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Protein

Glutaredoxin-related protein 5, mitochondrial

Gene

Glrx5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. May protect cells against apoptosis due to reactive oxygen species and oxidative stress.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551GlutathioneBy similarity
Metal bindingi63 – 631Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity
Binding sitei105 – 1051Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-related protein 5, mitochondrial
Alternative name(s):
Monothiol glutaredoxin-5
Gene namesi
Name:Glrx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1920296. Glrx5.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131MitochondrionSequence AnalysisAdd
BLAST
Chaini32 – 152121Glutaredoxin-related protein 5, mitochondrialPRO_0000141651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-succinyllysine1 Publication

Proteomic databases

MaxQBiQ80Y14.
PaxDbiQ80Y14.
PRIDEiQ80Y14.

PTM databases

PhosphoSiteiQ80Y14.

Expressioni

Tissue specificityi

Detected in bone, liver, muscle and kidney.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ80Y14.
CleanExiMM_GLRX5.
GenevisibleiQ80Y14. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ80Y14. 1 interaction.
MINTiMINT-1753495.
STRINGi10090.ENSMUSP00000021522.

Structurei

3D structure databases

ProteinModelPortaliQ80Y14.
SMRiQ80Y14. Positions 38-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 141104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 975Glutathione bindingBy similarity
Regioni118 – 1192Glutathione bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 114Poly-Ala
Compositional biasi20 – 234Poly-Gly

Sequence similaritiesi

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0278.
GeneTreeiENSGT00550000075082.
HOGENOMiHOG000095211.
InParanoidiQ80Y14.
KOiK07390.
OMAiQMHQNGE.
OrthoDBiEOG7B5WX3.
PhylomeDBiQ80Y14.
TreeFamiTF318988.

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.

Q80Y14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASLSRAAA ALLRWGRSAG GGGLPGAGVR AASSGGQAEQ LDALVKKDKV
60 70 80 90 100
VVFLKGTPEQ PQCGFSNAVV QILRLHGVRD YAAYNVLDDP ELRQGIKDYS
110 120 130 140 150
NWPTIPQVYL NGEFVGGCDI LLQMHQNGDL VEELKKLGIR SALVDEKDQD

SK
Length:152
Mass (Da):16,292
Last modified:February 1, 2005 - v2
Checksum:i76EBEAA30F482825
GO

Sequence cautioni

The sequence AAH50937.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ083330 mRNA. Translation: AAZ30730.1.
AK013761 mRNA. Translation: BAB28985.1.
AK050883 mRNA. Translation: BAC34443.1.
BC050937 mRNA. Translation: AAH50937.1. Different initiation.
BC058371 mRNA. Translation: AAH58371.1.
CCDSiCCDS26154.1.
RefSeqiNP_082695.1. NM_028419.2.
UniGeneiMm.29128.
Mm.490286.

Genome annotation databases

EnsembliENSMUST00000021522; ENSMUSP00000021522; ENSMUSG00000021102.
GeneIDi73046.
KEGGimmu:73046.
UCSCiuc007oxu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ083330 mRNA. Translation: AAZ30730.1.
AK013761 mRNA. Translation: BAB28985.1.
AK050883 mRNA. Translation: BAC34443.1.
BC050937 mRNA. Translation: AAH50937.1. Different initiation.
BC058371 mRNA. Translation: AAH58371.1.
CCDSiCCDS26154.1.
RefSeqiNP_082695.1. NM_028419.2.
UniGeneiMm.29128.
Mm.490286.

3D structure databases

ProteinModelPortaliQ80Y14.
SMRiQ80Y14. Positions 38-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80Y14. 1 interaction.
MINTiMINT-1753495.
STRINGi10090.ENSMUSP00000021522.

PTM databases

PhosphoSiteiQ80Y14.

Proteomic databases

MaxQBiQ80Y14.
PaxDbiQ80Y14.
PRIDEiQ80Y14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021522; ENSMUSP00000021522; ENSMUSG00000021102.
GeneIDi73046.
KEGGimmu:73046.
UCSCiuc007oxu.1. mouse.

Organism-specific databases

CTDi51218.
MGIiMGI:1920296. Glrx5.

Phylogenomic databases

eggNOGiCOG0278.
GeneTreeiENSGT00550000075082.
HOGENOMiHOG000095211.
InParanoidiQ80Y14.
KOiK07390.
OMAiQMHQNGE.
OrthoDBiEOG7B5WX3.
PhylomeDBiQ80Y14.
TreeFamiTF318988.

Miscellaneous databases

ChiTaRSiGlrx5. mouse.
NextBioi337371.
PROiQ80Y14.
SOURCEiSearch...

Gene expression databases

BgeeiQ80Y14.
CleanExiMM_GLRX5.
GenevisibleiQ80Y14. MM.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress."
    Linares G.R., Xing W., Govoni K.E., Chen S.T., Mohan S.
    Bone 44:795-804(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLRX5_MOUSE
AccessioniPrimary (citable) accession number: Q80Y14
Secondary accession number(s): Q3YML1, Q9D6E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 24, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.