TBL19_ARATH
ID TBL19_ARATH Reviewed; 426 AA.
AC Q9LFT0;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein trichome birefringence-like 19;
GN Name=TBL19; OrderedLocusNames=At5g15900; ORFNames=F1N13.40;
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 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 [4]
RP 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 [5]
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: May act as a bridging protein that binds pectin and other
CC cell wall polysaccharides. Probably involved in maintaining
CC esterification of pectins (By similarity). May be involved in the
CC specific O-acetylation of cell wall polymers (By similarity).
CC {ECO:0000250|UniProtKB:Q9FG35, ECO:0000250|UniProtKB:Q9LY46}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
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}.
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DR EMBL; AL391145; CAC01789.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92222.1; -; Genomic_DNA.
DR PIR; T51373; T51373.
DR RefSeq; NP_197094.1; NM_121595.3.
DR AlphaFoldDB; Q9LFT0; -.
DR SMR; Q9LFT0; -.
DR STRING; 3702.AT5G15900.1; -.
DR PaxDb; Q9LFT0; -.
DR PRIDE; Q9LFT0; -.
DR ProteomicsDB; 234245; -.
DR EnsemblPlants; AT5G15900.1; AT5G15900.1; AT5G15900.
DR GeneID; 831447; -.
DR Gramene; AT5G15900.1; AT5G15900.1; AT5G15900.
DR KEGG; ath:AT5G15900; -.
DR Araport; AT5G15900; -.
DR TAIR; locus:2146077; AT5G15900.
DR eggNOG; ENOG502QR7B; Eukaryota.
DR HOGENOM; CLU_020953_6_5_1; -.
DR InParanoid; Q9LFT0; -.
DR PhylomeDB; Q9LFT0; -.
DR PRO; PR:Q9LFT0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFT0; baseline and differential.
DR Genevisible; Q9LFT0; AT.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..426
FT /note="Protein trichome birefringence-like 19"
FT /id="PRO_0000425384"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 142..144
FT /note="GDS motif"
FT MOTIF 388..402
FT /note="DCXHWCLPGXXDXWN motif"
SQ SEQUENCE 426 AA; 49527 MW; 01860E07015C19F3 CRC64;
MELVHSATFP CKQKLLIAVT IATSLLTIIP LLYPLLEDPN FFLKQQPPSQ SSIINLENGV
VTSHDSCDIF SGEWVPNPEA PYYTNTTCWA IHEHQNCMKF GRPDTDFIKW KWKPYGCEDG
LPVFDPVRFL EIVRGKTMAF VGDSVSRNHM QSLICLLSQV EYPMDASVKN DDYFKRWTYE
TYNFTIAAFW TPHLVKSKEP DQTQPKHIDI FDLYLDEADE SWTADIGDFD FVIISSGHWH
YRPSVYYENR TITGCHYCQL PNITDLTMFY GYRKAFRTAF KAILDSESFK GVMYLRSFAP
SHFEGGLWNE GGDCLRKQPY RSNETQDETT MKLHKIQLEE FWRAEEEAKK KGKRLRLLDT
TQAMWLRPDG HPSRYGHIPE ANVTLYNDCV HWCLPGPIDN LNDFLLAMLK REEDKGFLAQ
VRKMLS
