Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Monothiol glutaredoxin-S14, chloroplastic (AtGRXcp) (AtGrxS14) (CAX-interacting protein 1) (CXIP1)

 GRS14_ARATH             Reviewed;         173 AA.
Q84Y95; Q9SV38;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-APR-2018, entry version 102.
RecName: Full=Monothiol glutaredoxin-S14, chloroplastic {ECO:0000303|PubMed:15170506};
Short=AtGRXcp {ECO:0000303|PubMed:16829529};
Short=AtGrxS14 {ECO:0000303|PubMed:15170506};
AltName: Full=CAX-interacting protein 1 {ECO:0000303|PubMed:12480930};
Short=CXIP1 {ECO:0000303|PubMed:12480930};
Flags: Precursor;
Name=GRXS14 {ECO:0000303|PubMed:15170506};
Synonyms=CXIP1 {ECO:0000303|PubMed:12480930},
GRX5P {ECO:0000303|PubMed:18044966},
GRXCP {ECO:0000303|PubMed:16829529};
OrderedLocusNames=At3g54900 {ECO:0000312|Araport:AT3G54900};
ORFNames=F28P10.120 {ECO:0000312|EMBL:CAB41094.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CAX1, TISSUE SPECIFICITY,
INDUCTION, AND MUTAGENESIS OF 97-CYS--SER-100 AND 133-SER--THR-137.
PubMed=12480930; DOI=10.1074/jbc.M210883200;
Cheng N.-H., Hirschi K.D.;
"Cloning and characterization of CXIP1 A novel PICOT domain-containing
Arabidopsis protein that associates with CAX1.";
J. Biol. Chem. 278:6503-6509(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15170506; DOI=10.1007/s00018-004-3410-y;
Rouhier N., Gelhaye E., Jacquot J.-P.;
"Plant glutaredoxins: still mysterious reducing systems.";
Cell. Mol. Life Sci. 61:1266-1277(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
MUTAGENESIS OF CYS-97 AND PHE-99, AND DISRUPTION PHENOTYPE.
PubMed=16829529; DOI=10.1074/jbc.M601354200;
Cheng N.-H., Liu J.-Z., Brock A., Nelson R.S., Hirschi K.D.;
"AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for
protection against protein oxidative damage.";
J. Biol. Chem. 281:26280-26288(2006).
[7]
GENE FAMILY.
PubMed=16720602; DOI=10.1093/jxb/erl001;
Rouhier N., Couturier J., Jacquot J.-P.;
"Genome-wide analysis of plant glutaredoxin systems.";
J. Exp. Bot. 57:1685-1696(2006).
[8]
FUNCTION, AND IRON-SULFUR CLUSTER BINDING.
PubMed=18044966; DOI=10.1021/bi7013272;
Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., Chauvat F.;
"CGFS-type monothiol glutaredoxins from the cyanobacterium
Synechocystis PCC6803 and other evolutionary distant model organisms
possess a glutathione-ligated [2Fe-2S] cluster.";
Biochemistry 46:15018-15026(2007).
[9]
INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND MUTAGENESIS OF
CYS-97.
PubMed=24203231; DOI=10.1093/mp/sst156;
Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D.,
Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
"Monothiol glutaredoxin-BolA interactions: redox control of
Arabidopsis thaliana BolA2 and SufE1.";
Mol. Plant 7:187-205(2014).
[10]
FUNCTION, AND INTERACTION WITH BOLA1.
PubMed=24714563; DOI=10.4161/psb.28564;
Dhalleine T., Rouhier N., Couturier J.;
"Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
Plant Signal. Behav. 9:E28564-E28564(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 65-173.
PubMed=20516625; DOI=10.1107/S0907444910013119;
Li L., Cheng N., Hirschi K.D., Wang X.;
"Structure of Arabidopsis chloroplastic monothiol glutaredoxin
AtGRXcp.";
Acta Crystallogr. D 66:725-732(2010).
[12]
STRUCTURE BY NMR OF 67-173 IN COMPLEX WITH BOLA1, AND DOMAIN.
PubMed=25012657; DOI=10.1074/jbc.M114.572701;
Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N.,
Didierjean C.;
"Structural and spectroscopic insights into BolA-glutaredoxin
complexes.";
J. Biol. Chem. 289:24588-24598(2014).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:16829529, ECO:0000269|PubMed:18044966,
ECO:0000269|PubMed:24714563, ECO:0000305}.
-!- SUBUNIT: [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).
{ECO:0000250|UniProtKB:Q03835, ECO:0000269|PubMed:12480930,
ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:16829529}.
-!- TISSUE SPECIFICITY: Hihgly expressed in leaves, at intermediate
levels in stems and at lower levels in roots and flowers.
{ECO:0000269|PubMed:12480930, ECO:0000269|PubMed:16829529}.
-!- INDUCTION: By sodium and magnesium chloride.
{ECO:0000269|PubMed:12480930, ECO:0000269|PubMed:16829529}.
-!- DOMAIN: The C-terminal region (79-168) is involved in BOLA
recognition in GRXS-BOLA apo-heterodimer.
{ECO:0000269|PubMed:25012657}.
-!- DISRUPTION PHENOTYPE: Plants display high sensitivity to external
oxidants, and their content of protein carbonylation is higher
than wild-type plants. {ECO:0000269|PubMed:16829529}.
-!- 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. {ECO:0000269|PubMed:25012657}.
-!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY157988; AAO19647.1; -; mRNA.
EMBL; AL049655; CAB41094.1; -; Genomic_DNA.
EMBL; CP002686; AEE79309.1; -; Genomic_DNA.
EMBL; AF385708; AAK60300.1; -; mRNA.
EMBL; AY078020; AAL77721.1; -; mRNA.
PIR; T06730; T06730.
RefSeq; NP_191050.1; NM_115347.4.
UniGene; At.23079; -.
PDB; 2MMA; NMR; -; A=65-173.
PDB; 3IPZ; X-ray; 2.40 A; A=65-173.
PDBsum; 2MMA; -.
PDBsum; 3IPZ; -.
ProteinModelPortal; Q84Y95; -.
SMR; Q84Y95; -.
BioGrid; 9971; 10.
IntAct; Q84Y95; 4.
STRING; 3702.AT3G54900.1; -.
PaxDb; Q84Y95; -.
PRIDE; Q84Y95; -.
EnsemblPlants; AT3G54900.1; AT3G54900.1; AT3G54900.
GeneID; 824655; -.
Gramene; AT3G54900.1; AT3G54900.1; AT3G54900.
KEGG; ath:AT3G54900; -.
Araport; AT3G54900; -.
TAIR; locus:2082647; AT3G54900.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
HOGENOM; HOG000095211; -.
InParanoid; Q84Y95; -.
OMA; EVEKAMC; -.
OrthoDB; EOG09360Q6L; -.
PhylomeDB; Q84Y95; -.
EvolutionaryTrace; Q84Y95; -.
PRO; PR:Q84Y95; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q84Y95; baseline and differential.
Genevisible; Q84Y95; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0015297; F:antiporter activity; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0006812; P:cation transport; IDA:TAIR.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
CDD; cd03028; GRX_PICOT_like; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Chloroplast; Complete proteome; Disulfide bond;
Glutathionylation; Iron; Iron-sulfur; Metal-binding; Plastid;
Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 63 Chloroplast. {ECO:0000255}.
CHAIN 64 173 Monothiol glutaredoxin-S14,
chloroplastic.
/FTId=PRO_0000268734.
DOMAIN 72 173 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 97 100 Required for CAX1 activation.
REGION 133 137 Required for CAX1 activation.
REGION 151 152 Glutathione binding.
{ECO:0000250|UniProtKB:P0AC69}.
METAL 97 97 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000305|PubMed:18044966,
ECO:0000305|PubMed:20516625}.
METAL 99 99 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000305|PubMed:18044966,
ECO:0000305|PubMed:20516625}.
BINDING 89 89 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 126 126 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 130 130 Glutathione.
{ECO:0000305|PubMed:20516625}.
BINDING 138 138 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P0AC69}.
MOD_RES 97 97 S-glutathionyl cysteine.
{ECO:0000250|UniProtKB:Q9NS18}.
DISULFID 172 172 Interchain.
{ECO:0000305|PubMed:20516625}.
MUTAGEN 97 100 CGFS->AAAA: Loss of CAX1 activation.
{ECO:0000269|PubMed:12480930}.
MUTAGEN 97 97 C->A: Decreases protein stability.
{ECO:0000269|PubMed:16829529}.
MUTAGEN 97 97 C->S: No effect on interactions with BOLA
proteins, but strongly reduced
interaction with SUFE1.
{ECO:0000269|PubMed:24203231}.
MUTAGEN 99 99 F->A: No effect on protein stability.
{ECO:0000269|PubMed:16829529}.
MUTAGEN 133 137 SNWPT->AAAAA: Loss of CAX1 activation.
{ECO:0000269|PubMed:12480930}.
CONFLICT 14 14 S -> P (in Ref. 1; AAO19647).
{ECO:0000305}.
HELIX 69 79 {ECO:0000244|PDB:3IPZ}.
STRAND 81 90 {ECO:0000244|PDB:3IPZ}.
STRAND 92 97 {ECO:0000244|PDB:3IPZ}.
HELIX 98 109 {ECO:0000244|PDB:3IPZ}.
STRAND 115 118 {ECO:0000244|PDB:3IPZ}.
HELIX 119 121 {ECO:0000244|PDB:3IPZ}.
HELIX 123 133 {ECO:0000244|PDB:3IPZ}.
STRAND 136 138 {ECO:0000244|PDB:3IPZ}.
STRAND 140 143 {ECO:0000244|PDB:3IPZ}.
STRAND 146 149 {ECO:0000244|PDB:3IPZ}.
HELIX 151 160 {ECO:0000244|PDB:3IPZ}.
HELIX 162 172 {ECO:0000244|PDB:3IPZ}.
SEQUENCE 173 AA; 19309 MW; 3C005CCD72742A09 CRC64;
MALRSVKTPT LITSVAVVSS SVTNKPHSIR FSLKPTSALV VHNHQLSFYG SNLKLKPTKF
RCSASALTPQ LKDTLEKLVN SEKVVLFMKG TRDFPMCGFS NTVVQILKNL NVPFEDVNIL
ENEMLRQGLK EYSNWPTFPQ LYIGGEFFGG CDITLEAFKT GELQEEVEKA MCS


Related products :

Catalog number Product name Quantity


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur