ID   TBL21_ARATH             Reviewed;         526 AA.
AC   Q9LFT1;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein trichome birefringence-like 21;
GN   Name=TBL21; OrderedLocusNames=At5g15890; ORFNames=F1N13.30;
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; CAC01788.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92221.1; -; Genomic_DNA.
DR   PIR; T51372; T51372.
DR   RefSeq; NP_197093.1; NM_121594.2.
DR   AlphaFoldDB; Q9LFT1; -.
DR   SMR; Q9LFT1; -.
DR   STRING; 3702.AT5G15890.1; -.
DR   PaxDb; Q9LFT1; -.
DR   PRIDE; Q9LFT1; -.
DR   ProteomicsDB; 234142; -.
DR   EnsemblPlants; AT5G15890.1; AT5G15890.1; AT5G15890.
DR   GeneID; 831446; -.
DR   Gramene; AT5G15890.1; AT5G15890.1; AT5G15890.
DR   KEGG; ath:AT5G15890; -.
DR   Araport; AT5G15890; -.
DR   TAIR; locus:2146062; AT5G15890.
DR   eggNOG; ENOG502QSJI; Eukaryota.
DR   HOGENOM; CLU_020953_6_5_1; -.
DR   InParanoid; Q9LFT1; -.
DR   OMA; TISMFWS; -.
DR   OrthoDB; 724989at2759; -.
DR   PhylomeDB; Q9LFT1; -.
DR   PRO; PR:Q9LFT1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFT1; baseline and differential.
DR   Genevisible; Q9LFT1; 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..526
FT                   /note="Protein trichome birefringence-like 21"
FT                   /id="PRO_0000425386"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   REGION          57..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           260..262
FT                   /note="GDS motif"
FT   MOTIF           501..515
FT                   /note="DCXHWCLPGXXDXWN motif"
FT   COMPBIAS        106..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  59866 MW;  2B08C04FFD2CB91D CRC64;
     MELPLFAILQ RTPRVAITLA FVLFVLTIVP ALYTLLADPI LPPSISSFET DHTRLSHLNS
     SSNQIPSPVN GSIPTPPYHT PSKHRKSSFH RIPKPKKGPI SSPTDHIPLR QRSSSFDQIP
     SPMNSPVPAP PHRNSSADQS PSPVNGPIPA PLNHTSLRHL NSSSDDHSSP VTTSPSRTRI
     RDDEQMCDLF TGEWVPNEEA PYYTNTTCWA IHEHQNCMKY GRPDTGFMRW RWKPESCDLP
     IFDPQEFLEM VRGKAMGFVG DSISRNQVQS LLCLLSRVEY PEDISPSPDT DFKVWNYTSY
     NFTLHVMWSP FLVKATKPDP KSNFFSLYLD EYDTKWTSQL DQLDYLVISS GHWFSRPVIF
     YENQQISGCQ YCALPNTTEL PLTYGYRKAL RISLKAIIEN FKGLAFLRSF SPQHFEGGAW
     NEGGDCVRTQ PYRRNETIPE ADLKVHDIQR EEFRAAEEDG MKKSGLRLKL MDTTQAMLLR
     PDGHPGRYGH LQNPNVTLRN DCIHWCLPGP IDTLNDILLQ MMKTDN