(data stored in ACNUC13479 zone)

SWISSPROT: 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   30-AUG-2017, entry version 88.
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; 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).
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
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   [7]
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: May be involved in the specific O-acetylation of cell
CC       wall polymers. {ECO:0000250, ECO:0000269|PubMed:20657172}.
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         Note=No experimental confirmation available. Derived from EST
CC         data.;
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=CAB82278.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   UniGene; At.33531; -.
DR   STRING; 3702.AT5G01620.3; -.
DR   iPTMnet; Q8RXQ1; -.
DR   PaxDb; Q8RXQ1; -.
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.
DR   Gramene; AT5G01620.2; AT5G01620.2; AT5G01620.
DR   Gramene; AT5G01620.3; AT5G01620.3; AT5G01620.
DR   KEGG; ath:AT5G01620; -.
DR   Araport; AT5G01620; -.
DR   TAIR; locus:2149785; AT5G01620.
DR   eggNOG; ENOG410IVJS; Eukaryota.
DR   eggNOG; ENOG410YG4N; LUCA.
DR   HOGENOM; HOG000238066; -.
DR   OMA; IEFLWAP; -.
DR   OrthoDB; EOG09360ACH; -.
DR   PhylomeDB; Q8RXQ1; -.
DR   PRO; PR:Q8RXQ1; -.
DR   Proteomes; UP000006548; Chromosome 5.
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: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; IPR025846; PMR5_N_dom.
DR   InterPro; IPR029962; TBL.
DR   PANTHER; PTHR32285; PTHR32285; 1.
DR   Pfam; PF13839; PC-Esterase; 1.
DR   Pfam; PF14416; PMR5N; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q8RXQ1.
DR   SWISS-2DPAGE; Q8RXQ1.
KW   Alternative splicing; Complete proteome; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    449       Protein trichome birefringence-like 35.
FT                                /FTId=PRO_0000425400.
FT   TRANSMEM     12     29       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   MOTIF       185    187       GDS motif.
FT   MOTIF       428    442       DCXHWCLPGXXDXWN motif.
FT   VAR_SEQ      70     70       H -> HGFCFEKNA (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_053694.
FT   CONFLICT     74     74       D -> G (in Ref. 4; AAM61008).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       W -> C (in Ref. 4; AAM61008).
FT                                {ECO:0000305}.
FT   CONFLICT    169    169       A -> V (in Ref. 4; AAM61008).
FT                                {ECO:0000305}.
FT   CONFLICT    191    191       G -> S (in Ref. 4; AAM61008).
FT                                {ECO:0000305}.
FT   CONFLICT    201    201       Q -> R (in Ref. 4; AAM61008).
FT                                {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
//

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