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

Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5)

 GLRX5_MOUSE             Reviewed;         152 AA.
Q80Y14; Q3YML1; Q9D6E9;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
25-OCT-2017, entry version 119.
RecName: Full=Glutaredoxin-related protein 5, mitochondrial;
AltName: Full=Monothiol glutaredoxin-5;
Flags: Precursor;
Name=Glrx5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=16110529; DOI=10.1038/nature03887;
The Tuebingen 2000 screen consortium;
Wingert R.A., Galloway J.L., Barut B., Foott H., Fraenkel P.,
Axe J.L., Weber G.J., Dooley K., Davidson A.J., Schmid B., Paw B.H.,
Shaw G.C., Kingsley P., Palis J., Schubert H., Chen O., Kaplan J.,
Zon L.I.;
"Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for
vertebrate haem synthesis.";
Nature 436:1035-1039(2005).
[2]
ERRATUM.
The Tuebingen 2000 screen consortium;
Wingert R.A., Galloway J.L., Barut B., Foott H., Fraenkel P.,
Axe J.L., Weber G.J., Dooley K., Davidson A.J., Schmid B., Paw B.H.,
Shaw G.C., Kingsley P., Palis J., Schubert H., Chen O., Kaplan J.,
Zon L.I.;
Nature 437:920-920(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Hippocampus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19442627; DOI=10.1016/j.bone.2009.01.003;
Linares G.R., Xing W., Govoni K.E., Chen S.T., Mohan S.;
"Glutaredoxin 5 regulates osteoblast apoptosis by protecting against
oxidative stress.";
Bone 44:795-804(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of
iron-sulfur clusters (By similarity). Involved in protein
lipoylation, acting in the pathway that provides an iron-sulfur
cluster to lipoate synthase (By similarity). Required for normal
iron homeostasis (By similarity). Required for normal regulation
of hemoglobin synthesis by the iron-sulfur protein ACO1 (By
similarity). May protect cells against apoptosis due to reactive
oxygen species and oxidative stress (PubMed:19442627).
{ECO:0000250|UniProtKB:Q86SX6, ECO:0000269|PubMed:19442627}.
-!- SUBUNIT: Homodimer. Interacts with ISCU. Interacts with BOLA1.
{ECO:0000250|UniProtKB:Q86SX6}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q86SX6}.
-!- TISSUE SPECIFICITY: Detected in bone, liver, muscle and kidney.
{ECO:0000269|PubMed:19442627}.
-!- DEVELOPMENTAL STAGE: Ubiquitously expressed at 7.5 dpc. At 8.5
dpc, preferential expression in yolk sac blood islands.
Progressive down-regulation in maturing primitive red cells
between 10.5 and 12.5 dpc. High expression in fetal liver at 12.5
dpc. {ECO:0000269|PubMed:16110529}.
-!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH50937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ083330; AAZ30730.1; -; mRNA.
EMBL; AK013761; BAB28985.1; -; mRNA.
EMBL; AK050883; BAC34443.1; -; mRNA.
EMBL; BC050937; AAH50937.1; ALT_INIT; mRNA.
EMBL; BC058371; AAH58371.1; -; mRNA.
CCDS; CCDS26154.1; -.
RefSeq; NP_082695.1; NM_028419.3.
UniGene; Mm.29128; -.
UniGene; Mm.490286; -.
ProteinModelPortal; Q80Y14; -.
SMR; Q80Y14; -.
IntAct; Q80Y14; 4.
MINT; MINT-1753495; -.
STRING; 10090.ENSMUSP00000021522; -.
iPTMnet; Q80Y14; -.
PhosphoSitePlus; Q80Y14; -.
SwissPalm; Q80Y14; -.
EPD; Q80Y14; -.
MaxQB; Q80Y14; -.
PaxDb; Q80Y14; -.
PeptideAtlas; Q80Y14; -.
PRIDE; Q80Y14; -.
Ensembl; ENSMUST00000021522; ENSMUSP00000021522; ENSMUSG00000021102.
GeneID; 73046; -.
KEGG; mmu:73046; -.
UCSC; uc007oxu.1; mouse.
CTD; 51218; -.
MGI; MGI:1920296; Glrx5.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
GeneTree; ENSGT00550000075082; -.
HOGENOM; HOG000095211; -.
InParanoid; Q80Y14; -.
KO; K07390; -.
OMA; KGTKLMP; -.
OrthoDB; EOG091G0YN0; -.
PhylomeDB; Q80Y14; -.
TreeFam; TF318988; -.
Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
ChiTaRS; Glrx5; mouse.
PRO; PR:Q80Y14; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021102; -.
CleanEx; MM_GLRX5; -.
Genevisible; Q80Y14; MM.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier 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:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0009249; P:protein lipoylation; ISO:MGI.
CDD; cd03028; GRX_PICOT_like; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR014434; Monothiol_GRX.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 1.
PIRSF; PIRSF005894; Monothiol_GRX; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
Mitochondrion; Phosphoprotein; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 31 Mitochondrion. {ECO:0000255}.
CHAIN 32 152 Glutaredoxin-related protein 5,
mitochondrial.
/FTId=PRO_0000141651.
DOMAIN 38 141 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 93 97 Glutathione binding.
{ECO:0000250|UniProtKB:Q86SX6}.
REGION 118 119 Glutathione binding.
{ECO:0000250|UniProtKB:Q86SX6}.
COMPBIAS 8 11 Poly-Ala.
COMPBIAS 20 23 Poly-Gly.
METAL 63 63 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:Q86SX6}.
BINDING 55 55 Glutathione.
{ECO:0000250|UniProtKB:Q86SX6}.
BINDING 105 105 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:Q86SX6}.
MOD_RES 55 55 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 152 AA; 16292 MW; 76EBEAA30F482825 CRC64;
MSASLSRAAA ALLRWGRSAG GGGLPGAGVR AASSGGQAEQ LDALVKKDKV VVFLKGTPEQ
PQCGFSNAVV QILRLHGVRD YAAYNVLDDP ELRQGIKDYS NWPTIPQVYL NGEFVGGCDI
LLQMHQNGDL VEELKKLGIR SALVDEKDQD SK


Related products :

Catalog number Product name Quantity
GLRX5_HUMAN Human ELISA Kit FOR Glutaredoxin-related protein 5, mitochondrial 96T
CSB-EL009524MO Mouse Glutaredoxin-related protein 5, mitochondrial(GLRX5) ELISA kit 96T
CSB-EL009524HU Human Glutaredoxin-related protein 5, mitochondrial(GLRX5) ELISA kit 96T
CSB-EL009524HU Human Glutaredoxin-related protein 5, mitochondrial(GLRX5) ELISA kit SpeciesHuman 96T
CSB-EL009524MO Mouse Glutaredoxin-related protein 5, mitochondrial(GLRX5) ELISA kit SpeciesMouse 96T
GLRX5_MOUSE ELISA Kit FOR Glutaredoxin-related protein 5, mitochondrial; organism: Mouse; gene name: Glrx5 96T
orb90118 Yeast Glutaredoxin 1 protein Glutaredoxin Saccharamyces cerevisiae Recombinant conaining 6x His tag at C-Terminus produced in E.coli is a single, non-glycosylated, Polypeptide chain having a molecular 10
orb90120 Yeast Glutaredoxin 2 protein Glutaredoxin-2 Saccharamyces cerevisiae Recombinant conaining 6x His tag at C-terminus produced in E.coli is a single, non-glycosylated, Polypeptide chain having a molecul 10
orb90119 Human Glutaredoxin 2 protein Glutaredoxin-2 Human Recombinant produced in E.coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass o 5
orb90117 Human Glutaredoxin 1 protein Glutaredoxin Human Recombinant produced in E.coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa. For rese 10
LF-MA0082 anti-Glutaredoxin 1 (30A1), Mouse monoclonal to Glutaredoxin 1, Isotype IgG1, Host Mouse 100 ul
CSB-EL009522RA Rat Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit 96T
FDXA1_HUMAN Bovine ELISA Kit FOR Glutaredoxin-2, mitochondrial 96T
E0223p Bovine ELISA Kit FOR Glutaredoxin-2, mitochondrial 96T
BOLA1_BOVIN Bovine ELISA Kit FOR Glutaredoxin-2, mitochondrial 96T
CSB-EL009522HU Human Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit 96T
CSB-EL009522MO Mouse Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit 96T
CSB-EL009522RA Rat Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit SpeciesRat 96T
CSB-EL009522BO Bovine Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit 96T
CSB-EL009522HU Human Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit SpeciesHuman 96T
CSB-EL009522MO Mouse Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit SpeciesMouse 96T
CSB-EL009522BO Bovine Glutaredoxin-2, mitochondrial(GLRX2) ELISA kit SpeciesBovine 96T
GLRX2_MOUSE ELISA Kit FOR Glutaredoxin-2, mitochondrial; organism: Mouse; gene name: Glrx2 96T
LF-P0016 Glutaredoxin 2, Human , Protein 0.1 mg
LF-P0003 Glutaredoxin 1, Human, Protein 0.1 mg


 

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