OFT28_ARATH
ID OFT28_ARATH Reviewed; 638 AA.
AC Q9M393;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=O-fucosyltransferase 28 {ECO:0000305};
DE Short=O-FucT-28 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31434.1};
GN Name=OFUT28 {ECO:0000305};
GN OrderedLocusNames=At3g54100 {ECO:0000312|Araport:AT3G54100};
GN ORFNames=F24B22.60 {ECO:0000312|EMBL:CAB70984.1};
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 [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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 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 -!- SEQUENCE CAUTION:
CC Sequence=BX823589; 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; KY906070; ARJ31434.1; -; mRNA.
DR EMBL; AL132957; CAB70984.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79188.1; -; Genomic_DNA.
DR EMBL; BX823589; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T47569; T47569.
DR RefSeq; NP_190978.1; NM_115270.5.
DR AlphaFoldDB; Q9M393; -.
DR PaxDb; Q9M393; -.
DR PRIDE; Q9M393; -.
DR ProteomicsDB; 238931; -.
DR EnsemblPlants; AT3G54100.1; AT3G54100.1; AT3G54100.
DR GeneID; 824577; -.
DR Gramene; AT3G54100.1; AT3G54100.1; AT3G54100.
DR KEGG; ath:AT3G54100; -.
DR Araport; AT3G54100; -.
DR TAIR; locus:2080285; AT3G54100.
DR eggNOG; ENOG502QQ4D; Eukaryota.
DR HOGENOM; CLU_018420_7_0_1; -.
DR InParanoid; Q9M393; -.
DR OMA; CLCRKVQ; -.
DR OrthoDB; 476565at2759; -.
DR PhylomeDB; Q9M393; -.
DR PRO; PR:Q9M393; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M393; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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.
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..638
FT /note="O-fucosyltransferase 28"
FT /id="PRO_0000442090"
FT TRANSMEM 125..145
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT REGION 49..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
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 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 97
FT /note="K -> E (in Ref. 4; BX823589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 72907 MW; 01599F1FE623ADBB CRC64;
MSVVGAINPV PIAPTTRRRV GDSLDVISER PSNSSDYCNT INQPIVGSTD LDGGDATGQD
SSPSSESSAS STGSHYHHDH YHRFYSHPVI RYLLLRKFWI PFYGGASTVV IGQGFRSGRN
VGRRILGLLM LLVVASVFLR VYLMGGVRVV DHARLKEFVV VRTLRDDWSM AQREVAENQA
SSQPMRVLEK LPIPEIWQKP ESGNYRQCVT RPKNYTRLQR QTNGYLVVHA NGGLNQMRTG
ICDMVAVAKI MNATLVLPLL DHESFWTDPS TFKDIFDWRN FMNVLKHDVD IVEYLPPQYA
AMKPLLKAPV SWSKASYYRS EMLPLLKRHK VLKFTLTDSR LANNGLPPSI QRLRCRANYQ
ALLYTKEIED LGKILVNRLR NNTEPYIALH LRYEKDMLAF TGCNHNLTTE EAEELRIMRY
SVKHWKEKEI DSRERRIQGG CPMSPREAAI FLKAMGYPSS TTVYIVAGEI YGSESMDAFR
AEYPNVFSHS TLATEEELEP FSQYQNRLAA LDYIVALESD VFVYTYDGNM AKAVQGHRKF
EGFRKSINPD RLNFVRLIDH FDEGIISWEE FSSEVKRLNR DRIGAAYGRL PAALPRLEEN
FYANPQPDCI CNKSHPEQLR KQSSLRTDSK SWKKSALR
