TBL16_ARATH
ID TBL16_ARATH Reviewed; 551 AA.
AC F4K5L5; A8MQ97; B9DFA9; Q93ZW1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein trichome birefringence-like 16;
GN Name=TBL16; OrderedLocusNames=At5g20680; ORFNames=T1M15.80;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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=F4K5L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K5L5-2; Sequence=VSP_053692;
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; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92875.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92876.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92877.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70443.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70444.1; -; Genomic_DNA.
DR EMBL; AY056231; AAL07080.1; -; mRNA.
DR EMBL; AK316699; BAH19426.1; -; mRNA.
DR RefSeq; NP_001078609.1; NM_001085140.2. [F4K5L5-2]
DR RefSeq; NP_001154728.1; NM_001161256.2. [F4K5L5-1]
DR RefSeq; NP_001332053.1; NM_001343680.1. [F4K5L5-1]
DR RefSeq; NP_001332054.1; NM_001343681.1. [F4K5L5-1]
DR RefSeq; NP_568398.1; NM_122075.2. [F4K5L5-1]
DR AlphaFoldDB; F4K5L5; -.
DR SMR; F4K5L5; -.
DR STRING; 3702.AT5G20680.1; -.
DR PaxDb; F4K5L5; -.
DR PRIDE; F4K5L5; -.
DR ProteomicsDB; 232987; -. [F4K5L5-1]
DR EnsemblPlants; AT5G20680.1; AT5G20680.1; AT5G20680. [F4K5L5-1]
DR EnsemblPlants; AT5G20680.2; AT5G20680.2; AT5G20680. [F4K5L5-2]
DR EnsemblPlants; AT5G20680.3; AT5G20680.3; AT5G20680. [F4K5L5-1]
DR EnsemblPlants; AT5G20680.4; AT5G20680.4; AT5G20680. [F4K5L5-1]
DR EnsemblPlants; AT5G20680.5; AT5G20680.5; AT5G20680. [F4K5L5-1]
DR GeneID; 832191; -.
DR Gramene; AT5G20680.1; AT5G20680.1; AT5G20680. [F4K5L5-1]
DR Gramene; AT5G20680.2; AT5G20680.2; AT5G20680. [F4K5L5-2]
DR Gramene; AT5G20680.3; AT5G20680.3; AT5G20680. [F4K5L5-1]
DR Gramene; AT5G20680.4; AT5G20680.4; AT5G20680. [F4K5L5-1]
DR Gramene; AT5G20680.5; AT5G20680.5; AT5G20680. [F4K5L5-1]
DR KEGG; ath:AT5G20680; -.
DR Araport; AT5G20680; -.
DR TAIR; locus:2180399; AT5G20680.
DR eggNOG; ENOG502QRJ5; Eukaryota.
DR InParanoid; F4K5L5; -.
DR PRO; PR:F4K5L5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K5L5; baseline and differential.
DR Genevisible; F4K5L5; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR029969; TBL16.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 2.
DR PANTHER; PTHR32285:SF278; PTHR32285:SF278; 2.
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..551
FT /note="Protein trichome birefringence-like 16"
FT /id="PRO_0000425382"
FT TRANSMEM 31..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 77..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..288
FT /note="GDS motif"
FT MOTIF 530..544
FT /note="DCXHWCLPGXXDXWN motif"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053692"
FT CONFLICT 95
FT /note="N -> S (in Ref. 4; BAH19426)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> S (in Ref. 3; AAL07080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 62316 MW; 7F2362467F599C36 CRC64;
MNETFSATPR SMTIHRYRMK RGALRRRARD ISVMLVVLVC ATVVIWTWDR TPTSAFLPPE
SHYLKLQSEE KVEKLPTALN TETKDSYSSA IPFVNKEESK EDSSDNKDTE EEEEKQVEEV
TVSNTNRGKI PTIEEKKGEH EVIASEPKYR KTPTREDFKL EKVKHEVAVG EGEATETTHI
KETNSDPKSN ILATDEERTD GTSTARITNQ ACNYAKGKWV VDNHRPLYSG SQCKQWLASM
WACRLMQRTD FAFESLRWQP KDCSMEEFEG SKFLRRMKNK TLAFVGDSLG RQQFQSMMCM
ISGGKERLDV LDVGPEFGFI TPEGGARPGG WAYRFPETNT TVLYHWSSTL CDIEPLNITD
PATEHAMHLD RPPAFLRQYL QKIDVLVMNT GHHWNRGKLN GNKWVMHVNG VPNTNRKLAA
LGNAKNFTIH STVSWVNSQL PLHPGLKAFY RSLSPRHFVG GEWNTGGSCN NTTPMSIGKE
VLQEESSDYS AGRAVKGTGV KLLDITALSH IRDEGHISRF SISASRGVQD CLHWCLPGVP
DTWNEILFAM I
