/journal.pone.0042914;
RA Neumetzler L., Humphrey T., Lumba S., Snyder S., Yeats T.H., Usadel B.,
RA Vasilevski A., Patel J., Rose J.K., Persson S., Bonetta D.;
RT "The FRIABLE1 gene product affects cell adhesion in Arabidopsis.";
RL PLoS ONE 7:E42914-E42914(2012).
RN [7]
RP GENE FAMILY.
RX PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA Voxeur A., Andre A., Breton C., Lerouge P.;
RT "Identification of putative rhamnogalacturonan-II specific
RT glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT approaches.";
RL PLoS ONE 7:E51129-E51129(2012).
RN [8]
RP GENE FAMILY.
RX PubMed=22966747; DOI=10.1111/tpj.12019;
RA Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT "Identification of an additional protein involved in mannan biosynthesis.";
RL Plant J. 73:105-117(2013).
RN [9]
RP WEB RESOURCE.
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
CC -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4IAL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IAL1-2; Sequence=VSP_059166;
CC Name=3;
CC IsoId=F4IAL1-3; Sequence=VSP_059165, VSP_059166;
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002131; AAC17628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28824.1; -; Genomic_DNA.
DR EMBL; AY924664; AAX23739.1; -; mRNA.
DR EMBL; DQ132647; AAZ52677.1; -; mRNA.
DR EMBL; DQ132648; AAZ52678.1; -; mRNA.
DR PIR; H86254; H86254.
DR RefSeq; NP_172663.2; NM_101071.3. [F4IAL1-1]
DR AlphaFoldDB; F4IAL1; -.
DR PaxDb; F4IAL1; -.
DR PRIDE; F4IAL1; -.
DR ProteomicsDB; 250896; -. [F4IAL1-1]
DR EnsemblPlants; AT1G11990.1; AT1G11990.1; AT1G11990. [F4IAL1-1]
DR GeneID; 837751; -.
DR Gramene; AT1G11990.1; AT1G11990.1; AT1G11990. [F4IAL1-1]
DR KEGG; ath:AT1G11990; -.
DR Araport; AT1G11990; -.
DR TAIR; locus:2008935; AT1G11990.
DR eggNOG; ENOG502QU78; Eukaryota.
DR HOGENOM; CLU_018420_8_0_1; -.
DR InParanoid; F4IAL1; -.
DR PRO; PR:F4IAL1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAL1; baseline and differential.
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: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 Alternative splicing; Carbohydrate metabolism; Fucose metabolism;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..590
FT /note="O-fucosyltransferase 2"
FT /id="PRO_0000442065"
FT TRANSMEM 67..87
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365..367
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform 3)"
FT /id="VSP_059165"
FT VAR_SEQ 360
FT /note="Y -> YVAPLDLHLLGPKYASLILDNKSDSPVQEEAASSSSSK (in
FT isoform 2 and isoform 3)"
FT /id="VSP_059166"
SQ SEQUENCE 590 AA; 67314 MW; E0E8C68C70135951 CRC64;
MGQERPNDEE RPESRDLGVY GCSPPHSPRL GPTRFYVFAG DPNPKQTIKR CKRKRIQACN
DQRTAKTAIG VMAILGFFCL VNWFMLSRLH EGRVWLRRGL SENPKHVSAQ NEERKKFEKQ
KMKYNGTYGR MLSLATDALA EGMRDNRYCN GFDFEQNKLE TKDLWQEPKE QASAWKPCAD
QRSLTPDDGK NGYIMVTANG GINQQRVAVC NIVVVARLLN AALVIPKFML SDVWTDASQF
GDIYQEEHFM EYLSPDIRIV KELPKELQSL NLEEIGSVVT DIEVMKEAKP DFYMTHILPI
LLKNRVIHFV GFGNRLAFDP LPFELQRLRC RCNFHALNFV PRIQETAALL VKRLRGSGSY
YLALHLRFEI DMVAHSLCYF GGGETEQKEL DSYRQKHFPS LSTLTRKKKF RSADVLRTEG
LCPLTPEEAV LMLAALGFNR ETRVFVAGAN IYGGSKRLAV LTSLYPNLVT KEKLLTESEL
QPFKNFSSQL AALDFIACAA ADAFAMTDSG SQLSSLVSGY RIYYGGGKLP TIRPNKRRLS
DILLKNSTIE WNVFEKRVRK AIRQTKHVFA RPNGRSVYRY PRCKECMCHA
