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Protein

Thylakoid lumenal 29 kDa protein, chloroplastic

Gene

TL29

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Protein family/group databases

PeroxiBasei3920. AtAPx07.

Names & Taxonomyi

Protein namesi
Recommended name:
Thylakoid lumenal 29 kDa protein, chloroplastic (EC:1.-.-.-)
Short name:
TL29
Alternative name(s):
AtAPx07
P29
Probable L-ascorbate peroxidase 4
Gene namesi
Name:TL29
Synonyms:APX4
Ordered Locus Names:At4g09010
ORF Names:F23J3.40
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G09010.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast thylakoid Source: TAIR
  • chloroplast thylakoid lumen Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
  • thylakoid Source: TAIR
  • thylakoid lumen Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei? – 82Thylakoid2 Publications
Transit peptidei1 – ?ChloroplastSequence analysis
Chaini83 – 349267Thylakoid lumenal 29 kDa protein, chloroplasticPRO_0000023635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP82281.
PRIDEiP82281.

PTM databases

iPTMnetiP82281.

Expressioni

Developmental stagei

Down-regulated during leaf senescence.1 Publication

Gene expression databases

GenevisibleiP82281. AT.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
trxAP0AA252EBI-2895799,EBI-368542From a different organism.

Protein-protein interaction databases

BioGridi11779. 2 interactions.
IntActiP82281. 3 interactions.
STRINGi3702.AT4G09010.1.

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi86 – 10823Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 12412Combined sources
Turni129 – 1324Combined sources
Beta strandi135 – 1384Combined sources
Helixi139 – 1413Combined sources
Helixi143 – 1464Combined sources
Helixi149 – 1513Combined sources
Helixi155 – 16915Combined sources
Helixi179 – 20224Combined sources
Turni203 – 2053Combined sources
Helixi207 – 21610Combined sources
Helixi220 – 2234Combined sources
Helixi224 – 2285Combined sources
Helixi247 – 2493Combined sources
Helixi252 – 26110Combined sources
Helixi266 – 2716Combined sources
Helixi273 – 2764Combined sources
Helixi280 – 2878Combined sources
Turni291 – 2933Combined sources
Helixi294 – 30512Combined sources
Beta strandi306 – 3083Combined sources
Helixi310 – 32415Combined sources
Turni325 – 3273Combined sources
Turni332 – 3354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RRWX-ray2.50A/B83-349[»]
ProteinModelPortaliP82281.
SMRiP82281. Positions 85-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGN6. Eukaryota.
ENOG410XSAA. LUCA.
HOGENOMiHOG000005679.
InParanoidiP82281.
KOiK00434.
OMAiNLLYTAY.
PhylomeDBiP82281.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P82281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGVSFLSTV PSFTNTTNHQ HLTTLSSSSH RSAVIRCSKI EPQVSGESLA
60 70 80 90 100
FHRRDVLKLA GTAVGMELIG NGFINNVGDA KAADLNQRRQ RSEFQSKIKI
110 120 130 140 150
LLSTTIKAKP ELVPSLLKLA LNDAMTYDKA TKSGGANGSI RFSSELSRAE
160 170 180 190 200
NEGLSDGLSL IEEVKKEIDS ISKGGPISYA DIIQLAGQSA VKFTYLASAI
210 220 230 240 250
RKCGGNEEKG NLLYTAYGSA GQWGLFDRNF GRSDATEADP EGRVPQWGKA
260 270 280 290 300
TVQEMKDKFI AVGLGPRQLA VMSAFLGPDQ AATEQLLATD PQVAPWVQKY
310 320 330 340
QRSRETVSQT DYEVDLITAF TKLSCLGQQI NFEAYTYPVE RINLSKLKL
Length:349
Mass (Da):37,934
Last modified:December 1, 2000 - v2
Checksum:iABD439188BDA8E61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961S → A in AAP72143 (PubMed:12068123).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005359 Genomic DNA. No translation available.
AL161513 Genomic DNA. Translation: CAB78025.1.
CP002687 Genomic DNA. Translation: AEE82711.1.
AF370534 mRNA. Translation: AAK48961.1.
AY072503 mRNA. Translation: AAL66918.1.
AF441713 mRNA. Translation: AAP72143.1.
PIRiA85091.
RefSeqiNP_192640.1. NM_116970.3.
UniGeneiAt.22637.
At.47549.

Genome annotation databases

EnsemblPlantsiAT4G09010.1; AT4G09010.1; AT4G09010.
GeneIDi826480.
GrameneiAT4G09010.1; AT4G09010.1; AT4G09010.
KEGGiath:AT4G09010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005359 Genomic DNA. No translation available.
AL161513 Genomic DNA. Translation: CAB78025.1.
CP002687 Genomic DNA. Translation: AEE82711.1.
AF370534 mRNA. Translation: AAK48961.1.
AY072503 mRNA. Translation: AAL66918.1.
AF441713 mRNA. Translation: AAP72143.1.
PIRiA85091.
RefSeqiNP_192640.1. NM_116970.3.
UniGeneiAt.22637.
At.47549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RRWX-ray2.50A/B83-349[»]
ProteinModelPortaliP82281.
SMRiP82281. Positions 85-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11779. 2 interactions.
IntActiP82281. 3 interactions.
STRINGi3702.AT4G09010.1.

Protein family/group databases

PeroxiBasei3920. AtAPx07.

PTM databases

iPTMnetiP82281.

Proteomic databases

PaxDbiP82281.
PRIDEiP82281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G09010.1; AT4G09010.1; AT4G09010.
GeneIDi826480.
GrameneiAT4G09010.1; AT4G09010.1; AT4G09010.
KEGGiath:AT4G09010.

Organism-specific databases

TAIRiAT4G09010.

Phylogenomic databases

eggNOGiENOG410IGN6. Eukaryota.
ENOG410XSAA. LUCA.
HOGENOMiHOG000005679.
InParanoidiP82281.
KOiK00434.
OMAiNLLYTAY.
PhylomeDBiP82281.

Miscellaneous databases

PROiP82281.

Gene expression databases

GenevisibleiP82281. AT.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis."
    Panchuk I.I., Volkov R.A., Schoffl F.
    Plant Physiol. 129:838-853(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-306.
    Strain: cv. Columbia.
    Tissue: Leaf.
  5. "A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen."
    Kieselbach T., Bystedt M., Hynds P., Robinson C., Schroeder W.P.
    FEBS Lett. 480:271-276(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 83-112, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  6. Cited for: PROTEIN SEQUENCE OF 83-112, SUBCELLULAR LOCATION.
  7. "Expression of the Apx gene family during leaf senescence of Arabidopsis thaliana."
    Panchuk I.I., Zentgraf U., Volkov R.A.
    Planta 222:926-932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "The TL29 protein is lumen located, associated with PSII and not an ascorbate peroxidase."
    Granlund I., Storm P., Schubert M., Garcia-Cerdan J.G., Funk C., Schroder W.P.
    Plant Cell Physiol. 50:1898-1910(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION REVISION, SUBCELLULAR LOCATION.
  9. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTL29_ARATH
AccessioniPrimary (citable) accession number: P82281
Secondary accession number(s): Q7XZP6, Q9M0S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 17, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be an ascorbate peroxidase (PubMed:12068123, PubMed:16034597). PubMed:19828564 fails to show any peroxidase activity associated with TL29 and demonstrates that TL29 could bind neither heme nor ascorbate. TL29 lacks the heme-binding site, the proton acceptor and the transition state stabilizer, which are conserved features of the ascorbate peroxidase.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.