OFT20_ARATH
ID OFT20_ARATH Reviewed; 573 AA.
AC O64884; F4IU48;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=O-fucosyltransferase 20 {ECO:0000305};
DE Short=O-FucT-20 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=OFUT20 {ECO:0000305};
GN OrderedLocusNames=At2g44500 {ECO:0000312|Araport:AT2G44500};
GN ORFNames=F4I1.31 {ECO:0000312|EMBL:AAC16096.1};
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=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 [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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 INTERACTION WITH RACK1A.
RX PubMed=23435172; DOI=10.4161/psb.24012;
RA Kundu N., Dozier U., Deslandes L., Somssich I.E., Ullah H.;
RT "Arabidopsis scaffold protein RACK1A interacts with diverse environmental
RT stress and photosynthesis related proteins.";
RL Plant Signal. Behav. 8:E24012-E24012(2013).
RN [10]
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).
RN [11]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RA Halliday J.;
RT "Molecular analysis and functional elucidation of a novel plant O-
RT fucosyltransferase in Arabidopsis thaliana and Brassica napus.";
RL Thesis (2016), University of Guelph, Canada.
CC -!- FUNCTION: May play a role in the biosynthesis of matrix polysaccharides
CC and contribute to the biomechanics and development of the plant cell
CC wall. {ECO:0000269|Ref.11}.
CC -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with RACK1A. {ECO:0000269|PubMed:23435172}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|Ref.11};
CC Single-pass type II membrane protein {ECO:0000305|Ref.11}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64884-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64884-2; Sequence=VSP_059171, VSP_059172;
CC -!- TISSUE SPECIFICITY: Highly expressed in shoot apical meristem (SAM) and
CC in young vegetative tissues. {ECO:0000269|Ref.11}.
CC -!- DISRUPTION PHENOTYPE: Increased number of lateral roots and wider stem
CC diameter. Altered cell wall composition with an increased level of de-
CC esterified pectins. {ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX819345; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; AC004521; AAC16096.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10430.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10429.1; -; Genomic_DNA.
DR EMBL; AF370605; AAK43924.1; -; mRNA.
DR EMBL; BX819345; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T02405; T02405.
DR RefSeq; NP_181978.1; NM_130013.4. [O64884-1]
DR RefSeq; NP_973688.1; NM_201959.1. [O64884-2]
DR AlphaFoldDB; O64884; -.
DR STRING; 3702.AT2G44500.1; -.
DR iPTMnet; O64884; -.
DR PaxDb; O64884; -.
DR PRIDE; O64884; -.
DR ProteomicsDB; 250794; -. [O64884-1]
DR EnsemblPlants; AT2G44500.1; AT2G44500.1; AT2G44500. [O64884-1]
DR EnsemblPlants; AT2G44500.2; AT2G44500.2; AT2G44500. [O64884-2]
DR GeneID; 819057; -.
DR Gramene; AT2G44500.1; AT2G44500.1; AT2G44500. [O64884-1]
DR Gramene; AT2G44500.2; AT2G44500.2; AT2G44500. [O64884-2]
DR KEGG; ath:AT2G44500; -.
DR Araport; AT2G44500; -.
DR TAIR; locus:2050564; AT2G44500.
DR eggNOG; ENOG502QTBC; Eukaryota.
DR HOGENOM; CLU_018420_7_3_1; -.
DR InParanoid; O64884; -.
DR OMA; PECMCSD; -.
DR PhylomeDB; O64884; -.
DR PRO; PR:O64884; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64884; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; 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 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism;
KW Cell wall biogenesis/degradation; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..573
FT /note="O-fucosyltransferase 20"
FT /id="PRO_0000442082"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|Ref.11"
FT TRANSMEM 61..81
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305|Ref.11"
FT TOPO_DOM 82..573
FT /note="Lumenal"
FT /evidence="ECO:0000305|Ref.11"
FT REGION 547..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 407..422
FT /note="LLKALEAPKDARIYWA -> YYTNSMNKSFCLCFFK (in isoform 2)"
FT /id="VSP_059171"
FT VAR_SEQ 423..573
FT /note="Missing (in isoform 2)"
FT /id="VSP_059172"
SQ SEQUENCE 573 AA; 64585 MW; 146E632E25EBC8EF CRC64;
MALSKNSNSN SFNKKKVSYI SVPSQIINSL SSSSLQSLLV SPKKSSRSTN RFSFSYRNPR
IWFFTLFLVS LFGMLKLGFN VDPISLPFSR YPCSTTQQPL SFDGEQNAAS HLGLAQEPIL
STGSSNSNAI IQLNGGKNET LLTEGDFWKQ PDGLGFKPCL GFTSQYRKDS NSILKNRWKY
LLVVVSGGMN QQRNQIVDAV VIARILGASL VVPVLQVNVI WGDESEFADI FDLEHFKDVL
ADDVHIVSSL PSTHVMTRPV EEKRTPLHAS PQWIRAHYLK RINRERVLLL RGLDSRLSKD
LPSDLQKLRC KVAFQALRFS PRILELGNKL ASRMRNQGQY LSLHLRMEKD VWVRTGCLPG
LTPEYDEIVN SERERHPELL TGRSNMTYHE RKLAGLCPLT ALEVTRLLKA LEAPKDARIY
WAGGEPLGGK EVLEPLTKEF PQFYNKHDLA LPGELEPFAN KASVMAAIDY IVCEKSDVFI
PSHGGNMGHA LQGQRAYAGH KKYITPNKRQ MLPYFMNSSL PESDFNRIVK DLHRESLGQP
ELRMSKAGKD VTKHPVPECM CSDRQQQEQQ SDA
