TBL38_ARATH
ID TBL38_ARATH Reviewed; 380 AA.
AC Q8VY22; Q9LP35;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein trichome birefringence-like 38;
GN Name=TBL38; OrderedLocusNames=At1g29050; ORFNames=F28N24.24;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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=AAF88130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021043; AAF88130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31037.1; -; Genomic_DNA.
DR EMBL; AY074272; AAL66969.1; -; mRNA.
DR EMBL; AY096662; AAM20296.1; -; mRNA.
DR EMBL; AK227259; BAE99289.1; -; mRNA.
DR PIR; G86412; G86412.
DR RefSeq; NP_564318.1; NM_102646.5.
DR AlphaFoldDB; Q8VY22; -.
DR SMR; Q8VY22; -.
DR STRING; 3702.AT1G29050.1; -.
DR PaxDb; Q8VY22; -.
DR PRIDE; Q8VY22; -.
DR ProteomicsDB; 234162; -.
DR EnsemblPlants; AT1G29050.1; AT1G29050.1; AT1G29050.
DR GeneID; 839779; -.
DR Gramene; AT1G29050.1; AT1G29050.1; AT1G29050.
DR KEGG; ath:AT1G29050; -.
DR Araport; AT1G29050; -.
DR TAIR; locus:2029959; AT1G29050.
DR eggNOG; ENOG502QQWH; Eukaryota.
DR HOGENOM; CLU_020953_3_0_1; -.
DR InParanoid; Q8VY22; -.
DR OMA; RWSGKKI; -.
DR OrthoDB; 664606at2759; -.
DR PhylomeDB; Q8VY22; -.
DR PRO; PR:Q8VY22; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VY22; baseline and differential.
DR Genevisible; Q8VY22; 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; 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..380
FT /note="Protein trichome birefringence-like 38"
FT /id="PRO_0000425403"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 134..136
FT /note="GDS motif"
FT MOTIF 357..371
FT /note="DCXHWCLPGXXDXWN motif"
SQ SEQUENCE 380 AA; 42709 MW; F6B295CACB7F3B8C CRC64;
MGFKLISLLL LFLPLLTVTI LSGVEQAFAS DKALLVTGRN ITADGGRSSL RGKKQRRASG
CNLFQGRWVF DASYPFYDSS KCPFIDGEFD CLKFGRPDKQ FLKYSWQPES CTIPRFDGGA
FLRKYRGKRV MFVGDSLSLN MWESLACMIH ASVPNAKTTF LKRTPLSTLT FQEYGVTLYL
YRTPYIVDIS KERVGRVLNL GAIEGGADAW KNMDVLVFNS WHWWTHKGQS QGWDYIRDGS
SLVRDMNRLD AFYKGLSTWA RWVDQNVDTA KTRVFFQGIS PTHYEGREWN EPRKTCSGQM
QPLGGSSYPS GQPPSSGVVS KVLSSMKKPV TLLDITTLSQ LRKDAHPSSY GGDGGTDCSH
WCLPGLPDTW NQLLYAALTM
