OFT23_ARATH
ID OFT23_ARATH Reviewed; 445 AA.
AC Q9MA87; Q8H0U6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=O-fucosyltransferase 23 {ECO:0000305};
DE Short=O-FucT-23 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase 1 {ECO:0000303|PubMed:29467178};
DE Short=AtOFT1 {ECO:0000303|PubMed:29467178};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=OFUT23 {ECO:0000305};
GN Synonyms=GT65 {ECO:0000303|PubMed:23272088},
GN OFT1 {ECO:0000303|PubMed:29467178};
GN OrderedLocusNames=At3g05320 {ECO:0000312|Araport:AT3G05320};
GN ORFNames=T12H1.29 {ECO:0000312|EMBL:AAF27038.1};
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], AND WEB RESOURCE.
RC STRAIN=cv. Columbia;
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 [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] OF 72-445.
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=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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ARG-51; HIS-54; ARG-260 AND ASP-264.
RX PubMed=29467178; DOI=10.1104/pp.17.01577;
RA Smith D.K., Jones D.M., Lau J.B.R., Cruz E.R., Brown E., Harper J.F.,
RA Wallace I.S.;
RT "A putative protein O-fucosyltransferase facilitates pollen tube
RT penetration through the stigma-style interface.";
RL Plant Physiol. 176:2804-2818(2018).
CC -!- FUNCTION: Probable protein O-fucosyltransferase required for correct
CC pollen tube penetration through the stigma-style interface
CC (PubMed:29467178). May be involved in protein O-glycosylation events
CC during pollen-pistil interactions (PubMed:29467178).
CC {ECO:0000269|PubMed:29467178}.
CC -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:29467178}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in dry pollen grains and germinating
CC pollen grains. {ECO:0000269|PubMed:29467178}.
CC -!- DISRUPTION PHENOTYPE: Altered silique morphology and reduced seed set.
CC {ECO:0000269|PubMed:29467178}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN72045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; KJ138840; AHL38780.1; -; mRNA.
DR EMBL; AC009177; AAF27038.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74219.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65886.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65887.1; -; Genomic_DNA.
DR EMBL; BT002034; AAN72045.1; ALT_INIT; mRNA.
DR EMBL; BT015041; AAT70492.1; -; mRNA.
DR RefSeq; NP_001327823.1; NM_001337577.1.
DR RefSeq; NP_001327824.1; NM_001337578.1.
DR RefSeq; NP_187183.3; NM_111405.4.
DR AlphaFoldDB; Q9MA87; -.
DR STRING; 3702.AT3G05320.1; -.
DR PaxDb; Q9MA87; -.
DR PRIDE; Q9MA87; -.
DR ProteomicsDB; 239027; -.
DR EnsemblPlants; AT3G05320.1; AT3G05320.1; AT3G05320.
DR EnsemblPlants; AT3G05320.2; AT3G05320.2; AT3G05320.
DR EnsemblPlants; AT3G05320.3; AT3G05320.3; AT3G05320.
DR GeneID; 819696; -.
DR Gramene; AT3G05320.1; AT3G05320.1; AT3G05320.
DR Gramene; AT3G05320.2; AT3G05320.2; AT3G05320.
DR Gramene; AT3G05320.3; AT3G05320.3; AT3G05320.
DR KEGG; ath:AT3G05320; -.
DR Araport; AT3G05320; -.
DR TAIR; locus:2096239; AT3G05320.
DR eggNOG; ENOG502QST1; Eukaryota.
DR HOGENOM; CLU_041881_0_0_1; -.
DR InParanoid; Q9MA87; -.
DR OMA; RWMTNMS; -.
DR OrthoDB; 1127619at2759; -.
DR PhylomeDB; Q9MA87; -.
DR BRENDA; 2.4.1.221; 399.
DR PRO; PR:Q9MA87; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA87; baseline and differential.
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:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009875; P:pollen-pistil interaction; IEA:InterPro.
DR GO; GO:0009856; P:pollination; IMP:TAIR.
DR InterPro; IPR044982; AtOFT1-like.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR PANTHER; PTHR37220; PTHR37220; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..445
FT /note="O-fucosyltransferase 23"
FT /id="PRO_0000442085"
FT TRANSMEM 12..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 374..375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 51
FT /note="R->A: Unable to complement the mutant reduced seed
FT set phenotype."
FT /evidence="ECO:0000269|PubMed:29467178"
FT MUTAGEN 54
FT /note="H->A: Unable to complement the mutant reduced seed
FT set phenotype."
FT /evidence="ECO:0000269|PubMed:29467178"
FT MUTAGEN 54
FT /note="H->N: Complements the mutant reduced seed set
FT phenotype."
FT /evidence="ECO:0000269|PubMed:29467178"
FT MUTAGEN 260
FT /note="R->A,K: Unable to complement the mutant reduced seed
FT set phenotype."
FT /evidence="ECO:0000269|PubMed:29467178"
FT MUTAGEN 264
FT /note="D->A: Unable to complement the mutant reduced seed
FT set phenotype."
FT /evidence="ECO:0000269|PubMed:29467178"
SQ SEQUENCE 445 AA; 50648 MW; 05A2DEEFEBF34B3B CRC64;
MNSPLSSKNL RIFSKSVACK CLVLVGIALF YRALLLSYSP RNALSNSLLF RDRHMSDSSS
TGGIRTDKFL EVPQIVWGLN NQKIAFARAC LTARMMNRTL LMPSLSASLF YKEVDKLRPI
PFDKVFQFER FNSLCSGFVR LSRFSDVKNR AQVFDLEKGS GRRWTVERDL EHLKQSARNE
SIDEFEVIRL IGKNPFLWHD HWPVEDYAKV FECMVVVDEI SREADKVVMK IREAGEAERA
KLASKTEILG PVPFVAVHMR IEIDWMIHCK KLEQRKKISE ICSSKREILD RVGNISGLKT
PTVLYLAVAD TLLEEKEEDS SVLSGWRDGL IPFEKKKLGV KEEIYGKYSY LIQSAIDYEV
CLRADVFVGN SFSTFSSLIV LERTQKARRL GFMSSCKDGG NKWRSYAYNL AGESNGVPRR
WMTNMTHSSL QAISYGSNSV SCSSG
