TBR_ARATH
ID TBR_ARATH Reviewed; 608 AA.
AC Q9FG35; D9I8D9; Q8LEF8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein trichome birefringence;
GN Name=TBR; OrderedLocusNames=At5g06700; ORFNames=MPH15.5;
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 [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLY-427, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20388664; DOI=10.1104/pp.110.153320;
RA Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA Persson S., Delmer D., Scheible W.R.;
RT "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL Plant Physiol. 153:590-602(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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] OF 280-608.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL Plant J. 49:786-799(2007).
RN [7]
RP 3D-STRUCTURE MODELING, AND FUNCTION.
RX PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA Bischoff V., Selbig J., Scheible W.R.;
RT "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL Plant Signal. Behav. 5:1057-1059(2010).
CC -!- FUNCTION: Required during cellulose deposition (PubMed:20388664). May
CC act as a bridging protein that binds pectin and other cell wall
CC polysaccharides. Probably involved in maintaining esterification of
CC pectins (Probable). May be involved in the specific O-acetylation of
CC cell wall polymers (By similarity). {ECO:0000250|UniProtKB:Q9LY46,
CC ECO:0000269|PubMed:20388664, ECO:0000305|PubMed:20657172}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf vasculature, growing part of the
CC root, expanding inflorescence stems and trichomes.
CC {ECO:0000269|PubMed:20388664}.
CC -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC it is unlikely that this protein belongs to the catalytically active
CC pectin esterases (PubMed:20657172). Tbr mutants are lacking leaf and
CC stem trichome birefringence characteristic of plant cells that contain
CC highly ordered cellulose in their secondary walls (PubMed:20388664).
CC {ECO:0000305|PubMed:20388664, ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; HM120873; ADI48429.1; -; Genomic_DNA.
DR EMBL; AP002032; BAB09804.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91052.1; -; Genomic_DNA.
DR EMBL; AK229444; BAF01304.1; -; mRNA.
DR EMBL; AY085444; AAM67355.1; -; mRNA.
DR RefSeq; NP_568173.2; NM_120753.4.
DR AlphaFoldDB; Q9FG35; -.
DR SMR; Q9FG35; -.
DR STRING; 3702.AT5G06700.1; -.
DR PaxDb; Q9FG35; -.
DR PRIDE; Q9FG35; -.
DR ProMEX; Q9FG35; -.
DR ProteomicsDB; 233017; -.
DR EnsemblPlants; AT5G06700.1; AT5G06700.1; AT5G06700.
DR GeneID; 830559; -.
DR Gramene; AT5G06700.1; AT5G06700.1; AT5G06700.
DR KEGG; ath:AT5G06700; -.
DR Araport; AT5G06700; -.
DR TAIR; locus:2170184; AT5G06700.
DR eggNOG; ENOG502QVEF; Eukaryota.
DR HOGENOM; CLU_020953_5_0_1; -.
DR InParanoid; Q9FG35; -.
DR OMA; QNNESHD; -.
DR OrthoDB; 336321at2759; -.
DR PhylomeDB; Q9FG35; -.
DR PRO; PR:Q9FG35; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG35; baseline and differential.
DR Genevisible; Q9FG35; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0045489; P:pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..608
FT /note="Protein trichome birefringence"
FT /id="PRO_0000425366"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 101..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 328..330
FT /note="GDS motif"
FT MOTIF 573..587
FT /note="DCXHWCLPGXXDXWN motif"
FT MUTAGEN 427
FT /note="G->E: Reduced crystalline cellulose in trichomes."
FT /evidence="ECO:0000269|PubMed:20388664"
SQ SEQUENCE 608 AA; 67925 MW; 75B5DF42E697586C CRC64;
MASDAVKYMP IHGGGTTATT AADIKSFFSA LKPKKTSTFA YAFVITFVSF TLFFAFSPSP
NSSSPWFSNI FTSSSTTTTS DNTSGSQFSS IFSYILPNVT STKPTNRSSD ATDSLSVNAT
SPPLNSNSKN GTLQTPAPET HTPVAKNTTF ESPIVNGTNP DAKNNTSSHP LLSDKSSTTG
SNNQSRTTAD TETVNRNQTT SPAPSKAPVS VDLKTNSSSN SSTASSTPKK QTKTVDLVSS
VKQEIEKWSE SLKNCEFFDG EWIKDDSYPL YKPGSCNLID EQFNCITNGR PDKDFQKLKW
KPKKCSLPRL NGAILLEMLR GRRLVFVGDS LNRNMWESLV CILKGSVKDE TKVYEARGRH
HFRGEAEYSF VFQDYNCTVE FFVSPFLVQE WEIVDKKGTK KETLRLDLVG KSSEQYKGAD
VIVFNTGHWW THEKTSKGED YYQEGSNVYH ELAVLEAFRK ALTTWGRWVE KNVNPAKSLV
FFRGYSASHF SGGQWNSGGA CDSETEPIKN DTYLTPYPSK MKVLEKVLRG MKTPVTYLNI
TRLTDYRKDG HPSVYRKQSL SEKEKKSPLL YQDCSHWCLP GVPDSWNEIL YAELIVKLNQ
LSQTQRKT
