ID   TBL6_ARATH              Reviewed;         475 AA.
AC   Q9LZQ1;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein trichome birefringence-like 6;
GN   Name=TBL6; OrderedLocusNames=At3g62390; ORFNames=T12C14.90;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
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   [6]
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   [7]
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; AL162507; CAB82953.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80346.1; -; Genomic_DNA.
DR   EMBL; AK229044; BAF00927.1; -; mRNA.
DR   EMBL; AY085065; AAM61621.1; -; mRNA.
DR   PIR; T48031; T48031.
DR   RefSeq; NP_191798.1; NM_116104.7.
DR   AlphaFoldDB; Q9LZQ1; -.
DR   SMR; Q9LZQ1; -.
DR   STRING; 3702.AT3G62390.1; -.
DR   PaxDb; Q9LZQ1; -.
DR   PRIDE; Q9LZQ1; -.
DR   ProteomicsDB; 233012; -.
DR   EnsemblPlants; AT3G62390.1; AT3G62390.1; AT3G62390.
DR   GeneID; 825412; -.
DR   Gramene; AT3G62390.1; AT3G62390.1; AT3G62390.
DR   KEGG; ath:AT3G62390; -.
DR   Araport; AT3G62390; -.
DR   TAIR; locus:2096094; AT3G62390.
DR   eggNOG; ENOG502QQD3; Eukaryota.
DR   HOGENOM; CLU_020953_5_3_1; -.
DR   InParanoid; Q9LZQ1; -.
DR   OMA; LRIDTMD; -.
DR   OrthoDB; 785345at2759; -.
DR   PhylomeDB; Q9LZQ1; -.
DR   PRO; PR:Q9LZQ1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LZQ1; baseline and differential.
DR   Genevisible; Q9LZQ1; 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; IPR029965; TBL6.
DR   InterPro; IPR025846; TBL_N.
DR   PANTHER; PTHR32285; PTHR32285; 1.
DR   PANTHER; PTHR32285:SF211; PTHR32285:SF211; 1.
DR   Pfam; PF13839; PC-Esterase; 1.
DR   Pfam; PF14416; PMR5N; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..475
FT                   /note="Protein trichome birefringence-like 6"
FT                   /id="PRO_0000425372"
FT   TRANSMEM        14..34
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           211..213
FT                   /note="GDS motif"
FT   MOTIF           450..464
FT                   /note="DCXHWCLPGXXDXWN motif"
SQ   SEQUENCE   475 AA;  54638 MW;  7FF8CC8DDC4E8CB6 CRC64;
     MERQRSFSVK STRVLAFIIT IISSAIVFFT FFSSSLLKSN SSLYPTPEAN FQIDLSPIAA
     ISDSSVSPQA SPILISTHFN SPENTSGSSK ISVFEQKISG ESLVKEVREI ANLTSIKVIE
     LPSNNGEDKK TEKRIEECDV TKGKWVYDSD YPLYTNASCP FIDEGFGCQS NGRLDLNYMN
     WRWEPQDCHA PRFNATKMLE MIRGKRLVFV GDSINRNQWE SMLCLLFQAV KDPKRVYETH
     NRRITKEKGN YSFRFVDYKC TVEFYVTHFL VREGRARIGK KRRETLRIDA MDRTSSRWKG
     ANILVFNTAH WWSHYKTKSG VNYYQEGDLI HPKLDVSTAF KKALQTWSSW VDKNVDPKKT
     RVFFRSAAPS HFSGGEWNSG GHCREANMPL NQTFKPSYSS KKSIVEDVLK QMRTPVTLLN
     VSGLSQYRID AHPSIYGTKP ENRRSRAVQD CSHWCLPGVP DTWNHFLYLH LLHKR