OFT11_ARATH
ID OFT11_ARATH Reviewed; 589 AA.
AC Q8GUM0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=O-fucosyltransferase 11 {ECO:0000305};
DE Short=O-FucT-11 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31411.1};
GN Name=OFUT11 {ECO:0000305};
GN OrderedLocusNames=At1g38131 {ECO:0000312|Araport:AT1G38131};
GN ORFNames=T18N24 {ECO:0000312|EMBL:AC074111};
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].
RC STRAIN=cv. Columbia;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransferases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 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 -!- 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";
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DR EMBL; KY906047; ARJ31411.1; -; mRNA.
DR EMBL; AC074111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31900.1; -; Genomic_DNA.
DR EMBL; BT002394; AAO00754.1; -; mRNA.
DR RefSeq; NP_683362.1; NM_148521.3.
DR AlphaFoldDB; Q8GUM0; -.
DR PaxDb; Q8GUM0; -.
DR PRIDE; Q8GUM0; -.
DR ProteomicsDB; 250891; -.
DR EnsemblPlants; AT1G38131.1; AT1G38131.1; AT1G38131.
DR GeneID; 840652; -.
DR Gramene; AT1G38131.1; AT1G38131.1; AT1G38131.
DR KEGG; ath:AT1G38131; -.
DR Araport; AT1G38131; -.
DR TAIR; locus:504956200; AT1G38131.
DR eggNOG; ENOG502QS83; Eukaryota.
DR HOGENOM; CLU_018420_8_1_1; -.
DR InParanoid; Q8GUM0; -.
DR OMA; ANRLSMH; -.
DR OrthoDB; 427717at2759; -.
DR PhylomeDB; Q8GUM0; -.
DR PRO; PR:Q8GUM0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GUM0; 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 PANTHER; PTHR31288; PTHR31288; 1.
DR Pfam; PF10250; O-FucT; 1.
DR PIRSF; PIRSF009360; UCP009360; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="O-fucosyltransferase 11"
FT /id="PRO_0000442074"
FT TRANSMEM 68..88
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332..334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 589 AA; 66493 MW; 71EF1DC1C5020871 CRC64;
MKSKIHHQPN GSNNGVVSSN DNGCRSESPS PPLSPNRRVL RRQRRQTLLR ASSFSLRRNL
RYLLLLPMIY ASGLLMCVGP FSGLVGWVYV PGSVYRSPEI YRKLKDDIFS DNSTALELSS
VWKFKRRPKM PKPCPNSTVS SHFGLNRESS ALAPSSGYLI VEANGGLNQQ RSAICNAVAV
AGLLNAVLVI PRFEFHAIWK DSSNFGDIYD EDHFISSLEG YVKIVRDVPD EIMTRFSYNV
SSIPTIRVQA WATVNYYNGE VYPVLKEHGV IRITPFANRL AMSVPPYIQL LRCIANYKAL
KFSSPISTLA EKLVDRMVEK SSATGGKYVS VHLRFEEDMV AFSCCLYEGG RAEKSEMDVI
RQKSWKGKFK RRDRVIRPDL NRVNGKCPLT PLEVGMMLRG MGFDNNTSIY LASGRIYQPE
KHLAPLQEMF PRLYTKESLA TPEELAPFQG YSSRMAALDY TVSLLSEVFV TTQGGNFPHF
LMGHRRFLFG GHAKTVIPDK PKLVLLLQDM EMRWEVFKKE MKLMLGESDR KGVMVPRVRK
INRKTSIYTY PLPECECIFH LSSNFSNTGN ILSLGALHPS SNLISSARL
