TBL5_ARATH
ID TBL5_ARATH Reviewed; 485 AA.
AC F4K5K4; Q8LD24;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Protein trichome birefringence-like 5;
GN Name=TBL5; OrderedLocusNames=At5g20590; ORFNames=F7C8.180;
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].
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 [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 -!- 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; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92864.1; -; Genomic_DNA.
DR EMBL; AY086247; AAM64322.1; -; mRNA.
DR RefSeq; NP_197559.1; NM_122066.4.
DR AlphaFoldDB; F4K5K4; -.
DR SMR; F4K5K4; -.
DR STRING; 3702.AT5G20590.1; -.
DR PaxDb; F4K5K4; -.
DR PRIDE; F4K5K4; -.
DR ProteomicsDB; 234185; -.
DR EnsemblPlants; AT5G20590.1; AT5G20590.1; AT5G20590.
DR GeneID; 832181; -.
DR Gramene; AT5G20590.1; AT5G20590.1; AT5G20590.
DR KEGG; ath:AT5G20590; -.
DR Araport; AT5G20590; -.
DR TAIR; locus:2149947; AT5G20590.
DR eggNOG; ENOG502QQD3; Eukaryota.
DR HOGENOM; CLU_020953_5_3_1; -.
DR InParanoid; F4K5K4; -.
DR OMA; DGEWARD; -.
DR OrthoDB; 730689at2759; -.
DR PRO; PR:F4K5K4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K5K4; baseline and differential.
DR Genevisible; F4K5K4; 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; IPR029970; TBL5.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF8; PTHR32285:SF8; 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..485
FT /note="Protein trichome birefringence-like 5"
FT /id="PRO_0000425371"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 65..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..217
FT /note="GDS motif"
FT MOTIF 458..472
FT /note="DCXHWCLPGXXDXWN motif"
FT COMPBIAS 73..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 32
FT /note="F -> L (in Ref. 3; AAM64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> S (in Ref. 3; AAM64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="P -> Q (in Ref. 3; AAM64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> R (in Ref. 3; AAM64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="G -> D (in Ref. 3; AAM64322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55389 MW; 402B82D20680465D CRC64;
MSTSSSFPRT IVSYTVTTSL FIVIFLCSVF FFTRRTLEPS LSPYHTADIP LPAVDLPPPT
PLLPQIEPHD GDVTVETNPK EVEDSRRGGD DVAVETELKL KDVEDSHTEK TEEEEEGRGE
SPGEVSVESV EHAVIEKMRG CDLYKGSWVK GDDEYPLYQP GSCPYVDDAF DCQRNGRRDS
DYLNWRWKPD GCDLPRFNAT DFLVKLRGKS LMLVGDSMNR NQFESMLCVL REGLSDKSRM
YEVHGHNITK GRGYFVFKFE DYNCTVEFVR SHFLVREGVR ANAQGNTNPT LSIDRIDKSH
AKWKRADILV FNTGHWWVHG KTARGKNYYK EGDYIYPKFD ATEAYRRSLK TWAKWIDQNV
NPKKQLVFYR GYSSAHFRGG EWDSGGSCNG EVEPVKKGSI IDSYPLKMKI VQEAIKEMQV
PVILLNVTKL TNFRKDGHPS IYGKTNTDGK KVSTRRQDCS HWCLPGVPDV WNHLIYASLL
LQPHS
