TBL1_ARATH
ID TBL1_ARATH Reviewed; 556 AA.
AC Q9LHL6; A0MEV4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein trichome birefringence-like 1;
GN Name=TBL1; OrderedLocusNames=At3g12060; ORFNames=MEC18.19, T21B14.12;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 FUNCTION, TISSUE 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 [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: Can complement TBR and is therefore functionally equivalent,
CC but may work in different tissue (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: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Not expressed in 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. {ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28553.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP002040; BAB03118.1; -; Genomic_DNA.
DR EMBL; AC069473; AAG51057.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75143.1; -; Genomic_DNA.
DR EMBL; DQ446655; ABE65935.1; -; mRNA.
DR EMBL; DQ653077; ABK28553.1; ALT_SEQ; mRNA.
DR RefSeq; NP_187813.1; NM_112040.2.
DR AlphaFoldDB; Q9LHL6; -.
DR SMR; Q9LHL6; -.
DR BioGRID; 5714; 2.
DR IntAct; Q9LHL6; 2.
DR STRING; 3702.AT3G12060.1; -.
DR PaxDb; Q9LHL6; -.
DR PRIDE; Q9LHL6; -.
DR ProteomicsDB; 233014; -.
DR EnsemblPlants; AT3G12060.1; AT3G12060.1; AT3G12060.
DR GeneID; 820380; -.
DR Gramene; AT3G12060.1; AT3G12060.1; AT3G12060.
DR KEGG; ath:AT3G12060; -.
DR Araport; AT3G12060; -.
DR TAIR; locus:2088659; AT3G12060.
DR eggNOG; ENOG502SHHV; Eukaryota.
DR HOGENOM; CLU_020953_5_1_1; -.
DR InParanoid; Q9LHL6; -.
DR OMA; AKENISC; -.
DR OrthoDB; 336321at2759; -.
DR PhylomeDB; Q9LHL6; -.
DR PRO; PR:Q9LHL6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHL6; baseline and differential.
DR Genevisible; Q9LHL6; 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 GO; GO:0030244; P:cellulose biosynthetic process; 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 2: Evidence at transcript level;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..556
FT /note="Protein trichome birefringence-like 1"
FT /id="PRO_0000425367"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 269..271
FT /note="GDS motif"
FT MOTIF 514..528
FT /note="DCXHWCLPGXXDXWN motif"
SQ SEQUENCE 556 AA; 63005 MW; F697359ABBB7213F CRC64;
MALDSVKHLP IHGVSAFSSV TVEIKSFFST VKPRKTSTFV YAFVVTFVAL TVFLAFSPSP
ITVALAPSIS SYVLPNITVS NSSNSSPSSL DSNFTTLRTP APENLTAVTK NLTFESPVAN
GTTDTNAKTI TIQFQTGHAK ENISCPDNKT ARDLDTHGAR KAPLSEVLAV NSTASPKRKQ
RRKSSLRKVI ESLKSCEFFE GDWVKDDSYP LYKPGSCNLI DEQFNCISNG RPDVDFQKLK
WKPKQCSLPR LNGGKLLEMI RGRRLVFVGD SLNRNMWESL VCILKGSVKD ESQVFEAHGR
HQFRWEAEYS FVFKDYNCTV EFFASPFLVQ EWEVTEKNGT KKETLRLDLV GKSSEQYKGA
DILVFNTGHW WTHEKTSKGE DYYQEGSTVH PKLDVDEAFR KALTTWGRWV DKNVNPKKSL
VFFRGYSPSH FSGGQWNAGG ACDDETEPIK NETYLTPYML KMEILERVLR GMKTPVTYLN
ITRLTDYRKD AHPSIYRKQK LSAEESKSPL LYQDCSHWCL PGVPDSWNEI FYAELLVKLD
QLGGKRRRKA LKDHRS