TL29_ARATH
ID TL29_ARATH Reviewed; 349 AA.
AC P82281; Q7XZP6; Q9M0S6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Thylakoid lumenal 29 kDa protein, chloroplastic;
DE Short=TL29;
DE EC=1.-.-.-;
DE AltName: Full=AtAPx07;
DE AltName: Full=P29;
DE AltName: Full=Probable L-ascorbate peroxidase 4;
DE Flags: Precursor;
GN Name=TL29; Synonyms=APX4; OrderedLocusNames=At4g09010; ORFNames=F23J3.40;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [MRNA] OF 11-306.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=12068123; DOI=10.1104/pp.001362;
RA Panchuk I.I., Volkov R.A., Schoffl F.;
RT "Heat stress- and heat shock transcription factor-dependent expression and
RT activity of ascorbate peroxidase in Arabidopsis.";
RL Plant Physiol. 129:838-853(2002).
RN [5]
RP PROTEIN SEQUENCE OF 83-112, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11034343; DOI=10.1016/s0014-5793(00)01890-1;
RA Kieselbach T., Bystedt M., Hynds P., Robinson C., Schroeder W.P.;
RT "A peroxidase homologue and novel plastocyanin located by proteomics to the
RT Arabidopsis chloroplast thylakoid lumen.";
RL FEBS Lett. 480:271-276(2000).
RN [6]
RP PROTEIN SEQUENCE OF 83-112, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=16034597; DOI=10.1007/s00425-005-0028-8;
RA Panchuk I.I., Zentgraf U., Volkov R.A.;
RT "Expression of the Apx gene family during leaf senescence of Arabidopsis
RT thaliana.";
RL Planta 222:926-932(2005).
RN [8]
RP FUNCTION REVISION, AND SUBCELLULAR LOCATION.
RX PubMed=19828564; DOI=10.1093/pcp/pcp134;
RA Granlund I., Storm P., Schubert M., Garcia-Cerdan J.G., Funk C.,
RA Schroder W.P.;
RT "The TL29 protein is lumen located, associated with PSII and not an
RT ascorbate peroxidase.";
RL Plant Cell Physiol. 50:1898-1910(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- INTERACTION:
CC P82281; P0AA25: trxA; Xeno; NbExp=2; IntAct=EBI-2895799, EBI-368542;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11034343, ECO:0000269|PubMed:11719511,
CC ECO:0000269|PubMed:19828564}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during leaf senescence.
CC {ECO:0000269|PubMed:16034597}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an ascorbate peroxidase
CC (PubMed:12068123, PubMed:16034597). PubMed:19828564 fails to show any
CC peroxidase activity associated with TL29 and demonstrates that TL29
CC could bind neither heme nor ascorbate. TL29 lacks the heme-binding
CC site, the proton acceptor and the transition state stabilizer, which
CC are conserved features of the ascorbate peroxidase.
CC {ECO:0000305|PubMed:12068123, ECO:0000305|PubMed:16034597}.
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DR EMBL; AC005359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161513; CAB78025.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82711.1; -; Genomic_DNA.
DR EMBL; AF370534; AAK48961.1; -; mRNA.
DR EMBL; AY072503; AAL66918.1; -; mRNA.
DR EMBL; AF441713; AAP72143.1; -; mRNA.
DR PIR; A85091; A85091.
DR RefSeq; NP_192640.1; NM_116970.3.
DR PDB; 3RRW; X-ray; 2.50 A; A/B=83-349.
DR PDBsum; 3RRW; -.
DR AlphaFoldDB; P82281; -.
DR SMR; P82281; -.
DR BioGRID; 11779; 2.
DR IntAct; P82281; 3.
DR STRING; 3702.AT4G09010.1; -.
DR PeroxiBase; 3920; AtAPx07.
DR iPTMnet; P82281; -.
DR MetOSite; P82281; -.
DR PaxDb; P82281; -.
DR PRIDE; P82281; -.
DR ProteomicsDB; 234320; -.
DR EnsemblPlants; AT4G09010.1; AT4G09010.1; AT4G09010.
DR GeneID; 826480; -.
DR Gramene; AT4G09010.1; AT4G09010.1; AT4G09010.
DR KEGG; ath:AT4G09010; -.
DR Araport; AT4G09010; -.
DR TAIR; locus:2122333; AT4G09010.
DR eggNOG; ENOG502QR5T; Eukaryota.
DR HOGENOM; CLU_059254_0_0_1; -.
DR InParanoid; P82281; -.
DR PhylomeDB; P82281; -.
DR PRO; PR:P82281; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P82281; baseline and differential.
DR Genevisible; P82281; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002207; Peroxidase_I.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Oxidoreductase;
KW Phosphoprotein; Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..82
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11034343,
FT ECO:0000269|PubMed:11719511"
FT CHAIN 83..349
FT /note="Thylakoid lumenal 29 kDa protein, chloroplastic"
FT /id="PRO_0000023635"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 96
FT /note="S -> A (in Ref. 4; AAP72143)"
FT /evidence="ECO:0000305"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:3RRW"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:3RRW"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:3RRW"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:3RRW"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:3RRW"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3RRW"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:3RRW"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:3RRW"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:3RRW"
SQ SEQUENCE 349 AA; 37934 MW; ABD439188BDA8E61 CRC64;
MGGVSFLSTV PSFTNTTNHQ HLTTLSSSSH RSAVIRCSKI EPQVSGESLA FHRRDVLKLA
GTAVGMELIG NGFINNVGDA KAADLNQRRQ RSEFQSKIKI LLSTTIKAKP ELVPSLLKLA
LNDAMTYDKA TKSGGANGSI RFSSELSRAE NEGLSDGLSL IEEVKKEIDS ISKGGPISYA
DIIQLAGQSA VKFTYLASAI RKCGGNEEKG NLLYTAYGSA GQWGLFDRNF GRSDATEADP
EGRVPQWGKA TVQEMKDKFI AVGLGPRQLA VMSAFLGPDQ AATEQLLATD PQVAPWVQKY
QRSRETVSQT DYEVDLITAF TKLSCLGQQI NFEAYTYPVE RINLSKLKL
