Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q80Y14 (GLRX5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaredoxin-related protein 5, mitochondrial
Alternative name(s):
Monothiol glutaredoxin-5
Gene names
Name:Glrx5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Detected in bone, liver, muscle and kidney. Ref.5

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. Ref.1

Sequence similarities

Belongs to the glutaredoxin family. Monothiol subfamily.

Contains 1 glutaredoxin domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion Potential
Chain32 – 152121Glutaredoxin-related protein 5, mitochondrial
PRO_0000141651

Regions

Domain38 – 141104Glutaredoxin
Region93 – 975Glutathione binding By similarity
Region118 – 1192Glutathione binding By similarity
Compositional bias8 – 114Poly-Ala
Compositional bias20 – 234Poly-Gly

Sites

Metal binding631Iron-sulfur (2Fe-2S); shared with dimeric partner By similarity
Binding site551Glutathione By similarity
Binding site1051Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue551N6-succinyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q80Y14 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 76EBEAA30F482825

FASTA15216,292
        10         20         30         40         50         60 
MSASLSRAAA ALLRWGRSAG GGGLPGAGVR AASSGGQAEQ LDALVKKDKV VVFLKGTPEQ 

        70         80         90        100        110        120 
PQCGFSNAVV QILRLHGVRD YAAYNVLDDP ELRQGIKDYS NWPTIPQVYL NGEFVGGCDI 

       130        140        150 
LLQMHQNGDL VEELKKLGIR SALVDEKDQD SK 

« Hide

References

« Hide 'large scale' references
[1]"Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis."
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 436:1035-1039(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[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]"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. expand/collapse author list , 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.
[4]"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.
[5]"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.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_082695.1. NM_028419.2.
UniGeneMm.29128.
Mm.490286.

3D structure databases

ProteinModelPortalQ80Y14.
SMRQ80Y14. Positions 38-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80Y14. 1 interaction.
MINTMINT-1753495.

PTM databases

PhosphoSiteQ80Y14.

Proteomic databases

PaxDbQ80Y14.
PRIDEQ80Y14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021522; ENSMUSP00000021522; ENSMUSG00000021102.
GeneID73046.
KEGGmmu:73046.
UCSCuc007oxu.1. mouse.

Organism-specific databases

CTD51218.
MGIMGI:1920296. Glrx5.

Phylogenomic databases

eggNOGCOG0278.
GeneTreeENSGT00550000075082.
HOGENOMHOG000095211.
InParanoidQ80Y14.
KOK07390.
OMADPQLRQG.
OrthoDBEOG7B5WX3.
PhylomeDBQ80Y14.
TreeFamTF318988.

Gene expression databases

BgeeQ80Y14.
CleanExMM_GLRX5.
GenevestigatorQ80Y14.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR10293. PTHR10293. 1 hit.
PfamPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR00365. TIGR00365. 1 hit.
PROSITEPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGLRX5. mouse.
NextBio337371.
PROQ80Y14.
SOURCESearch...

Entry information

Entry nameGLRX5_MOUSE
AccessionPrimary (citable) accession number: Q80Y14
Secondary accession number(s): Q3YML1, Q9D6E9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot