TTL3_ARATH
ID TTL3_ARATH Reviewed; 691 AA.
AC Q9SIN1; Q9ASR6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Inactive TPR repeat-containing thioredoxin TTL3;
DE AltName: Full=Tetratricopeptide repeat thioredoxin-like 3;
DE AltName: Full=VH1-interacting TPR-containing protein;
GN Name=TTL3; Synonyms=VIT; OrderedLocusNames=At2g42580; ORFNames=F14N22.15;
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].
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 INDUCTION.
RX PubMed=12805584; DOI=10.1104/pp.103.020511;
RA Lee J.Y., Lee D.H.;
RT "Use of serial analysis of gene expression technology to reveal changes in
RT gene expression in Arabidopsis pollen undergoing cold stress.";
RL Plant Physiol. 132:517-529(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=16998088; DOI=10.1104/pp.106.085191;
RA Rosado A., Schapire A.L., Bressan R.A., Harfouche A.L., Hasegawa P.M.,
RA Valpuesta V., Botella M.A.;
RT "The Arabidopsis tetratricopeptide repeat-containing protein TTL1 is
RT required for osmotic stress responses and abscisic acid sensitivity.";
RL Plant Physiol. 142:1113-1126(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, INTERACTION WITH BRL2, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19000166; DOI=10.1111/j.1365-313x.2008.03742.x;
RA Ceserani T., Trofka A., Gandotra N., Nelson T.;
RT "VH1/BRL2 receptor-like kinase interacts with vascular-specific adaptor
RT proteins VIT and VIK to influence leaf venation.";
RL Plant J. 57:1000-1014(2009).
RN [8]
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22232384; DOI=10.1104/pp.111.188920;
RA Lakhssassi N., Doblas V.G., Rosado A., Esteban Del Valle A., Pose D.,
RA Jimenez A.J., Castillo A.G., Valpuesta V., Borsani O., Botella M.A.;
RT "The Arabidopsis thaliana TETRATRICO PEPTIDE THIOREDOXIN-LIKE gene family
RT is required for osmotic stress tolerance and male sporogenesis.";
RL Plant Physiol. 158:1252-1266(2012).
CC -!- FUNCTION: Involved in osmotic and salt stress tolerance. May play a
CC role in the control of meristematic cell size during osmotic stress.
CC May function as an adaptor protein for BRL2 and may be required for
CC signaling affecting leaf vascular tissue pattern formation.
CC {ECO:0000269|PubMed:19000166}.
CC -!- SUBUNIT: Interacts with BRL2. {ECO:0000269|PubMed:19000166}.
CC -!- INTERACTION:
CC Q9SIN1; Q9ZPS9: BRL2; NbExp=2; IntAct=EBI-2292882, EBI-2292728;
CC Q9SIN1; Q8L856: CYB561A; NbExp=2; IntAct=EBI-2292882, EBI-2295096;
CC -!- TISSUE SPECIFICITY: Expressed in embryos and organ primordia in shoot
CC and root. In primary and cauline leaves and petals, is expressed in
CC hydathodes, guard cells, petiole cells and cells associated with
CC differentiating vascular bundles. {ECO:0000269|PubMed:19000166,
CC ECO:0000269|PubMed:22232384}.
CC -!- INDUCTION: By salt treatment in cotyledons and cold stress in pollen.
CC {ECO:0000269|PubMed:12805584, ECO:0000269|PubMed:22232384}.
CC -!- DOMAIN: The thioredoxin domain is inactive.
CC {ECO:0000269|PubMed:19000166}.
CC -!- DISRUPTION PHENOTYPE: Altered vein pattern in cotyledons and primary
CC leaves. Mutant seedlings show increased sensitivity to osmotic and salt
CC stresses in roots. {ECO:0000269|PubMed:19000166,
CC ECO:0000269|PubMed:22232384}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007087; AAD22995.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10141.1; -; Genomic_DNA.
DR EMBL; AF367321; AAK32908.1; -; mRNA.
DR EMBL; AY143941; AAN28880.1; -; mRNA.
DR PIR; F84855; F84855.
DR RefSeq; NP_565976.1; NM_129819.3.
DR AlphaFoldDB; Q9SIN1; -.
DR SMR; Q9SIN1; -.
DR BioGRID; 4195; 48.
DR IntAct; Q9SIN1; 47.
DR STRING; 3702.AT2G42580.1; -.
DR iPTMnet; Q9SIN1; -.
DR PaxDb; Q9SIN1; -.
DR PRIDE; Q9SIN1; -.
DR ProteomicsDB; 232367; -.
DR EnsemblPlants; AT2G42580.1; AT2G42580.1; AT2G42580.
DR GeneID; 818858; -.
DR Gramene; AT2G42580.1; AT2G42580.1; AT2G42580.
DR KEGG; ath:AT2G42580; -.
DR Araport; AT2G42580; -.
DR TAIR; locus:2041559; AT2G42580.
DR eggNOG; KOG0907; Eukaryota.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_015299_0_0_1; -.
DR InParanoid; Q9SIN1; -.
DR OMA; PFINMLC; -.
DR OrthoDB; 506649at2759; -.
DR PhylomeDB; Q9SIN1; -.
DR PRO; PR:Q9SIN1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIN1; baseline and differential.
DR Genevisible; Q9SIN1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR044534; TTL1-4.
DR PANTHER; PTHR46050; PTHR46050; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; Stress response; TPR repeat.
FT CHAIN 1..691
FT /note="Inactive TPR repeat-containing thioredoxin TTL3"
FT /id="PRO_0000415944"
FT REPEAT 220..253
FT /note="TPR 1"
FT REPEAT 255..287
FT /note="TPR 2"
FT REPEAT 289..321
FT /note="TPR 3"
FT REPEAT 412..445
FT /note="TPR 4"
FT REPEAT 458..491
FT /note="TPR 5"
FT REPEAT 492..525
FT /note="TPR 6"
FT REPEAT 527..559
FT /note="TPR 7"
FT DOMAIN 596..683
FT /note="Thioredoxin"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9MAH1"
SQ SEQUENCE 691 AA; 75461 MW; A8F8F6090DBB6E19 CRC64;
MSHSRRLSLE PAIDSITGRF RDLQRNDDDV NKPDFRELDL GSPVSTLMPR GSASSSAAAT
PTSSSGSSGS ASGKPSVSSQ MAKRLDDAYK SHSGELSSPG SGMPTTTRIL KPGHRRSSST
GTPLIFSGSS FTSATSHTSP QGGGSGATSA VSPNTGVLPA GNICPSGRIL KTGMASRTSS
RTETLCTGTG NYGHGNVVRS GGGGGTSGKA VRVAENGENP EELKRMGNDM YRRGSFSEAL
SLYDRAILIS PGNAAYRSNR AAALTALRRL GEAVKECLEA VRIDPSYSRA HQRLASLYLR
LGEAENARRH ICFSGQCPDQ ADLQRLQTLE KHLRRCWEAR KIGDWKTAIK ETDAAIANGA
DSSPQLVACK AEAFLRLKQI EDSDFCVSCI PRLDHHYHSQ PQVKLFGMVV EAYVLCIQAQ
VDMALGRFEN AVVKAERAAM LDQTNPEVVS VLNNVKMVVR ARTRGNELFS SGRFSEACVA
YGDGLKQDDS NSVLYCNRAA CWYKLGLWEK SVEDCNHALK SQPSYIKALL RRAASYGKLG
RWEDAVKDYE FLRRELPGDS EVAESLERAK TVLMNRSQES KSLGFNNEVE AVSTLDKFKK
SVALPGVSVF HFKSSSNRQC EEISPFINTL CLRYPLVHFF MVDVEESMAL AKAESIRKVP
TFKMYKNGDK VKEMVCPSHQ FLEDSIKHFL L
