TBL31_ARATH
ID TBL31_ARATH Reviewed; 413 AA.
AC Q1PFD9; A0MEG1; Q9CAT0; Q9SSL4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protein trichome birefringence-like 31;
GN Name=TBL31; OrderedLocusNames=At1g73140; ORFNames=F3N23.34;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABK28465.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008017; AAD55661.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010556; AAG52129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35418.1; -; Genomic_DNA.
DR EMBL; DQ446424; ABE65767.1; -; mRNA.
DR EMBL; DQ652931; ABK28465.1; ALT_SEQ; mRNA.
DR PIR; C96757; C96757.
DR RefSeq; NP_177457.2; NM_105972.4.
DR AlphaFoldDB; Q1PFD9; -.
DR SMR; Q1PFD9; -.
DR STRING; 3702.AT1G73140.1; -.
DR PaxDb; Q1PFD9; -.
DR PRIDE; Q1PFD9; -.
DR ProteomicsDB; 233016; -.
DR EnsemblPlants; AT1G73140.1; AT1G73140.1; AT1G73140.
DR GeneID; 843645; -.
DR Gramene; AT1G73140.1; AT1G73140.1; AT1G73140.
DR KEGG; ath:AT1G73140; -.
DR Araport; AT1G73140; -.
DR TAIR; locus:2032677; AT1G73140.
DR eggNOG; ENOG502QV20; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q1PFD9; -.
DR OMA; GPYWGTG; -.
DR OrthoDB; 873227at2759; -.
DR PhylomeDB; Q1PFD9; -.
DR PRO; PR:Q1PFD9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1PFD9; baseline and differential.
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 Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..413
FT /note="Protein trichome birefringence-like 31"
FT /id="PRO_0000425396"
FT TRANSMEM 12..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 141..143
FT /note="GDS motif"
FT MOTIF 384..398
FT /note="DCXHWCLPGXXDXWN motif"
SQ SEQUENCE 413 AA; 48589 MW; 69B74565D7C9FD2E CRC64;
MSIQTTADSR MIQSIFQVVL VSLLVLGSVR WILDELKSKE SRISKLYGFR QKEAVFVTKE
DQLDESCNVF EGQWVWDNVS YPLYTEKSCP YLVKQTTCQR NGRPDSYYQN WRWKPSSCDL
PRFNALKLLD VLRNKRLMFI GDSVQRSTFE SMVCMVQSVI PEKKKSFHRI PPMKIFKAEE
YNASIEYYWA PFIVESISDH ATNHTVHKRL VKLDAIEKHS KSWEGVDVLV FESYVWWMHQ
PKINATYGDT SEVREYNVTT AYKMALETWA KWFKTKINSE KQKVFFTSMS PTHLWSWEWN
PGSDGTCYDE LYPIDKRSYW GTGSNQEIMK IVGDVLSRVG ENVTFLNITQ LSEYRKDGHT
TVYGERRGKL LTKEQRADPK NYGDCIHWCL PGVPDTWNEI LYAYLLRSHR NFF
