TBL20_ARATH
ID TBL20_ARATH Reviewed; 478 AA.
AC Q9M896;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein trichome birefringence-like 20;
GN Name=TBL20; OrderedLocusNames=At3g02440; ORFNames=F16B3.7;
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] OF 25-478.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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=AAF32451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021640; AAF32451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73808.2; -; Genomic_DNA.
DR EMBL; BX822813; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001319451.1; NM_001337407.1.
DR AlphaFoldDB; Q9M896; -.
DR SMR; Q9M896; -.
DR STRING; 3702.AT3G02440.1; -.
DR PaxDb; Q9M896; -.
DR PRIDE; Q9M896; -.
DR ProteomicsDB; 234141; -.
DR EnsemblPlants; AT3G02440.1; AT3G02440.1; AT3G02440.
DR GeneID; 821154; -.
DR Gramene; AT3G02440.1; AT3G02440.1; AT3G02440.
DR KEGG; ath:AT3G02440; -.
DR Araport; AT3G02440; -.
DR TAIR; locus:2076909; AT3G02440.
DR eggNOG; ENOG502QR7B; Eukaryota.
DR HOGENOM; CLU_020953_6_5_1; -.
DR InParanoid; Q9M896; -.
DR OMA; TRCSIYY; -.
DR PRO; PR:Q9M896; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M896; baseline and differential.
DR Genevisible; Q9M896; AT.
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..478
FT /note="Protein trichome birefringence-like 20"
FT /id="PRO_0000425385"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 50..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..202
FT /note="GDS motif"
FT MOTIF 447..461
FT /note="DCXHWCLPGXXDXWN motif"
FT COMPBIAS 50..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 55845 MW; E4B0FBDB7A0B17DB CRC64;
MELPATKLRI GLVIFPLILL TIAPILYLFF GYPLYYSTST YKHLSNSSSS SAISSPSRYN
HSSSSSDSYK TEDSEPSSYD NDYDDTYHDP KSSSLHNNDR LSISSSNGHH QVTPKKEHRR
KKRKRKCDIF SGEWIPNPKA PYYTNTTCRA IHEHQNCIKY GRPDLGFMKW RWKPKECDLP
LFDPYEFLEI VRGTRMAFVG DSVSRNHVQS LICLLSRVEH PEGDSQQEFN FQRWKYKTYN
FTIATFWTTH LVRAEETETG PTGPNSFYNL YLDEPDPTWA SQIGEFDYII ISSGQWFFRP
LFLFDKQKRI GCLYCYIPGV RNVGAHFAYR RALRTTFKTI LGLENFKGEV FLRTFAPSHF
EGGEWDKGGN CLKTRPYRSN ETELDGMNLE THSIQLDEFR IANRDKNRND GLNLRLLDVT
QMMLLRPDGH PSRFGHKRED KVILYNDCVH WCLPGPIDSW NDFLLDMLKN RDLKRLKY
