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Protein

Monothiol glutaredoxin-S14, chloroplastic

Gene

GRXS14

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

Functioni

May only reduce GSH-thiol disulfides, but not protein disulfides (Potential). Probably involved in the regulation of the redox state of the BOLA proteins (Potential). May act as Fe-S cluster donors to Fe-S cluster-requiring proteins (PubMed:18044966). May protect cells against protein oxidative damage (PubMed:16829529). May regulate CAX cation transporters (PubMed:16829529). The GRXS14-BOLA1 heterodimer binds a labile, oxygen sensitive Fe-S cluster (PubMed:24714563).Curated3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891GlutathioneBy similarity
Metal bindingi97 – 971Iron-sulfur (2Fe-2S); shared with dimeric partner2 Publications
Metal bindingi99 – 991Iron-sulfur (2Fe-2S); shared with dimeric partner2 Publications
Binding sitei126 – 1261GlutathioneBy similarity
Binding sitei130 – 1301Glutathione1 Publication
Binding sitei138 – 1381Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

  • cation transport Source: TAIR
  • cell redox homeostasis Source: InterPro
  • transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Monothiol glutaredoxin-S14, chloroplastic1 Publication
Short name:
AtGRXcp1 Publication
Short name:
AtGrxS141 Publication
Alternative name(s):
CAX-interacting protein 11 Publication
Short name:
CXIP11 Publication
Gene namesi
Name:GRXS141 Publication
Synonyms:CXIP11 Publication, GRX5P1 Publication, GRXCP1 Publication
Ordered Locus Names:At3g54900Imported
ORF Names:F28P10.120Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G54900.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Plants display high sensitivity to external oxidants, and their content of protein carbonylation is higher than wild-type plants.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 1004CGFS → AAAA: Loss of CAX1 activation. 1 Publication
Mutagenesisi97 – 971C → A: Decreases protein stability. 1 Publication
Mutagenesisi97 – 971C → S: No effect on interactions with BOLA proteins, but strongly reduced interaction with SUFE1. 1 Publication
Mutagenesisi99 – 991F → A: No effect on protein stability. 1 Publication
Mutagenesisi133 – 1375SNWPT → AAAAA: Loss of CAX1 activation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6363ChloroplastSequence analysisAdd
BLAST
Chaini64 – 173110Monothiol glutaredoxin-S14, chloroplasticPRO_0000268734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971S-glutathionyl cysteineBy similarity
Disulfide bondi172 – 172Interchain1 Publication

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

PaxDbiQ84Y95.
PRIDEiQ84Y95.

Expressioni

Tissue specificityi

Hihgly expressed in leaves, at intermediate levels in stems and at lower levels in roots and flowers.2 Publications

Inductioni

By sodium and magnesium chloride.2 Publications

Gene expression databases

GenevisibleiQ84Y95. AT.

Interactioni

Subunit structurei

[2Fe-2S]-bridged holo-homodimer (By similarity). Interacts with N-terminal part of CAX1 in yeast (PubMed:12480930). Interacts in vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231). Interacts in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231, PubMed:24714563).By similarity3 Publications

Protein-protein interaction databases

BioGridi9971. 10 interactions.
IntActiQ84Y95. 4 interactions.
STRINGi3702.AT3G54900.1.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 7911Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi92 – 976Combined sources
Helixi98 – 10912Combined sources
Beta strandi115 – 1184Combined sources
Helixi119 – 1213Combined sources
Helixi123 – 13311Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 1494Combined sources
Helixi151 – 16010Combined sources
Helixi162 – 17211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MMANMR-A67-173[»]
3IPZX-ray2.40A65-173[»]
ProteinModelPortaliQ84Y95.
SMRiQ84Y95. Positions 65-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ84Y95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 173102GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 1004Required for CAX1 activation
Regioni133 – 1375Required for CAX1 activation
Regioni151 – 1522Glutathione bindingBy similarity

Domaini

The C-terminal region (79-168) is involved in BOLA recognition in GRXS-BOLA apo-heterodimer.1 Publication

Sequence similaritiesi

Belongs to the glutaredoxin family. CGFS subfamily.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0911. Eukaryota.
COG0278. LUCA.
HOGENOMiHOG000095211.
InParanoidiQ84Y95.
OMAiEVEKAMC.
PhylomeDBiQ84Y95.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q84Y95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRSVKTPT LITSVAVVSS SVTNKPHSIR FSLKPTSALV VHNHQLSFYG
60 70 80 90 100
SNLKLKPTKF RCSASALTPQ LKDTLEKLVN SEKVVLFMKG TRDFPMCGFS
110 120 130 140 150
NTVVQILKNL NVPFEDVNIL ENEMLRQGLK EYSNWPTFPQ LYIGGEFFGG
160 170
CDITLEAFKT GELQEEVEKA MCS
Length:173
Mass (Da):19,309
Last modified:December 12, 2006 - v2
Checksum:i3C005CCD72742A09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141S → P in AAO19647 (PubMed:12480930).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157988 mRNA. Translation: AAO19647.1.
AL049655 Genomic DNA. Translation: CAB41094.1.
CP002686 Genomic DNA. Translation: AEE79309.1.
AF385708 mRNA. Translation: AAK60300.1.
AY078020 mRNA. Translation: AAL77721.1.
PIRiT06730.
RefSeqiNP_191050.1. NM_115347.3.
UniGeneiAt.23079.

Genome annotation databases

EnsemblPlantsiAT3G54900.1; AT3G54900.1; AT3G54900.
GeneIDi824655.
GrameneiAT3G54900.1; AT3G54900.1; AT3G54900.
KEGGiath:AT3G54900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157988 mRNA. Translation: AAO19647.1.
AL049655 Genomic DNA. Translation: CAB41094.1.
CP002686 Genomic DNA. Translation: AEE79309.1.
AF385708 mRNA. Translation: AAK60300.1.
AY078020 mRNA. Translation: AAL77721.1.
PIRiT06730.
RefSeqiNP_191050.1. NM_115347.3.
UniGeneiAt.23079.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MMANMR-A67-173[»]
3IPZX-ray2.40A65-173[»]
ProteinModelPortaliQ84Y95.
SMRiQ84Y95. Positions 65-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9971. 10 interactions.
IntActiQ84Y95. 4 interactions.
STRINGi3702.AT3G54900.1.

Proteomic databases

PaxDbiQ84Y95.
PRIDEiQ84Y95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G54900.1; AT3G54900.1; AT3G54900.
GeneIDi824655.
GrameneiAT3G54900.1; AT3G54900.1; AT3G54900.
KEGGiath:AT3G54900.

Organism-specific databases

TAIRiAT3G54900.

Phylogenomic databases

eggNOGiKOG0911. Eukaryota.
COG0278. LUCA.
HOGENOMiHOG000095211.
InParanoidiQ84Y95.
OMAiEVEKAMC.
PhylomeDBiQ84Y95.

Miscellaneous databases

EvolutionaryTraceiQ84Y95.
PROiQ84Y95.

Gene expression databases

GenevisibleiQ84Y95. AT.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of CXIP1 A novel PICOT domain-containing Arabidopsis protein that associates with CAX1."
    Cheng N.-H., Hirschi K.D.
    J. Biol. Chem. 278:6503-6509(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CAX1, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF 97-CYS--SER-100 AND 133-SER--THR-137.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "Plant glutaredoxins: still mysterious reducing systems."
    Rouhier N., Gelhaye E., Jacquot J.-P.
    Cell. Mol. Life Sci. 61:1266-1277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  6. "AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage."
    Cheng N.-H., Liu J.-Z., Brock A., Nelson R.S., Hirschi K.D.
    J. Biol. Chem. 281:26280-26288(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF CYS-97 AND PHE-99, DISRUPTION PHENOTYPE.
  7. "Genome-wide analysis of plant glutaredoxin systems."
    Rouhier N., Couturier J., Jacquot J.-P.
    J. Exp. Bot. 57:1685-1696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  8. "CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster."
    Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., Chauvat F.
    Biochemistry 46:15018-15026(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IRON-SULFUR CLUSTER BINDING.
  9. "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1."
    Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.
    Mol. Plant 7:187-205(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, MUTAGENESIS OF CYS-97.
  10. "Putative roles of glutaredoxin-BolA holo-heterodimers in plants."
    Dhalleine T., Rouhier N., Couturier J.
    Plant Signal. Behav. 9:E28564-E28564(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BOLA1.
  11. "Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp."
    Li L., Cheng N., Hirschi K.D., Wang X.
    Acta Crystallogr. D 66:725-732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 65-173.
  12. "Structural and spectroscopic insights into BolA-glutaredoxin complexes."
    Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N., Didierjean C.
    J. Biol. Chem. 289:24588-24598(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 67-173 IN COMPLEX WITH BOLA1, DOMAIN.

Entry informationi

Entry nameiGRS14_ARATH
AccessioniPrimary (citable) accession number: Q84Y95
Secondary accession number(s): Q9SV38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: February 17, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The GRXS14-BOLA1 apo-heterodimer model derived from NMR data shows a domain arrangement totally different from the holo-heterodimer showing evidence for a Rieske-type ligation of a [2Fe-2S] cluster.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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.