TBL41_ARATH
ID TBL41_ARATH Reviewed; 356 AA.
AC F4IWA8; B9DI65; Q8W4B3; Q9LH70;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Protein trichome birefringence-like 41;
GN Name=TBL41; OrderedLocusNames=At3g14850; ORFNames=T21E2.11;
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 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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IWA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IWA8-2; Sequence=VSP_053696;
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=BAB02651.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002061; BAB02651.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75575.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75576.1; -; Genomic_DNA.
DR EMBL; AY062682; AAL32760.1; -; mRNA.
DR EMBL; AY093337; AAM13336.1; -; mRNA.
DR EMBL; AK317777; BAH20432.1; -; mRNA.
DR RefSeq; NP_188103.2; NM_112347.4. [F4IWA8-2]
DR RefSeq; NP_974314.2; NM_202585.3. [F4IWA8-1]
DR AlphaFoldDB; F4IWA8; -.
DR SMR; F4IWA8; -.
DR BioGRID; 6048; 2.
DR IntAct; F4IWA8; 2.
DR PaxDb; F4IWA8; -.
DR PRIDE; F4IWA8; -.
DR ProteomicsDB; 234242; -. [F4IWA8-1]
DR EnsemblPlants; AT3G14850.1; AT3G14850.1; AT3G14850. [F4IWA8-2]
DR EnsemblPlants; AT3G14850.2; AT3G14850.2; AT3G14850. [F4IWA8-1]
DR GeneID; 820714; -.
DR Gramene; AT3G14850.1; AT3G14850.1; AT3G14850. [F4IWA8-2]
DR Gramene; AT3G14850.2; AT3G14850.2; AT3G14850. [F4IWA8-1]
DR KEGG; ath:AT3G14850; -.
DR Araport; AT3G14850; -.
DR TAIR; locus:2099402; AT3G14850.
DR eggNOG; ENOG502QVJM; Eukaryota.
DR InParanoid; F4IWA8; -.
DR OMA; PHACNLQ; -.
DR PhylomeDB; F4IWA8; -.
DR PRO; PR:F4IWA8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IWA8; baseline and differential.
DR Genevisible; F4IWA8; 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 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..356
FT /note="Protein trichome birefringence-like 41"
FT /id="PRO_0000425406"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 107..109
FT /note="GDS motif"
FT MOTIF 333..347
FT /note="DCXHWCLPGXXDXWN motif"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053696"
FT CONFLICT 152
FT /note="K -> E (in Ref. 4; BAH20432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40111 MW; BE6297F62787F0A6 CRC64;
MGSKDNAISN DSALVLSLLL LLLLPLLHEA AEGCDMFTGR WVKDDSYPLY NSSTCPFIRH
EFSCQRNGRP DLDYSTFRWQ PLSCKLARFN GLQFLKKNKG KKIMFVGDSL SLNQWQSLAC
MLHSSVPNST YTLTTQGSIS TYTFKEYGLE LKLDRNVYLV DIVREKIGRV LKLDSINDGK
NWVEMDTLIF NTWHWWSRRG PAQPWDLIQI GTNVTKDMDR VAAFEIALGT WGKWVDTVLN
TKKTRVFFQG ISPSHYKGVL WGEPAAKSCV GQKEPLLGTK YPGGLPAEVG VLKRALGKIS
KPVTLLDITM LSLLRKDAHP SVYGLGGRNS SGDCSHWCLS GVPDTWNEIL YNYMVE
