TBL3_ARATH
ID TBL3_ARATH Reviewed; 434 AA.
AC Q8LED3; B9DH72; F4K9C5; Q0WSF4; Q9M036;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein trichome birefringence-like 3;
GN Name=TBL3; OrderedLocusNames=At5g01360; ORFNames=T10O8.70;
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=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 [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).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 214-324 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 FUNCTION, DISRUPTION PHENOTYPE, 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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21124849; DOI=10.1371/journal.pone.0015481;
RA Oikawa A., Joshi H.J., Rennie E.A., Ebert B., Manisseri C.,
RA Heazlewood J.L., Scheller H.V.;
RT "An integrative approach to the identification of Arabidopsis and rice
RT genes involved in xylan and secondary wall development.";
RL PLoS ONE 5:E15481-E15481(2010).
RN [9]
RP 3D-STRUCTURE MODELING.
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: Involved in secondary cell wall cellulose deposition.
CC Required for normal stem development (PubMed:20388664). May act as a
CC bridging protein that binds pectin and other cell wall polysaccharides.
CC Probably involved in maintaining esterification of pectins (By
CC similarity). May be involved in the specific O-acetylation of cell wall
CC polymers (By similarity). {ECO:0000250|UniProtKB:Q9FG35,
CC ECO:0000250|UniProtKB:Q9LY46, ECO:0000269|PubMed:20388664}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LED3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LED3-2; Sequence=VSP_053686;
CC -!- DISRUPTION PHENOTYPE: Reduction in inflorescence stem elongation.
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. {ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161746; CAB81919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90331.1; -; Genomic_DNA.
DR EMBL; AY085483; AAM62709.1; -; mRNA.
DR EMBL; AK227978; BAE99944.1; -; mRNA.
DR EMBL; AK317421; BAH20089.1; -; mRNA.
DR PIR; T48158; T48158.
DR RefSeq; NP_568089.1; NM_120214.4. [Q8LED3-1]
DR AlphaFoldDB; Q8LED3; -.
DR SMR; Q8LED3; -.
DR STRING; 3702.AT5G01360.1; -.
DR PaxDb; Q8LED3; -.
DR PRIDE; Q8LED3; -.
DR ProteomicsDB; 234197; -. [Q8LED3-1]
DR EnsemblPlants; AT5G01360.1; AT5G01360.1; AT5G01360. [Q8LED3-1]
DR GeneID; 830298; -.
DR Gramene; AT5G01360.1; AT5G01360.1; AT5G01360. [Q8LED3-1]
DR KEGG; ath:AT5G01360; -.
DR Araport; AT5G01360; -.
DR TAIR; locus:2179172; AT5G01360.
DR eggNOG; ENOG502QT29; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q8LED3; -.
DR OrthoDB; 697301at2759; -.
DR PhylomeDB; Q8LED3; -.
DR PRO; PR:Q8LED3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LED3; baseline and differential.
DR Genevisible; Q8LED3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990538; F:xylan O-acetyltransferase activity; IMP:TAIR.
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 GO; GO:1990937; P:xylan acetylation; IEA:EnsemblPlants.
DR GO; GO:0045492; P:xylan biosynthetic process; IMP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR029972; TBL3/8.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF294; PTHR32285:SF294; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Protein trichome birefringence-like 3"
FT /id="PRO_0000425369"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 166..168
FT /note="GDS motif"
FT MOTIF 413..427
FT /note="DCXHWCLPGXXDXWN motif"
FT VAR_SEQ 325..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053686"
FT CONFLICT 276
FT /note="G -> E (in Ref. 4; BAE99944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 49829 MW; 7C69D66539E5EBD2 CRC64;
MSFLIPNRGV GGTKIPLSII VLVLCGFMFF ILLYTERISL LSSSSSSSSS FFKLKSCPRK
DVSSKPKEKI RKERSEILEV LDDRFEFDPE ECNVAAGKWV YNSSIEPLYT DRSCPYIDRQ
FSCMKNGQPE TDYLRWEWQP DDCTIPRFSP KLAMNKLRGK RLLFVGDSLQ RSQWESFVCL
VESIIPEGEK SMKRSQKYFV FKAKEYNATI EFYWAPYIVE SNTDIPVISD PKKRIVKVDS
VKDRAKFWEG ADILVFNTYV WWMSGLRMKA LWGSFGNGES GAEALDTQVA YRLGLKTWAN
WVDSTVDPNK TRVFFTTMSP THTRSADWGK PNGTKCFNET KPIKDKKFWG TGSNKQMMKV
VSSVIKHMTT HVTVINITQL SEYRIDAHTS VYTETGGKIL TAEQRADPMH HADCIHWCLP
GLPDTWNRIL LAHL
