ID   TBL30_ARATH             Reviewed;         427 AA.
AC   Q9SEZ9; F4IGZ7; Q9XEE7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protein trichome birefringence-like 30;
GN   Name=TBL30; OrderedLocusNames=At2g40160; ORFNames=T7M7.25, T7M7.4;
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 [GENOMIC DNA].
RX   PubMed=10207155;
RA   Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT   "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL   Genome Res. 9:325-333(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
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   [4]
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., 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   [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., 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   [7]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SEZ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SEZ9-2; Sequence=VSP_053693;
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=AAD25931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF085279; AAD25931.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09790.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09791.1; -; Genomic_DNA.
DR   EMBL; AY056791; AAL10482.1; -; mRNA.
DR   EMBL; AY113175; AAM47478.1; -; mRNA.
DR   PIR; A84826; A84826.
DR   RefSeq; NP_001189720.1; NM_001202791.1. [Q9SEZ9-2]
DR   RefSeq; NP_565924.1; NM_129574.2. [Q9SEZ9-1]
DR   AlphaFoldDB; Q9SEZ9; -.
DR   SMR; Q9SEZ9; -.
DR   BioGRID; 3945; 1.
DR   IntAct; Q9SEZ9; 2.
DR   STRING; 3702.AT2G40160.2; -.
DR   PaxDb; Q9SEZ9; -.
DR   PRIDE; Q9SEZ9; -.
DR   ProteomicsDB; 234145; -. [Q9SEZ9-1]
DR   EnsemblPlants; AT2G40160.1; AT2G40160.1; AT2G40160. [Q9SEZ9-1]
DR   EnsemblPlants; AT2G40160.2; AT2G40160.2; AT2G40160. [Q9SEZ9-2]
DR   GeneID; 818607; -.
DR   Gramene; AT2G40160.1; AT2G40160.1; AT2G40160. [Q9SEZ9-1]
DR   Gramene; AT2G40160.2; AT2G40160.2; AT2G40160. [Q9SEZ9-2]
DR   KEGG; ath:AT2G40160; -.
DR   Araport; AT2G40160; -.
DR   TAIR; locus:2065051; AT2G40160.
DR   eggNOG; ENOG502QUBK; Eukaryota.
DR   HOGENOM; CLU_020953_3_1_1; -.
DR   OMA; VGDSIHY; -.
DR   OrthoDB; 634445at2759; -.
DR   PhylomeDB; Q9SEZ9; -.
DR   PRO; PR:Q9SEZ9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SEZ9; baseline and differential.
DR   Genevisible; Q9SEZ9; 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   Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..427
FT                   /note="Protein trichome birefringence-like 30"
FT                   /id="PRO_0000425395"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           151..153
FT                   /note="GDS motif"
FT   MOTIF           402..416
FT                   /note="DCXHWCLPGXXDXWN motif"
FT   VAR_SEQ         422..427
FT                   /note="YIIYKI -> FLLHRERQKVTGRDERATAK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053693"
SQ   SEQUENCE   427 AA;  50013 MW;  7B3F36FFAB4BDA96 CRC64;
     MKQTDGRERK AYLSLLYFAV ILLPVFLLGC YLYNEKQLRV GQFQEFNTHN LQEHITPLQQ
     SKEDKDKKTD LVPLEFCDVF TGKWVLDNVT HPLYKEDECE FLSEWVACTR NGRPDSKYQK
     WRWQPQDCSL PRFDSKLLLE KLRGKKLMFI GDSIHYNQWQ SMVCMVQSVI PSGKKTLKHT
     AQMSIFNIEE YNATISFYWA PFLVESNADP PDKRDGKTDP VIIPNSISKH GENWKDADYL
     IFNTYIWWTR HSTIKVLKQE SFNKGDSKEY NEIGIYIVYK QVLSTWTKWL EQNINPSQTS
     IFFSSMSPTH IRSSDWGFNE GSKCEKETEP ILNMSKPINV GTNRRLYEIA LNATKSTKVP
     IHFLNITTMS EYRKDGHTSF YGSINGKLMT PEQKLDPRTF ADCYHWCLPG LPDSWNELLS
     LYIIYKI