ID   TBL28_ARATH             Reviewed;         424 AA.
AC   Q94K00; Q9XEE7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protein trichome birefringence-like 28;
GN   Name=TBL28; OrderedLocusNames=At2g40150; ORFNames=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].
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   -!- 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; AEC09789.1; -; Genomic_DNA.
DR   EMBL; AF370500; AAK43877.1; -; mRNA.
DR   EMBL; BT003422; AAO30085.1; -; mRNA.
DR   PIR; H84825; H84825.
DR   RefSeq; NP_030560.1; NM_129573.2.
DR   AlphaFoldDB; Q94K00; -.
DR   SMR; Q94K00; -.
DR   STRING; 3702.AT2G40150.1; -.
DR   PaxDb; Q94K00; -.
DR   PRIDE; Q94K00; -.
DR   ProteomicsDB; 246454; -.
DR   EnsemblPlants; AT2G40150.1; AT2G40150.1; AT2G40150.
DR   GeneID; 818606; -.
DR   Gramene; AT2G40150.1; AT2G40150.1; AT2G40150.
DR   KEGG; ath:AT2G40150; -.
DR   Araport; AT2G40150; -.
DR   TAIR; locus:2065069; AT2G40150.
DR   eggNOG; ENOG502QUBK; Eukaryota.
DR   HOGENOM; CLU_020953_3_1_1; -.
DR   InParanoid; Q94K00; -.
DR   OMA; METQPIV; -.
DR   OrthoDB; 492414at2759; -.
DR   PhylomeDB; Q94K00; -.
DR   PRO; PR:Q94K00; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q94K00; baseline and differential.
DR   Genevisible; Q94K00; 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..424
FT                   /note="Protein trichome birefringence-like 28"
FT                   /id="PRO_0000425393"
FT   TRANSMEM        23..43
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           145..147
FT                   /note="GDS motif"
FT   MOTIF           399..413
FT                   /note="DCXHWCLPGXXDXWN motif"
SQ   SEQUENCE   424 AA;  49404 MW;  B5214F6DA2A7F780 CRC64;
     MQPSRTRVSF FETGETMKQR KKSYLSIFVI FFSLFFFGIF MYNDNLKSSI ADFTSSNPFS
     SSFVELPPDE CDLFTGQWVF DNKTYPLYKE EECEFLTEQV TCLRNGRKDS LFQNWRWQPR
     DCSLPKFNAR VLLEKLRNKR LMFVGDSLNR NQWESMVCLV QSVIPPGRKS LNQTGSLTVF
     KIQDYNATVE FYWAPFLVES NSDDPEKHSI IDRIIMPESI EKHGVNWIGV DFLVFNSYIW
     WMNTVSIKVL RGSFDDGDTE YDEIKRPIAY ERVLRTLGDW VDHNIDPLST TVFFMSMSPL
     HIKSSDWANP EGIRCALETT PILNMSFNVA YGQFSAVGTD YRLFPVAENV TQSLKVPIHF
     LNITALSEYR KDAHTSVYTI KQGKLLTREQ QNDPANFADC IHWCLPGLPD TWNEFLYTHI
     ISRR