TTL1_ARATH
ID TTL1_ARATH Reviewed; 699 AA.
AC Q9MAH1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=TPR repeat-containing thioredoxin TTL1;
DE AltName: Full=Tetratricopeptide repeat thioredoxin-like 1;
GN Name=TTL1; OrderedLocusNames=At1g53300; ORFNames=F12M16.20;
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 FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, 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 responses to osmotic stress and abscisic acid
CC (ABA). May act as a positive regulator of ABA signaling during
CC germination and seedling development under stress.
CC {ECO:0000269|PubMed:16998088, ECO:0000269|PubMed:22232384}.
CC -!- TISSUE SPECIFICITY: Expressed in the root elongation zone, stele, root
CC cap, embryo vascular system, leaf axilar buds, silique abscission zone
CC and guard cells. {ECO:0000269|PubMed:16998088,
CC ECO:0000269|PubMed:22232384}.
CC -!- INDUCTION: By salt and ABA treatments. {ECO:0000269|PubMed:16998088,
CC ECO:0000269|PubMed:22232384}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings show reduced root elongation under
CC salt stress and increased germination rates under osmotic stress and
CC exogenous ABA treatments. {ECO:0000269|PubMed:16998088,
CC ECO:0000269|PubMed:22232384}.
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DR EMBL; AC008007; AAF69536.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32920.1; -; Genomic_DNA.
DR EMBL; BT006444; AAP21252.1; -; mRNA.
DR RefSeq; NP_175737.1; NM_104208.3.
DR AlphaFoldDB; Q9MAH1; -.
DR SMR; Q9MAH1; -.
DR STRING; 3702.AT1G53300.1; -.
DR iPTMnet; Q9MAH1; -.
DR PaxDb; Q9MAH1; -.
DR PRIDE; Q9MAH1; -.
DR ProteomicsDB; 232365; -.
DR EnsemblPlants; AT1G53300.1; AT1G53300.1; AT1G53300.
DR GeneID; 841764; -.
DR Gramene; AT1G53300.1; AT1G53300.1; AT1G53300.
DR KEGG; ath:AT1G53300; -.
DR Araport; AT1G53300; -.
DR TAIR; locus:2009590; AT1G53300.
DR eggNOG; KOG0907; Eukaryota.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_015299_0_0_1; -.
DR InParanoid; Q9MAH1; -.
DR OMA; NSKMERW; -.
DR OrthoDB; 506649at2759; -.
DR PhylomeDB; Q9MAH1; -.
DR PRO; PR:Q9MAH1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAH1; baseline and differential.
DR Genevisible; Q9MAH1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR044534; TTL1-4.
DR PANTHER; PTHR46050; PTHR46050; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Phosphoprotein; Reference proteome;
KW Repeat; Stress response; TPR repeat.
FT CHAIN 1..699
FT /note="TPR repeat-containing thioredoxin TTL1"
FT /id="PRO_0000394549"
FT REPEAT 227..260
FT /note="TPR 1"
FT REPEAT 262..294
FT /note="TPR 2"
FT REPEAT 296..328
FT /note="TPR 3"
FT REPEAT 419..452
FT /note="TPR 4"
FT REPEAT 465..498
FT /note="TPR 5"
FT REPEAT 499..532
FT /note="TPR 6"
FT REPEAT 534..566
FT /note="TPR 7"
FT DOMAIN 605..691
FT /note="Thioredoxin"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SIN1"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 699 AA; 76115 MW; 3B329FCF6DDA4693 CRC64;
MPKSVKPISE SDKLSDHLRD SSLTSEINKP DFRELDLGSP VSPLRSQPRG LTTTTTTTTT
SSSSSSSSGS VTGRIKHAPV IGRSNSVRSQ SNSSSGNNNL RPRSDSATTS SSSHSQPLLS
SSSSSATSPA PTSPANVLPT GNICPSGKIQ ITGMTQSRSR SDVLGSGTGT YGHGSIMRGG
GISPAKPTNT GGGSNSPVNV GSSSRSSSTV ATGETPIWKK AILGSDSEEV KRVGNEMYRK
GLFNEALKLY DRAIALSPTN AAYRSNRAAA LIGLSRIGEA VKECEDAVRS DPNYGRAHHR
LALLLIRLGQ VNSARKHLCF LGRPSDPMEL QKLEAVEKHL IKCVDARRVT DWKTVLIEAD
AAIVSGADFS PQLFMCKVEA FLKLHRLDDA QSKLLEVPKV EPFPVSCSQT RFSGMACEAY
IYFVKAQIEM ALGRFENAVM AAEKASQIDP RCNEVAMLHN TVTLVARARA RGNDLYKSER
YTEASSAYAE GLRLDPCNAI LYCNRAACWF KLGMWERSIE DCNQALRYQP SYTKPLLRRA
ASNSKMERWG AAVSDYEALI RELPHDKEVA ESLFHAQVAL KKSRGEEVLN MEFGGEVEEI
YSLEQFKSAM NLPGVSVIHF STASDHQCKQ ISPFVDSLCT RYPSIHFLKV DIDKCPSIGN
AENVRVVPTV KIYKNGSRVK EIVCPSKEVL EYSVRHYSG
