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

 GLRX5_HUMAN             Reviewed;         157 AA.
Q86SX6; Q0X088; Q3YML0; Q86WY3; Q8IZ54;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=Glutaredoxin-related protein 5, mitochondrial;
AltName: Full=Monothiol glutaredoxin-5;
Flags: Precursor;
Name=GLRX5; Synonyms=C14orf87;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-146.
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.;
Nature 437:920-920(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Kurosawa N., Isobe M., Saito M.;
"Biological function of human glutaredoxin 3 (Grx 3), a novel
mitochondrial monothiol Grx.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-146.
TISSUE=Skin, and Testis;
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).
[7]
INVOLVEMENT IN SIDBA3.
PubMed=17485548; DOI=10.1182/blood-2007-02-072520;
Camaschella C., Campanella A., De Falco L., Boschetto L., Merlini R.,
Silvestri L., Levi S., Iolascon A.;
"The human counterpart of zebrafish shiraz shows sideroblastic-like
microcytic anemia and iron overload.";
Blood 110:1353-1358(2007).
[8]
INVOLVEMENT IN SIDBA3, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20364084; DOI=10.1172/JCI40372;
Ye H., Jeong S.Y., Ghosh M.C., Kovtunovych G., Silvestri L.,
Ortillo D., Uchida N., Tisdale J., Camaschella C., Rouault T.A.;
"Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically
impairing heme biosynthesis and depleting cytosolic iron in human
erythroblasts.";
J. Clin. Invest. 120:1749-1761(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, INVOLVEMENT IN SPAHGC, VARIANT SPAHGC LYS-51 DEL, AND
CHARACTERIZATION OF VARIANT SPAHGC LYS-51 DEL.
PubMed=24334290; DOI=10.1093/brain/awt328;
Baker P.R. II, Friederich M.W., Swanson M.A., Shaikh T.,
Bhattacharya K., Scharer G.H., Aicher J., Creadon-Swindell G.,
Geiger E., MacLean K.N., Lee W.T., Deshpande C., Freckmann M.L.,
Shih L.Y., Wasserstein M., Rasmussen M.B., Lund A.M., Procopis P.,
Cameron J.M., Robinson B.H., Brown G.K., Brown R.M., Compton A.G.,
Dieckmann C.L., Collard R., Coughlin C.R. II, Spector E., Wempe M.F.,
Van Hove J.L.;
"Variant non ketotic hyperglycinemia is caused by mutations in LIAS,
BOLA3 and the novel gene GLRX5.";
Brain 137:366-379(2014).
[11]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-31, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
INTERACTION WITH BOLA1.
PubMed=27532773; DOI=10.7554/eLife.15991;
Melber A., Na U., Vashisht A., Weiler B.D., Lill R.,
Wohlschlegel J.A., Winge D.R.;
"Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to
mitochondrial clients.";
Elife 5:0-0(2016).
[13]
INTERACTION WITH BOLA1.
PubMed=27532772; DOI=10.7554/eLife.16673;
Uzarska M.A., Nasta V., Weiler B.D., Spantgar F., Ciofi-Baffoni S.,
Saviello M.R., Gonnelli L., Muehlenhoff U., Banci L., Lill R.;
"Mitochondrial Bol1 and Bol3 function as assembly factors for specific
iron-sulfur proteins.";
Elife 5:0-0(2016).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-150 IN COMPLEX WITH
GLUTATHIONE AND IRON-SULFUR CLUSTER, AND SUBUNIT.
PubMed=21029046; DOI=10.1042/BJ20101286;
Johansson C., Roos A.K., Montano S.J., Sengupta R.,
Filippakopoulos P., Guo K., von Delft F., Holmgren A., Oppermann U.,
Kavanagh K.L.;
"The crystal structure of human GLRX5: iron-sulfur cluster co-
ordination, tetrameric assembly and monomer activity.";
Biochem. J. 433:303-311(2011).
[15]
VARIANTS SIDBA3 GLN-101 AND SER-148.
PubMed=25342667; DOI=10.1182/blood-2014-08-598508;
Liu G., Guo S., Anderson G.J., Camaschella C., Han B., Nie G.;
"Heterozygous missense mutations in the GLRX5 gene cause sideroblastic
anemia in a Chinese patient.";
Blood 124:2750-2751(2014).
[16]
CHARACTERIZATION OF VARIANTS SIDBA3 GLN-101 AND SER-148, AND
INTERACTION WITH ISCU.
PubMed=26100117; DOI=10.1002/jcb.25267;
Liu G., Wang Y., Anderson G.J., Camaschella C., Chang Y., Nie G.;
"Functional analysis of GLRX5 mutants reveals distinct functionalities
of GLRX5 protein.";
J. Cell. Biochem. 117:207-217(2016).
-!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of
iron-sulfur clusters (PubMed:20364084). Involved in protein
lipoylation, acting in the pathway that provides an iron-sulfur
cluster to lipoate synthase (PubMed:24334290). Required for normal
iron homeostasis. Required for normal regulation of hemoglobin
synthesis by the iron-sulfur protein ACO1 (PubMed:20364084). May
protect cells against apoptosis due to reactive oxygen species and
oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q80Y14,
ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:24334290}.
-!- SUBUNIT: Homodimer (PubMed:21029046). Interacts with ISCU
(PubMed:26100117). Interacts with BOLA1 (PubMed:27532773,
PubMed:27532772). {ECO:0000269|PubMed:26100117,
ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773,
ECO:0000305|PubMed:21029046}.
-!- INTERACTION:
Q8IWL3:HSCB; NbExp=3; IntAct=EBI-1049910, EBI-1805738;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:20364084}.
-!- DISEASE: Anemia, sideroblastic, 3, pyridoxine-refractory (SIDBA3)
[MIM:616860]: A form of sideroblastic anemia, a bone marrow
disorder defined by the presence of pathologic iron deposits in
erythroblast mitochondria. Sideroblastic anemia is characterized
by anemia of varying severity, hypochromic peripheral
erythrocytes, systemic iron overload secondary to chronic
ineffective erythropoiesis, and the presence of bone marrow ringed
sideroblasts. Sideroblasts are characterized by iron-loaded
mitochondria clustered around the nucleus. SIDBA3 is refractory to
treatment with vitamin B6, while iron chelation therapy may result
in clinical improvement. SIDBA3 inheritance is autosomal
recessive. {ECO:0000269|PubMed:17485548,
ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:25342667,
ECO:0000269|PubMed:26100117}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spasticity, childhood-onset, with hyperglycinemia
(SPAHGC) [MIM:616859]: An autosomal recessive disorder
characterized by childhood-onset of spasticity, spinal lesions,
leukodystrophy, optic atrophy in some patients, non-ketotic
hyperglycinemia, and defective enzymatic glycine cleavage. Glycine
levels in the cerebrospinal fluid are mildly increased in some but
not all patients. The increase is less pronounced than in patients
with classic non-ketotic hyperglycinemia.
{ECO:0000269|PubMed:24334290}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD62364.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; DQ083331; AAZ30731.1; -; mRNA.
EMBL; BX248075; CAD62364.1; ALT_INIT; mRNA.
EMBL; AB223038; BAF02301.1; -; mRNA.
EMBL; CH471061; EAW81607.1; -; Genomic_DNA.
EMBL; BC023528; AAH23528.2; -; mRNA.
EMBL; BC047680; AAH47680.1; -; mRNA.
CCDS; CCDS9936.1; -.
RefSeq; NP_057501.2; NM_016417.2.
UniGene; Hs.744943; -.
PDB; 2MMZ; NMR; -; A=35-150.
PDB; 2WUL; X-ray; 2.40 A; A/B/C/D=35-150.
PDBsum; 2MMZ; -.
PDBsum; 2WUL; -.
ProteinModelPortal; Q86SX6; -.
SMR; Q86SX6; -.
BioGrid; 119386; 22.
DIP; DIP-50654N; -.
IntAct; Q86SX6; 3.
STRING; 9606.ENSP00000328570; -.
iPTMnet; Q86SX6; -.
PhosphoSitePlus; Q86SX6; -.
BioMuta; GLRX5; -.
DMDM; 83288163; -.
EPD; Q86SX6; -.
MaxQB; Q86SX6; -.
PaxDb; Q86SX6; -.
PeptideAtlas; Q86SX6; -.
PRIDE; Q86SX6; -.
TopDownProteomics; Q86SX6; -.
Ensembl; ENST00000331334; ENSP00000328570; ENSG00000182512.
GeneID; 51218; -.
KEGG; hsa:51218; -.
UCSC; uc001yem.2; human.
CTD; 51218; -.
DisGeNET; 51218; -.
EuPathDB; HostDB:ENSG00000182512.4; -.
GeneCards; GLRX5; -.
HGNC; HGNC:20134; GLRX5.
HPA; HPA042465; -.
HPA; HPA063716; -.
MalaCards; GLRX5; -.
MIM; 609588; gene.
MIM; 616859; phenotype.
MIM; 616860; phenotype.
neXtProt; NX_Q86SX6; -.
OpenTargets; ENSG00000182512; -.
Orphanet; 255132; Adult-onset autosomal recessive sideroblastic anemia.
Orphanet; 401866; Spasticity-ataxia-gait anomalies syndrome.
PharmGKB; PA134992547; -.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
GeneTree; ENSGT00550000075082; -.
HOGENOM; HOG000095211; -.
HOVERGEN; HBG051012; -.
InParanoid; Q86SX6; -.
KO; K07390; -.
OMA; KGTKLMP; -.
OrthoDB; EOG091G0YN0; -.
PhylomeDB; Q86SX6; -.
TreeFam; TF318988; -.
Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
EvolutionaryTrace; Q86SX6; -.
GeneWiki; GLRX5; -.
GenomeRNAi; 51218; -.
PRO; PR:Q86SX6; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000182512; -.
CleanEx; HS_GLRX5; -.
ExpressionAtlas; Q86SX6; baseline and differential.
Genevisible; Q86SX6; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
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; IMP:UniProtKB.
GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
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; 3D-structure; Complete proteome; Disease mutation; Iron;
Iron-sulfur; Metal-binding; Mitochondrion; Phosphoprotein;
Polymorphism; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 31 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000255}.
CHAIN 32 157 Glutaredoxin-related protein 5,
mitochondrial.
/FTId=PRO_0000141650.
DOMAIN 42 145 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 97 101 Glutathione binding.
{ECO:0000269|PubMed:21029046}.
REGION 122 123 Glutathione binding.
{ECO:0000269|PubMed:21029046}.
COMPBIAS 8 11 Poly-Ala.
COMPBIAS 16 23 Poly-Gly.
COMPBIAS 33 40 Poly-Gly.
METAL 67 67 Iron-sulfur (2Fe-2S); shared with dimeric
partner.
BINDING 59 59 Glutathione.
{ECO:0000269|PubMed:21029046}.
BINDING 109 109 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:21029046}.
MOD_RES 59 59 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q80Y14}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Y14}.
VARIANT 51 51 Missing (in SPAHGC; no effect on protein
abundance in patient cells; probably
reduced activity in iron-sulfur cluster
assembly that results in reduced
production of the lipoate cofactor and
protein lipoylation).
{ECO:0000269|PubMed:24334290,
ECO:0000305}.
/FTId=VAR_076672.
VARIANT 101 101 K -> Q (in SIDBA3; deficiency in Fe-S
cluster synthesis; does not impair ISCU
binding; dbSNP:rs869312752).
{ECO:0000269|PubMed:25342667,
ECO:0000269|PubMed:26100117}.
/FTId=VAR_074550.
VARIANT 146 146 A -> T (in dbSNP:rs11628901).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16110529}.
/FTId=VAR_026125.
VARIANT 148 148 L -> S (in SIDBA3; deficiency in Fe-S
cluster synthesis; does not impair ISCU
binding; dbSNP:rs765487627).
{ECO:0000269|PubMed:25342667,
ECO:0000269|PubMed:26100117}.
/FTId=VAR_074551.
HELIX 42 51 {ECO:0000244|PDB:2WUL}.
STRAND 52 60 {ECO:0000244|PDB:2WUL}.
STRAND 62 67 {ECO:0000244|PDB:2WUL}.
HELIX 68 79 {ECO:0000244|PDB:2WUL}.
STRAND 86 89 {ECO:0000244|PDB:2WUL}.
HELIX 94 104 {ECO:0000244|PDB:2WUL}.
STRAND 111 114 {ECO:0000244|PDB:2WUL}.
STRAND 117 120 {ECO:0000244|PDB:2WUL}.
HELIX 122 131 {ECO:0000244|PDB:2WUL}.
HELIX 133 140 {ECO:0000244|PDB:2WUL}.
TURN 146 148 {ECO:0000244|PDB:2WUL}.
SEQUENCE 157 AA; 16628 MW; 5E6873BD5DE91F86 CRC64;
MSGSLGRAAA ALLRWGRGAG GGGLWGPGVR AAGSGAGGGG SAEQLDALVK KDKVVVFLKG
TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG
GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK


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