TBL35_ARATH
ID TBL35_ARATH Reviewed; 449 AA.
AC Q8RXQ1; F4K9F9; Q8LG69; Q9M014;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein trichome birefringence-like 35;
GN Name=TBL35; OrderedLocusNames=At5g01620; ORFNames=F7A7.140;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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].
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RXQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RXQ1-2; Sequence=VSP_053694;
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=CAB82278.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL161946; CAB82278.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90366.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90367.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90368.1; -; Genomic_DNA.
DR EMBL; AY080736; AAL86006.1; -; mRNA.
DR EMBL; AY117243; AAM51318.1; -; mRNA.
DR EMBL; AY084435; AAM61008.1; -; mRNA.
DR PIR; T48183; T48183.
DR RefSeq; NP_001190201.1; NM_001203272.1. [Q8RXQ1-2]
DR RefSeq; NP_568093.1; NM_120240.1. [Q8RXQ1-1]
DR RefSeq; NP_850749.1; NM_180418.4. [Q8RXQ1-1]
DR AlphaFoldDB; Q8RXQ1; -.
DR SMR; Q8RXQ1; -.
DR STRING; 3702.AT5G01620.3; -.
DR iPTMnet; Q8RXQ1; -.
DR PaxDb; Q8RXQ1; -.
DR PRIDE; Q8RXQ1; -.
DR ProteomicsDB; 232993; -. [Q8RXQ1-1]
DR EnsemblPlants; AT5G01620.1; AT5G01620.1; AT5G01620. [Q8RXQ1-1]
DR EnsemblPlants; AT5G01620.2; AT5G01620.2; AT5G01620. [Q8RXQ1-1]
DR EnsemblPlants; AT5G01620.3; AT5G01620.3; AT5G01620. [Q8RXQ1-2]
DR GeneID; 831716; -.
DR Gramene; AT5G01620.1; AT5G01620.1; AT5G01620. [Q8RXQ1-1]
DR Gramene; AT5G01620.2; AT5G01620.2; AT5G01620. [Q8RXQ1-1]
DR Gramene; AT5G01620.3; AT5G01620.3; AT5G01620. [Q8RXQ1-2]
DR KEGG; ath:AT5G01620; -.
DR Araport; AT5G01620; -.
DR TAIR; locus:2149785; AT5G01620.
DR eggNOG; ENOG502QV6P; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR OMA; LPTMQMV; -.
DR OrthoDB; 571838at2759; -.
DR PhylomeDB; Q8RXQ1; -.
DR PRO; PR:Q8RXQ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXQ1; baseline and differential.
DR Genevisible; Q8RXQ1; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:1990538; F:xylan O-acetyltransferase activity; IMP:TAIR.
DR GO; GO:0045492; P:xylan 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 Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..449
FT /note="Protein trichome birefringence-like 35"
FT /id="PRO_0000425400"
FT TRANSMEM 12..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 185..187
FT /note="GDS motif"
FT MOTIF 428..442
FT /note="DCXHWCLPGXXDXWN motif"
FT VAR_SEQ 70
FT /note="H -> HGFCFEKNA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053694"
FT CONFLICT 74
FT /note="D -> G (in Ref. 4; AAM61008)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="W -> C (in Ref. 4; AAM61008)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> V (in Ref. 4; AAM61008)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="G -> S (in Ref. 4; AAM61008)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="Q -> R (in Ref. 4; AAM61008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 52689 MW; 996C685BA017B9B5 CRC64;
MSQRWSRKKS RLPLAGLLFI LVVTFMILFN ERSIQQIHHH AASHTQNLRE PSTFDFVKPN
VPRINYLGAH EVLDRFSKCN STKEYSGKKI GWVDPFEDHP GQVTKEEQKC DVFSGKWVFD
NSSSYPLHKE SQCPYMSDQL ACQKHGRKDL EYQHWRWQPH ACNLKRWNAI EMWEKLRGKR
LMFVGDSLNR GQWISMVCLL QSVIPRDKQS MSPNAHLTIF RAEDYNATVE FLWAPLLVES
NSDDPVNHRL SERIIRPDSV LKHASKWQHA DILIFNTYLW WRQDSVKLRW SSEEKGSCEE
VKSAEGMEMA MDSWGDWVAN NVDPNKKRVF FVTMSPTHQW SREWNPGSEG NCYGEKKPIE
EESYWGSGSD IPTMRMVKRV LERLGPKVSV INITQLSEYR KDGHPSVYRK FWEPLNEDRL
KNPASYSDCT HWCVPGVPDV WNQLLFHFL
