GLRX5_DANRE
ID GLRX5_DANRE Reviewed; 155 AA.
AC Q6PBM1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glutaredoxin-related protein 5, mitochondrial;
DE AltName: Full=Monothiol glutaredoxin-5;
DE Flags: Precursor;
GN Name=glrx5; Synonyms=grx5, shiraz; ORFNames=si:ch211-121d13.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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.;
RL Nature 437:920-920(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (PubMed:16110529). Receives iron-sulfur
CC clusters from scaffold protein ISCU and mediates their transfer to
CC apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export
CC from mitochondrion (PubMed:16110529). Required for normal hemoglobin
CC biosynthesis (PubMed:16110529). {ECO:0000269|PubMed:16110529}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86SX6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16110529}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic intermediate cell mass (site
CC of hematopoiesis), liver and heart.
CC -!- DISRUPTION PHENOTYPE: Lethal between 7 and 10 dpf. Embryos show
CC hypochromia, and circulating blood cells are pale due to a defect in
CC hemoglobin biosynthesis. {ECO:0000269|PubMed:16110529}.
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DR EMBL; DQ083329; AAZ30729.1; -; mRNA.
DR EMBL; AL845550; CAI11571.1; -; Genomic_DNA.
DR EMBL; BC059659; AAH59659.1; -; mRNA.
DR RefSeq; NP_998186.1; NM_213021.1.
DR AlphaFoldDB; Q6PBM1; -.
DR SMR; Q6PBM1; -.
DR STRING; 7955.ENSDARP00000064111; -.
DR PaxDb; Q6PBM1; -.
DR Ensembl; ENSDART00000064112; ENSDARP00000064111; ENSDARG00000043665.
DR GeneID; 406294; -.
DR KEGG; dre:406294; -.
DR CTD; 51218; -.
DR ZFIN; ZDB-GENE-040426-1957; glrx5.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075082; -.
DR HOGENOM; CLU_026126_2_0_1; -.
DR InParanoid; Q6PBM1; -.
DR OMA; GCDILMQ; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q6PBM1; -.
DR TreeFam; TF318988; -.
DR Reactome; R-DRE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q6PBM1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000043665; Expressed in mature ovarian follicle and 30 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:ZFIN.
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:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:ZFIN.
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 2: Evidence at transcript level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..155
FT /note="Glutaredoxin-related protein 5, mitochondrial"
FT /id="PRO_0000392601"
FT DOMAIN 42..145
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 67
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 97..101
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 109
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
FT BINDING 122..123
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q86SX6"
SQ SEQUENCE 155 AA; 17377 MW; F0B356FA69AAEA27 CRC64;
MNSVFRSTAR CLRSATWQYK TAHKNGELSV GRARLMCSSA GQKNLEEMVK KDKVVVFMKG
TPAQPMCGFS NAVVQILRMH GVDNYASYNV LDDQDVRQGI KTFSNWPTIP QVFFNGEFVG
GCDILLQMHQ SGDLVEELQK LGIRSALLDQ EKESK
