P82281 (TL29_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thylakoid lumenal 29 kDa protein, chloroplastic
Short name=TL29
EC=1.-.-.-

Alternative name(s):
AtAPx07
P29
Probable L-ascorbate peroxidase 4

Gene names

Name:	TL29
Synonyms:	APX4
Ordered Locus Names:	At4g09010
ORF Names:	F23J3.40

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Plastid › chloroplast thylakoid lumen Ref.5 Ref.7.
Developmental stage	Down-regulated during leaf senescence. Ref.6
Sequence similarities	Belongs to the peroxidase family.
Caution	Was originally thought to be an ascorbate peroxidase (Ref.4, Ref.6). Ref.7 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.

Ontologies

Keywords
Cellular component	Chloroplast Plastid Thylakoid
Domain	Transit peptide
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast thylakoid membrane Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. Source: TAIR
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trxA	P0AA25	2	EBI-2895799,EBI-368542	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Chloroplast Potential

Transit peptide

? – 82

Thylakoid Ref.5

Chain

83 – 349

267

Thylakoid lumenal 29 kDa protein, chloroplastic

PRO_0000023635

Experimental info

Sequence conflict

96

1

S → A in AAP72143. Ref.4

Secondary structure

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349

Helix Strand Turn

Details...

Helix

86 – 108

23

Helix

110 – 112

3

Helix

113 – 124

12

Turn

129 – 132

4

Beta strand

135 – 138

4

Helix

139 – 141

3

Helix

143 – 146

4

Helix

149 – 151

3

Helix

155 – 169

15

Helix

179 – 202

24

Turn

203 – 205

3

Helix

207 – 216

10

Helix

220 – 223

4

Helix

224 – 228

5

Helix

247 – 249

3

Helix

252 – 261

10

Helix

266 – 271

6

Helix

273 – 276

4

Helix

280 – 287

8

Turn

291 – 293

3

Helix

294 – 305

12

Beta strand

306 – 308

3

Helix

310 – 324

15

Turn

325 – 327

3

Turn

332 – 335

4

Sequences

	Sequence		Length	Mass (Da)
	P82281 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: ABD439188BDA8E61	FASTA	349	37,934
	10 20 30 40 50 60 MGGVSFLSTV PSFTNTTNHQ HLTTLSSSSH RSAVIRCSKI EPQVSGESLA FHRRDVLKLA 70 80 90 100 110 120 GTAVGMELIG NGFINNVGDA KAADLNQRRQ RSEFQSKIKI LLSTTIKAKP ELVPSLLKLA 130 140 150 160 170 180 LNDAMTYDKA TKSGGANGSI RFSSELSRAE NEGLSDGLSL IEEVKKEIDS ISKGGPISYA 190 200 210 220 230 240 DIIQLAGQSA VKFTYLASAI RKCGGNEEKG NLLYTAYGSA GQWGLFDRNF GRSDATEADP 250 260 270 280 290 300 EGRVPQWGKA TVQEMKDKFI AVGLGPRQLA VMSAFLGPDQ AATEQLLATD PQVAPWVQKY 310 320 330 340 QRSRETVSQT DYEVDLITAF TKLSCLGQQI NFEAYTYPVE RINLSKLKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10617198] [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: 14593172] [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: 12068123] [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: 11034343] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-112, SUBCELLULAR LOCATION. Strain: cv. Columbia.
[6]	"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: 16034597] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[7]	"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: 19828564] [Abstract] Cited for: FUNCTION REVISION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00529692.

PIR

A85091.

RefSeq

NP_192640.1. NM_116970.3.

UniGene

At.22637.
At.47549.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RRW	X-ray	2.50	A/B	83-349	[»]

ProteinModelPortal

P82281.

SMR

P82281. Positions 85-339.

ModBase

Search...

Protein-protein interaction databases

IntAct

P82281. 3 interactions.

STRING

P82281.

Protein family/group databases

PeroxiBase

3920. AtAPx07.

Proteomic databases

PRIDE

P82281.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G09010.1; AT4G09010.1; AT4G09010.

GeneID

826480.

GenomeReviews

Gene locus AT4G09010 in contig CT486007_GR.

KEGG

ath:AT4G09010.

NMPDR

fig|3702.1.peg.18558.

Organism-specific databases

GeneFarm

1959. 146.

TAIR

At4g09010.

Phylogenomic databases

GeneTree

EPGT00050000009945.

HOGENOM

HBG318899.

InParanoid

P82281.

OMA

GQWGLFD.

PhylomeDB

P82281.

ProtClustDB

CLSN2686017.

Gene expression databases

Genevestigator

P82281.

GermOnline

AT4G09010. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]

KO

K00434.

Pfam

PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00459. ASPEROXIDASE.

SUPFAM

SSF48113. Peroxidase_super. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TL29_ARATH

Accession

Primary (citable) accession number: P82281
Secondary accession number(s): Q7XZP6, Q9M0S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	December 14, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program