TBL12_ARATH
ID TBL12_ARATH Reviewed; 407 AA.
AC Q9FGE9; F4KDP9; F4KDQ1; Q944J6;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein trichome birefringence-like 12;
GN Name=TBL12; OrderedLocusNames=At5g64470; ORFNames=T12B11.6;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORMS 1 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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 [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FGE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FGE9-2; Sequence=VSP_053690;
CC Name=3;
CC IsoId=Q9FGE9-3; Sequence=VSP_053689, VSP_053691;
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; AB025640; BAB11608.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97903.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97904.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97905.1; -; Genomic_DNA.
DR EMBL; AF360229; AAK25939.1; -; mRNA.
DR EMBL; AY040030; AAK64088.1; -; mRNA.
DR EMBL; AF428365; AAL16295.1; -; mRNA.
DR RefSeq; NP_001190614.1; NM_001203685.1. [Q9FGE9-2]
DR RefSeq; NP_201252.1; NM_125843.3. [Q9FGE9-1]
DR RefSeq; NP_851267.1; NM_180936.2. [Q9FGE9-3]
DR AlphaFoldDB; Q9FGE9; -.
DR SMR; Q9FGE9; -.
DR STRING; 3702.AT5G64470.2; -.
DR PaxDb; Q9FGE9; -.
DR PRIDE; Q9FGE9; -.
DR ProteomicsDB; 234263; -. [Q9FGE9-1]
DR EnsemblPlants; AT5G64470.1; AT5G64470.1; AT5G64470. [Q9FGE9-3]
DR EnsemblPlants; AT5G64470.2; AT5G64470.2; AT5G64470. [Q9FGE9-1]
DR EnsemblPlants; AT5G64470.3; AT5G64470.3; AT5G64470. [Q9FGE9-2]
DR GeneID; 836568; -.
DR Gramene; AT5G64470.1; AT5G64470.1; AT5G64470. [Q9FGE9-3]
DR Gramene; AT5G64470.2; AT5G64470.2; AT5G64470. [Q9FGE9-1]
DR Gramene; AT5G64470.3; AT5G64470.3; AT5G64470. [Q9FGE9-2]
DR KEGG; ath:AT5G64470; -.
DR Araport; AT5G64470; -.
DR TAIR; locus:2179386; AT5G64470.
DR eggNOG; ENOG502QUKA; Eukaryota.
DR HOGENOM; CLU_020953_1_0_1; -.
DR InParanoid; Q9FGE9; -.
DR OMA; GHWWGFD; -.
DR OrthoDB; 834476at2759; -.
DR PhylomeDB; Q9FGE9; -.
DR PRO; PR:Q9FGE9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGE9; baseline and differential.
DR Genevisible; Q9FGE9; 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; IPR029966; TBL12.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF23; PTHR32285:SF23; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..407
FT /note="Protein trichome birefringence-like 12"
FT /id="PRO_0000425378"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 130..132
FT /note="GDS motif"
FT MOTIF 379..393
FT /note="DCXHWCLPGXXDXWN motif"
FT VAR_SEQ 315..325
FT /note="LDLWFDPRNNG -> EQWSEQRSKKD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053689"
FT VAR_SEQ 315..322
FT /note="LDLWFDPR -> VW (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053690"
FT VAR_SEQ 326..407
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053691"
FT CONFLICT 198
FT /note="G -> E (in Ref. 3; AAL16295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 47142 MW; 5753AC62A35CA1B0 CRC64;
MELGSRRIYT TMPSKLRSSS SLLPRILLLS LLLLLFYSLI LRRPITSNIA SPPPCDLFSG
RWVFNPETPK PLYDETCPFH RNAWNCLRNK RDNMDVINSW RWEPNGCGLS RIDPTRFLGM
MRNKNVGFVG DSLNENFLVS FLCILRVADP SAIKWKKKKA WRGAYFPKFN VTVAYHRAVL
LAKYQWQARS SAEANQDGVK GTYRVDVDVP ANEWINVTSF YDVLIFNSGH WWGYDKFPKE
TPLVFYRKGK PINPPLDILP GFELVLQNMV SYIQREVPAK TLKFWRLQSP RHFYGGDWNQ
NGSCLLDKPL EENQLDLWFD PRNNGVNKEA RKINQIIKNE LQTTKIKLLD LTHLSEFRAD
AHPAIWLGKQ DAVAIWGQDC MHWCLPGVPD TWVDILAELI LTNLKTE
