ID   TBL37_ARATH             Reviewed;         385 AA.
AC   O22960;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protein trichome birefringence-like 37;
GN   Name=TBL37; OrderedLocusNames=At2g34070; ORFNames=T14G11.19;
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=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   [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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AC002341; AAB67625.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08913.1; -; Genomic_DNA.
DR   EMBL; AY086504; AAM63505.1; -; mRNA.
DR   PIR; A84752; A84752.
DR   RefSeq; NP_565779.1; NM_128958.3.
DR   AlphaFoldDB; O22960; -.
DR   SMR; O22960; -.
DR   STRING; 3702.AT2G34070.1; -.
DR   PaxDb; O22960; -.
DR   PRIDE; O22960; -.
DR   ProteomicsDB; 234147; -.
DR   EnsemblPlants; AT2G34070.1; AT2G34070.1; AT2G34070.
DR   GeneID; 817968; -.
DR   Gramene; AT2G34070.1; AT2G34070.1; AT2G34070.
DR   KEGG; ath:AT2G34070; -.
DR   Araport; AT2G34070; -.
DR   TAIR; locus:2055425; AT2G34070.
DR   eggNOG; ENOG502QQWH; Eukaryota.
DR   HOGENOM; CLU_020953_3_0_1; -.
DR   InParanoid; O22960; -.
DR   OMA; IFDASYH; -.
DR   OrthoDB; 664606at2759; -.
DR   PhylomeDB; O22960; -.
DR   PRO; PR:O22960; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22960; baseline and differential.
DR   Genevisible; O22960; AT.
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; IMP:TAIR.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IPI:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR   InterPro; IPR026057; PC-Esterase.
DR   InterPro; IPR029962; TBL.
DR   InterPro; IPR029986; TBL37/38.
DR   InterPro; IPR025846; TBL_N.
DR   PANTHER; PTHR32285; PTHR32285; 1.
DR   PANTHER; PTHR32285:SF238; PTHR32285:SF238; 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..385
FT                   /note="Protein trichome birefringence-like 37"
FT                   /id="PRO_0000425402"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           138..140
FT                   /note="GDS motif"
FT   MOTIF           362..376
FT                   /note="DCXHWCLPGXXDXWN motif"
SQ   SEQUENCE   385 AA;  43354 MW;  D27688CF401564F5 CRC64;
     MGFKLNSLFL LLSLLILTIL SGADQALAYV KKPHVSQRNK TALAAVAGRG GGKEMLKGRK
     QTSGCNLFQG RWVFDASYPF YDSSTCPFID GEFDCLKFGR PDKQFLKYSW QPDSCTVPRF
     DGEAFLKKWR GKRVMFVGDS LSLNMWESLA CMIHSSVPNT KTTFLKRTPL SSLTFQEYDV
     TLFLYRTPYL VDISKESVGR VLNLGAIEDG ADAWKNMDLL VFNSWHWWTH TGVQSQGWDF
     IRDGSSLMRD MDRLDAFNKG LTTWGQWVDQ NVNVSQTRVF FQGISPTHYM GREWNEPRKT
     CNGQMQPLTG STYPGGSLPA ASIVSRVLST MRTPVYLLDI TTLSQLRKDA HPSTYGGDGG
     TDCSHWCLPG LPDTWNQLLY AALSM