TBL32_ARATH
ID TBL32_ARATH Reviewed; 451 AA.
AC Q9SRL3;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein trichome birefringence-like 32 {ECO:0000303|PubMed:20388664};
GN Name=TBL32 {ECO:0000303|PubMed:20388664};
GN OrderedLocusNames=At3g11030 {ECO:0000312|Araport:AT3G11030};
GN ORFNames=F9F8.15 {ECO:0000312|EMBL:AAF01518.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26745802; DOI=10.1371/journal.pone.0146460;
RA Yuan Y., Teng Q., Zhong R., Haghighat M., Richardson E.A., Ye Z.H.;
RT "Mutations of Arabidopsis TBL32 and TBL33 affect xylan acetylation and
RT secondary wall deposition.";
RL PLoS ONE 11:e0146460-e0146460(2016).
CC -!- FUNCTION: Probable xylan acetyltransferase that plays a role in xylan
CC acetylation and normal deposition of secondary cell walls
CC (PubMed:26745802). Required for 2-O-monoacetylation, 3-O-
CC monoacetylation and 2,3-O-diacetylation of xylosyl residues in xylan
CC (PubMed:26745802). Required for the formation of 3-O-acetylated, 2-O-
CC glucoronic acid-substituted xylosyl residues (PubMed:26745802). May act
CC as a bridging protein that binds pectin and other cell wall
CC polysaccharides. Probably involved in maintaining esterification of
CC pectins (By similarity). {ECO:0000250|UniProtKB:Q9FG35,
CC ECO:0000269|PubMed:26745802}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:26745802}; Single-pass type II membrane protein
CC {ECO:0000255}.
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; AC009991; AAF01518.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74995.1; -; Genomic_DNA.
DR EMBL; BT002911; AAO22727.1; -; mRNA.
DR EMBL; BT004460; AAO42454.1; -; mRNA.
DR RefSeq; NP_187714.1; NM_111940.3.
DR AlphaFoldDB; Q9SRL3; -.
DR SMR; Q9SRL3; -.
DR BioGRID; 5608; 6.
DR IntAct; Q9SRL3; 2.
DR STRING; 3702.AT3G11030.1; -.
DR PaxDb; Q9SRL3; -.
DR PRIDE; Q9SRL3; -.
DR ProteomicsDB; 234146; -.
DR EnsemblPlants; AT3G11030.1; AT3G11030.1; AT3G11030.
DR GeneID; 820274; -.
DR Gramene; AT3G11030.1; AT3G11030.1; AT3G11030.
DR KEGG; ath:AT3G11030; -.
DR Araport; AT3G11030; -.
DR TAIR; locus:2085512; AT3G11030.
DR eggNOG; ENOG502QTQP; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q9SRL3; -.
DR OMA; RSKDWGD; -.
DR OrthoDB; 635575at2759; -.
DR PhylomeDB; Q9SRL3; -.
DR PRO; PR:Q9SRL3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRL3; baseline and differential.
DR Genevisible; Q9SRL3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA: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:0009834; P:plant-type secondary cell wall biogenesis; IGI:TAIR.
DR GO; GO:1990937; P:xylan acetylation; IMP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR029988; TBL32/TBL46.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF193; PTHR32285:SF193; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..451
FT /note="Protein trichome birefringence-like 32"
FT /id="PRO_0000425397"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..451
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 62..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 180..182
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:20657172"
FT MOTIF 427..441
FT /note="DCXHWCLPGXXDXWN motif"
FT /evidence="ECO:0000305|PubMed:20657172"
FT COMPBIAS 62..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 51708 MW; 8B63062C3EF8752F CRC64;
MTTALFSPSN RRKRRLTHFF FTVLAFILLA AFIYGHDFIS FSRRSLHSPT IVHQSAIVVV
VDEPPPPPPT SPPPPSPPPP SPPPPSPPPP SPPPPAFAVG KTPEGCDVFK GNWVKDWSTR
PLYRESECPY IQPQLTCRTH GRPDSDYQSW RWRPDSCSLP SFNATVMLES LRGKKMMFVG
DSLNRGMYVS LICLLHSQIP ENSKSMDTFG SLTVFSLKDY NATIEFYWAP FLLESNSDNA
TVHRVSDRIV RKGSINKHGR HWRGADIVVF NTYLWWRTGF KMKILEGSFK DEKKRIVEME
SEDAYRMALK TMVKWVKKNM DPLKTRVFFA TMSPTHYKGE DWGGEQGKNC YNQTTPIQDM
NHWPSDCSKT LMKVIGEELD QRAEFPVTVL NITQLSGYRK DAHTSIYKKQ WSPLTKEQLA
NPASYSDCIH WCLPGLQDTW NELFFAKLFY P
