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TBL11_ARATH
ID   TBL11_ARATH             Reviewed;         464 AA.
AC   Q5BPJ0;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein trichome birefringence-like 11;
GN   Name=TBL11; OrderedLocusNames=At5g19160; ORFNames=T24G5.60;
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].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=16244158; DOI=10.1104/pp.105.063479;
RA   Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA   Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT   "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT   reveals numerous transcript variants.";
RL   Plant Physiol. 139:1323-1337(2005).
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   -!- 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; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92663.1; -; Genomic_DNA.
DR   EMBL; AY924838; AAX23913.1; -; mRNA.
DR   EMBL; DQ132728; AAZ52758.1; -; mRNA.
DR   EMBL; DQ132729; AAZ52759.1; -; mRNA.
DR   RefSeq; NP_197417.1; NM_121921.4.
DR   AlphaFoldDB; Q5BPJ0; -.
DR   SMR; Q5BPJ0; -.
DR   STRING; 3702.AT5G19160.1; -.
DR   iPTMnet; Q5BPJ0; -.
DR   PaxDb; Q5BPJ0; -.
DR   PRIDE; Q5BPJ0; -.
DR   ProteomicsDB; 234240; -.
DR   EnsemblPlants; AT5G19160.1; AT5G19160.1; AT5G19160.
DR   GeneID; 832036; -.
DR   Gramene; AT5G19160.1; AT5G19160.1; AT5G19160.
DR   KEGG; ath:AT5G19160; -.
DR   Araport; AT5G19160; -.
DR   TAIR; locus:2182157; AT5G19160.
DR   eggNOG; ENOG502QPPC; Eukaryota.
DR   HOGENOM; CLU_020953_0_0_1; -.
DR   InParanoid; Q5BPJ0; -.
DR   OMA; RRKMVMP; -.
DR   OrthoDB; 667501at2759; -.
DR   PhylomeDB; Q5BPJ0; -.
DR   PRO; PR:Q5BPJ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q5BPJ0; baseline and differential.
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   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..464
FT                   /note="Protein trichome birefringence-like 11"
FT                   /id="PRO_0000425377"
FT   TRANSMEM        33..53
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           172..174
FT                   /note="GDS motif"
FT   MOTIF           423..437
FT                   /note="DCXHWCLPGXXDXWN motif"
SQ   SEQUENCE   464 AA;  54225 MW;  E8D5526E2ACE56DF CRC64;
     MSKNPSQEED EAMPISEVVI KRFKRLRLVF EPSLGVLGFF LVGLCLVFSF FYLDYRTVAK
     TKSHDFSDQS ERFLWLKELD GFEVNNTKVG FLEESGNGCD LFNGKWVWDE SYPLYQSKDC
     TFIDEGFRCT EFGRPDLFYT KWRWQPNHCD LPRFDAKLML EKLRNKRLVF VGDSIGRNQW
     ESLLCMLASA ISNKNLVYEV NNRPITKHMG FFVFRFHDYN CTVEYYRAPF LVLQSRPPEG
     SPEKVKTTLK LETMEWTADK WRDADILVFN TGHWWNYEKT IRGGCYFQEG EKVRMRMKIE
     HAYRRAMKTV MKWIQEEVDA NKTQVFFRTF APVHFRGGDW RTGGTCHMET LPDFGASLVP
     AETWDHIKLL QDVLSSSLYY SNISETVKLK VLNITAMAAQ RNDGHPSLYY LGLAGPAPFH
     RQDCSHWCLP GVPDSWNELL YALFLKHEGY SSPRSNNSDT DNFT
 
 
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