FRB1_ARATH
ID FRB1_ARATH Reviewed; 631 AA.
AC Q9LFC6; A0A1W6AK54; Q0WRS2;
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=Protein FRIABLE 1 {ECO:0000303|PubMed:22916179, ECO:0000312|EMBL:ARJ31446.1};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase 33 {ECO:0000305};
DE Short=O-FucT-33 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=FRB1 {ECO:0000303|PubMed:22916179, ECO:0000312|EMBL:ARJ31446.1};
GN Synonyms=OFUT33 {ECO:0000305};
GN OrderedLocusNames=At5g01100 {ECO:0000312|Araport:AT5G01100};
GN ORFNames=F7J8.80 {ECO:0000312|EMBL:CAB69838.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP GENE FAMILY, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
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 [8]
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 [9]
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 [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).
CC -!- FUNCTION: Glycosyltransferase required for normal cell adhesion and
CC cell wall integrity. {ECO:0000269|PubMed:22916179}.
CC -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22916179}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strong expression in young seedlings,
CC particularly at the junction between hypocotyl and root, in emerging
CC cotyledons, and in parts of the roots. Also detected in the
CC inflorescence (sepals, petals, mature pollen and siliques) and rosette
CC leaves. {ECO:0000269|PubMed:22916179}.
CC -!- DISRUPTION PHENOTYPE: Cell dissociation, spontaneous breakage and
CC ectopic organ fusion. Affected embryo development. Increased arabinosyl
CC and decreased galactosyl residues content in the cell wall.
CC {ECO:0000269|PubMed:22916179}.
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; KY906082; ARJ31446.1; -; mRNA.
DR EMBL; AL137189; CAB69838.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90299.1; -; Genomic_DNA.
DR EMBL; AK228227; BAF00177.1; -; mRNA.
DR EMBL; BT046173; ACI49772.1; -; mRNA.
DR PIR; T45950; T45950.
DR RefSeq; NP_195730.1; NM_120188.4.
DR AlphaFoldDB; Q9LFC6; -.
DR STRING; 3702.AT5G01100.1; -.
DR PaxDb; Q9LFC6; -.
DR PRIDE; Q9LFC6; -.
DR ProteomicsDB; 228916; -.
DR EnsemblPlants; AT5G01100.1; AT5G01100.1; AT5G01100.
DR GeneID; 831831; -.
DR Gramene; AT5G01100.1; AT5G01100.1; AT5G01100.
DR KEGG; ath:AT5G01100; -.
DR Araport; AT5G01100; -.
DR TAIR; locus:2150129; AT5G01100.
DR eggNOG; ENOG502QQ4D; Eukaryota.
DR HOGENOM; CLU_018420_7_0_1; -.
DR InParanoid; Q9LFC6; -.
DR OMA; PRNNIEK; -.
DR OrthoDB; 476565at2759; -.
DR PhylomeDB; Q9LFC6; -.
DR PRO; PR:Q9LFC6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFC6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
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:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0080157; P:regulation of plant-type cell wall organization or biogenesis; IMP:CACAO.
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; Cell adhesion; Cell wall biogenesis/degradation;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..631
FT /note="Protein FRIABLE 1"
FT /id="PRO_0000442095"
FT TOPO_DOM 1..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 142..631
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 356
FT /note="L -> P (in Ref. 4; BAF00177)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="R -> K (in Ref. 1; ARJ31446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 71307 MW; 0F49628454AD8371 CRC64;
MSVGVPVNPS SSSQLPAAPT TTTRRRVADS QEDHSHVNTV GGGNAVVYVP DEEETATSCC
GGGGGGGSLS CCPSGSHHNY LVGFLSLRKF RLVWMLMVEN KSKWTAGIAR NMRSTTNLGR
FILTLLSILV VTFFLIVALS GGVGRRRKHV EKHEFVVSIH PRPTIEKIIR EDESSNSFQV
LVPKTTSIPE IWNQPEVGNY QKCVARPKNQ RPIKQTNGYL LVHANGGLNQ MRTGICDMVA
IAKIMNATLV LPFLDHSSFW SDPSSFKDIF DWKHFIKVLA EDVNIVEYLP QEFASIKPLE
KNPVSWSKSS YYRNSISKLL KKHKVIVFNH TDSRLANNSP PPSIQRLRCR ANYEALRYSE
DIENLSNVLS SRLRENNEPY LALHLRYEKD MLAFTGCNHS LSNEESIDLE KMRFSIPHWK
EKVINGTERR LEGNCPMTPR EAAVFLKAMG FPSTTNIYIV AGKIYGQNSM TAFHEEFPNV
FFHNTLATEE ELSTIKPYQN RLAALDYNLA LESDIFAYTY DGNMAKAVQG HRRFEGFRKT
INPDRQRFVR LIDRLDAGLI SWEDFSSKVK KMHQHRIGAP YLRQPGKAGM SPKLEENFYA
NPLPGCVCDT SEEQTGLNRF ERPSLRAQSL R
