GLRX5_MOUSE
ID GLRX5_MOUSE Reviewed; 152 AA.
AC Q80Y14; Q3YML1; Q9D6E9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glutaredoxin-related protein 5, mitochondrial;
DE AltName: Full=Monothiol glutaredoxin-5;
DE Flags: Precursor;
GN Name=Glrx5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=16110529; DOI=10.1038/nature03887;
RG The Tuebingen 2000 screen consortium;
RA Wingert R.A., Galloway J.L., Barut B., Foott H., Fraenkel P., Axe J.L.,
RA Weber G.J., Dooley K., Davidson A.J., Schmid B., Paw B.H., Shaw G.C.,
RA Kingsley P., Palis J., Schubert H., Chen O., Kaplan J., Zon L.I.;
RT "Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for
RT vertebrate haem synthesis.";
RL Nature 436:1035-1039(2005).
RN [2]
RP ERRATUM OF PUBMED:16110529.
RG The Tuebingen 2000 screen consortium;
RA Wingert R.A., Galloway J.L., Barut B., Foott H., Fraenkel P., Axe J.L.,
RA Weber G.J., Dooley K., Davidson A.J., Schmid B., Paw B.H., Shaw G.C.,
RA Kingsley P., Palis J., Schubert H., Chen O., Kaplan J., Zon L.I.;
RL Nature 437:920-920(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19442627; DOI=10.1016/j.bone.2009.01.003;
RA Linares G.R., Xing W., Govoni K.E., Chen S.T., Mohan S.;
RT "Glutaredoxin 5 regulates osteoblast apoptosis by protecting against
RT oxidative stress.";
RL Bone 44:795-804(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (PubMed:19442627). Receives 2Fe/2S clusters
CC from scaffold protein ISCU and mediates their transfer to apoproteins,
CC to the 4Fe/FS cluster biosynthesis machinery, or export from
CC mitochondrion (By similarity). Required for normal regulation of
CC hemoglobin synthesis by the iron-sulfur protein ACO1 (By similarity).
CC {ECO:0000250|UniProtKB:Q86SX6, ECO:0000269|PubMed:19442627}.
CC -!- SUBUNIT: Homodimer. Interacts with ISCU. Interacts with BOLA1.
CC {ECO:0000250|UniProtKB:Q86SX6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q86SX6}.
CC -!- TISSUE SPECIFICITY: Detected in bone, liver, muscle and kidney.
CC {ECO:0000269|PubMed:19442627}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at 7.5 dpc. At 8.5 dpc,
CC preferential expression in yolk sac blood islands. Progressive down-
CC regulation in maturing primitive red cells between 10.5 and 12.5 dpc.
CC High expression in fetal liver at 12.5 dpc.
CC {ECO:0000269|PubMed:16110529}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ083330; AAZ30730.1; -; mRNA.
DR EMBL; AK013761; BAB28985.1; -; mRNA.
DR EMBL; AK050883; BAC34443.1; -; mRNA.
DR EMBL; BC050937; AAH50937.1; ALT_INIT; mRNA.
DR EMBL; BC058371; AAH58371.1; -; mRNA.
DR CCDS; CCDS26154.1; -.
DR RefSeq; NP_082695.1; NM_028419.3.
DR AlphaFoldDB; Q80Y14; -.
DR SMR; Q80Y14; -.
DR BioGRID; 215731; 5.
DR IntAct; Q80Y14; 4.
DR STRING; 10090.ENSMUSP00000021522; -.
DR iPTMnet; Q80Y14; -.
DR PhosphoSitePlus; Q80Y14; -.
DR SwissPalm; Q80Y14; -.
DR EPD; Q80Y14; -.
DR jPOST; Q80Y14; -.
DR MaxQB; Q80Y14; -.
DR PaxDb; Q80Y14; -.
DR PeptideAtlas; Q80Y14; -.
DR PRIDE; Q80Y14; -.
DR ProteomicsDB; 270998; -.
DR Antibodypedia; 47425; 150 antibodies from 25 providers.
DR DNASU; 73046; -.
DR Ensembl; ENSMUST00000021522; ENSMUSP00000021522; ENSMUSG00000021102.
DR GeneID; 73046; -.
DR KEGG; mmu:73046; -.
DR UCSC; uc007oxu.1; mouse.
DR CTD; 51218; -.
DR MGI; MGI:1920296; Glrx5.
DR VEuPathDB; HostDB:ENSMUSG00000021102; -.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075082; -.
DR HOGENOM; CLU_026126_2_0_1; -.
DR InParanoid; Q80Y14; -.
DR OMA; GCDILMQ; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q80Y14; -.
DR TreeFam; TF318988; -.
DR Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR BioGRID-ORCS; 73046; 23 hits in 70 CRISPR screens.
DR ChiTaRS; Glrx5; mouse.
DR PRO; PR:Q80Y14; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80Y14; protein.
DR Bgee; ENSMUSG00000021102; Expressed in otolith organ and 215 other tissues.
DR ExpressionAtlas; Q80Y14; baseline and differential.
DR Genevisible; Q80Y14; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; ISO:MGI.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; ISO:MGI.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10293; PTHR10293; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00365; TIGR00365; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..152
FT /note="Glutaredoxin-related protein 5, mitochondrial"
FT /id="PRO_0000141651"
FT DOMAIN 38..141
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 93..97
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 105
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 118..119
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT MOD_RES 55
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 152 AA; 16292 MW; 76EBEAA30F482825 CRC64;
MSASLSRAAA ALLRWGRSAG GGGLPGAGVR AASSGGQAEQ LDALVKKDKV VVFLKGTPEQ
PQCGFSNAVV QILRLHGVRD YAAYNVLDDP ELRQGIKDYS NWPTIPQVYL NGEFVGGCDI
LLQMHQNGDL VEELKKLGIR SALVDEKDQD SK
