(data stored in ACNUC13479 zone)

SWISSPROT: TBL3_ARATH

ID   TBL3_ARATH              Reviewed;         434 AA.
AC   Q8LED3; B9DH72; F4K9C5; Q0WSF4; Q9M036;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   30-AUG-2017, entry version 79.
DE   RecName: Full=Protein trichome birefringence-like 3;
GN   Name=TBL3; OrderedLocusNames=At5g01360; ORFNames=T10O8.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 214-324 (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
RA   Seki M., 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   [6]
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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=20388664; DOI=10.1104/pp.110.153320;
RA   Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A.,
RA   Eshed R., Persson S., Delmer D., Scheible W.R.;
RT   "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-
RT   specific DUF231 proteins required for cellulose biosynthesis in
RT   Arabidopsis.";
RL   Plant Physiol. 153:590-602(2010).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21124849; DOI=10.1371/journal.pone.0015481;
RA   Oikawa A., Joshi H.J., Rennie E.A., Ebert B., Manisseri C.,
RA   Heazlewood J.L., Scheller H.V.;
RT   "An integrative approach to the identification of Arabidopsis and rice
RT   genes involved in xylan and secondary wall development.";
RL   PLoS ONE 5:E15481-E15481(2010).
RN   [9]
RP   FUNCTION.
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: Involved in secondary cell wall cellulose deposition.
CC       Required for normal stem development. May act as a bridging
CC       protein that binds pectin and other cell wall polysaccharides.
CC       Probably involved in maintaining esterification of pectins or
CC       maybe in the specific O-acetylation of cell wall polymers.
CC       {ECO:0000269|PubMed:20388664, ECO:0000269|PubMed:20657172}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8LED3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8LED3-2; Sequence=VSP_053686;
CC   -!- DISRUPTION PHENOTYPE: Reduction in inflorescence stem elongation.
CC       {ECO:0000269|PubMed:20388664}.
CC   -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases,
CC       but it is unlikely that this protein belongs to the catalytically
CC       active pectin esterases. {ECO:0000305|PubMed:20657172}.
CC   -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB81919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL161746; CAB81919.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90331.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90332.1; -; Genomic_DNA.
DR   EMBL; AY085483; AAM62709.1; -; mRNA.
DR   EMBL; AK227978; BAE99944.1; -; mRNA.
DR   EMBL; AK317421; BAH20089.1; -; mRNA.
DR   PIR; T48158; T48158.
DR   RefSeq; NP_001318450.1; NM_001342585.1.
DR   RefSeq; NP_568089.1; NM_120214.4. [Q8LED3-1]
DR   UniGene; At.33899; -.
DR   STRING; 3702.AT5G01360.1; -.
DR   PaxDb; Q8LED3; -.
DR   PRIDE; Q8LED3; -.
DR   EnsemblPlants; AT5G01360.1; AT5G01360.1; AT5G01360. [Q8LED3-1]
DR   GeneID; 830298; -.
DR   Gramene; AT5G01360.1; AT5G01360.1; AT5G01360.
DR   KEGG; ath:AT5G01360; -.
DR   Araport; AT5G01360; -.
DR   TAIR; locus:2179172; AT5G01360.
DR   eggNOG; ENOG410IGVB; Eukaryota.
DR   eggNOG; ENOG410YCFN; LUCA.
DR   HOGENOM; HOG000238066; -.
DR   InParanoid; Q8LED3; -.
DR   OMA; TDCIHWC; -.
DR   OrthoDB; EOG09360F6Z; -.
DR   PhylomeDB; Q8LED3; -.
DR   PRO; PR:Q8LED3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q8LED3; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:1990538; F:xylan O-acetyltransferase activity; IMP:TAIR.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR   GO; GO:0045489; P:pectin biosynthetic process; IMP:TAIR.
DR   GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR   GO; GO:0045492; P:xylan biosynthetic process; IMP:TAIR.
DR   InterPro; IPR026057; PC-Esterase.
DR   InterPro; IPR025846; PMR5_N_dom.
DR   InterPro; IPR029962; TBL.
DR   InterPro; IPR029972; TBL3.
DR   PANTHER; PTHR32285; PTHR32285; 1.
DR   PANTHER; PTHR32285:SF110; PTHR32285:SF110; 1.
DR   Pfam; PF13839; PC-Esterase; 1.
DR   Pfam; PF14416; PMR5N; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q8LED3.
DR   SWISS-2DPAGE; Q8LED3.
KW   Alternative splicing; Complete proteome; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    434       Protein trichome birefringence-like 3.
FT                                /FTId=PRO_0000425369.
FT   TRANSMEM     15     35       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   MOTIF       166    168       GDS motif.
FT   MOTIF       413    427       DCXHWCLPGXXDXWN motif.
FT   COMPBIAS     39     64       Ser-rich.
FT   VAR_SEQ     325    434       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:19423640}.
FT                                /FTId=VSP_053686.
FT   CONFLICT    276    276       G -> E (in Ref. 4; BAE99944).
FT                                {ECO:0000305}.
SQ   SEQUENCE   434 AA;  49829 MW;  7C69D66539E5EBD2 CRC64;
     MSFLIPNRGV GGTKIPLSII VLVLCGFMFF ILLYTERISL LSSSSSSSSS FFKLKSCPRK
     DVSSKPKEKI RKERSEILEV LDDRFEFDPE ECNVAAGKWV YNSSIEPLYT DRSCPYIDRQ
     FSCMKNGQPE TDYLRWEWQP DDCTIPRFSP KLAMNKLRGK RLLFVGDSLQ RSQWESFVCL
     VESIIPEGEK SMKRSQKYFV FKAKEYNATI EFYWAPYIVE SNTDIPVISD PKKRIVKVDS
     VKDRAKFWEG ADILVFNTYV WWMSGLRMKA LWGSFGNGES GAEALDTQVA YRLGLKTWAN
     WVDSTVDPNK TRVFFTTMSP THTRSADWGK PNGTKCFNET KPIKDKKFWG TGSNKQMMKV
     VSSVIKHMTT HVTVINITQL SEYRIDAHTS VYTETGGKIL TAEQRADPMH HADCIHWCLP
     GLPDTWNRIL LAHL
//

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