GLRX5_HUMAN
ID GLRX5_HUMAN Reviewed; 157 AA.
AC Q86SX6; Q0X088; Q3YML0; Q86WY3; Q8IZ54;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Glutaredoxin-related protein 5, mitochondrial;
DE AltName: Full=Monothiol glutaredoxin-5;
DE Flags: Precursor;
GN Name=GLRX5; Synonyms=C14orf87;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-146.
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 [MRNA].
RA Kurosawa N., Isobe M., Saito M.;
RT "Biological function of human glutaredoxin 3 (Grx 3), a novel mitochondrial
RT monothiol Grx.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-146.
RC TISSUE=Skin, and Testis;
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 [7]
RP INVOLVEMENT IN SIDBA3.
RX PubMed=17485548; DOI=10.1182/blood-2007-02-072520;
RA Camaschella C., Campanella A., De Falco L., Boschetto L., Merlini R.,
RA Silvestri L., Levi S., Iolascon A.;
RT "The human counterpart of zebrafish shiraz shows sideroblastic-like
RT microcytic anemia and iron overload.";
RL Blood 110:1353-1358(2007).
RN [8]
RP INVOLVEMENT IN SIDBA3, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20364084; DOI=10.1172/jci40372;
RA Ye H., Jeong S.Y., Ghosh M.C., Kovtunovych G., Silvestri L., Ortillo D.,
RA Uchida N., Tisdale J., Camaschella C., Rouault T.A.;
RT "Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically
RT impairing heme biosynthesis and depleting cytosolic iron in human
RT erythroblasts.";
RL J. Clin. Invest. 120:1749-1761(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION.
RX PubMed=23615440; DOI=10.1091/mbc.e12-09-0644;
RA Uzarska M.A., Dutkiewicz R., Freibert S.A., Lill R., Muehlenhoff U.;
RT "The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer
RT from Isu1 to Grx5 by complex formation.";
RL Mol. Biol. Cell 24:1830-1841(2013).
RN [11]
RP FUNCTION, INVOLVEMENT IN SPAHGC, VARIANT SPAHGC LYS-51 DEL, AND
RP CHARACTERIZATION OF VARIANT SPAHGC LYS-51 DEL.
RX PubMed=24334290; DOI=10.1093/brain/awt328;
RA Baker P.R. II, Friederich M.W., Swanson M.A., Shaikh T., Bhattacharya K.,
RA Scharer G.H., Aicher J., Creadon-Swindell G., Geiger E., MacLean K.N.,
RA Lee W.T., Deshpande C., Freckmann M.L., Shih L.Y., Wasserstein M.,
RA Rasmussen M.B., Lund A.M., Procopis P., Cameron J.M., Robinson B.H.,
RA Brown G.K., Brown R.M., Compton A.G., Dieckmann C.L., Collard R.,
RA Coughlin C.R. II, Spector E., Wempe M.F., Van Hove J.L.;
RT "Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3
RT and the novel gene GLRX5.";
RL Brain 137:366-379(2014).
RN [12]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-31, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP INTERACTION WITH BOLA1.
RX PubMed=27532773; DOI=10.7554/elife.15991;
RA Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A.,
RA Winge D.R.;
RT "Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial
RT clients.";
RL Elife 5:0-0(2016).
RN [14]
RP INTERACTION WITH BOLA1.
RX PubMed=27532772; DOI=10.7554/elife.16673;
RA Uzarska M.A., Nasta V., Weiler B.D., Spantgar F., Ciofi-Baffoni S.,
RA Saviello M.R., Gonnelli L., Muehlenhoff U., Banci L., Lill R.;
RT "Mitochondrial Bol1 and Bol3 function as assembly factors for specific
RT iron-sulfur proteins.";
RL Elife 5:0-0(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-150 IN COMPLEX WITH GLUTATHIONE
RP AND IRON-SULFUR CLUSTER, AND SUBUNIT.
RX PubMed=21029046; DOI=10.1042/bj20101286;
RA Johansson C., Roos A.K., Montano S.J., Sengupta R., Filippakopoulos P.,
RA Guo K., von Delft F., Holmgren A., Oppermann U., Kavanagh K.L.;
RT "The crystal structure of human GLRX5: iron-sulfur cluster co-ordination,
RT tetrameric assembly and monomer activity.";
RL Biochem. J. 433:303-311(2011).
RN [16]
RP VARIANTS SIDBA3 GLN-101 AND SER-148.
RX PubMed=25342667; DOI=10.1182/blood-2014-08-598508;
RA Liu G., Guo S., Anderson G.J., Camaschella C., Han B., Nie G.;
RT "Heterozygous missense mutations in the GLRX5 gene cause sideroblastic
RT anemia in a Chinese patient.";
RL Blood 124:2750-2751(2014).
RN [17]
RP CHARACTERIZATION OF VARIANTS SIDBA3 GLN-101 AND SER-148, AND INTERACTION
RP WITH ISCU.
RX PubMed=26100117; DOI=10.1002/jcb.25267;
RA Liu G., Wang Y., Anderson G.J., Camaschella C., Chang Y., Nie G.;
RT "Functional analysis of GLRX5 mutants reveals distinct functionalities of
RT GLRX5 protein.";
RL J. Cell. Biochem. 117:207-217(2016).
CC -!- FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur
CC (Fe/S) cluster transfer (PubMed:20364084, PubMed:23615440). Receives
CC 2Fe/2S clusters from scaffold protein ISCU and mediates their transfer
CC to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export
CC from mitochondrion (PubMed:20364084, PubMed:23615440, PubMed:24334290).
CC Required for normal regulation of hemoglobin synthesis by the iron-
CC sulfur protein ACO1 (PubMed:20364084). {ECO:0000269|PubMed:20364084,
CC ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:24334290}.
CC -!- SUBUNIT: Homodimer (PubMed:21029046). Interacts with ISCU
CC (PubMed:26100117). Interacts with BOLA1 (PubMed:27532773,
CC PubMed:27532772). {ECO:0000269|PubMed:26100117,
CC ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773,
CC ECO:0000305|PubMed:21029046}.
CC -!- INTERACTION:
CC Q86SX6; Q53S33: BOLA3; NbExp=7; IntAct=EBI-1049910, EBI-12086950;
CC Q86SX6; Q8IWL3: HSCB; NbExp=3; IntAct=EBI-1049910, EBI-1805738;
CC PRO_0000141650; Q9Y3E2: BOLA1; NbExp=6; IntAct=EBI-27823755, EBI-1049556;
CC PRO_0000141650; Q53S33: BOLA3; NbExp=5; IntAct=EBI-27823755, EBI-12086950;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:20364084}.
CC -!- DISEASE: Anemia, sideroblastic, 3, pyridoxine-refractory (SIDBA3)
CC [MIM:616860]: A form of sideroblastic anemia, a bone marrow disorder
CC defined by the presence of pathologic iron deposits in erythroblast
CC mitochondria. Sideroblastic anemia is characterized by anemia of
CC varying severity, hypochromic peripheral erythrocytes, systemic iron
CC overload secondary to chronic ineffective erythropoiesis, and the
CC presence of bone marrow ringed sideroblasts. Sideroblasts are
CC characterized by iron-loaded mitochondria clustered around the nucleus.
CC SIDBA3 is refractory to treatment with vitamin B6, while iron chelation
CC therapy may result in clinical improvement. SIDBA3 inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:17485548,
CC ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:25342667,
CC ECO:0000269|PubMed:26100117}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spasticity, childhood-onset, with hyperglycinemia (SPAHGC)
CC [MIM:616859]: An autosomal recessive disorder characterized by
CC childhood-onset of spasticity, spinal lesions, leukodystrophy, optic
CC atrophy in some patients, non-ketotic hyperglycinemia, and defective
CC enzymatic glycine cleavage. Glycine levels in the cerebrospinal fluid
CC are mildly increased in some but not all patients. The increase is less
CC pronounced than in patients with classic non-ketotic hyperglycinemia.
CC {ECO:0000269|PubMed:24334290}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62364.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ083331; AAZ30731.1; -; mRNA.
DR EMBL; BX248075; CAD62364.1; ALT_INIT; mRNA.
DR EMBL; AB223038; BAF02301.1; -; mRNA.
DR EMBL; CH471061; EAW81607.1; -; Genomic_DNA.
DR EMBL; BC023528; AAH23528.2; -; mRNA.
DR EMBL; BC047680; AAH47680.1; -; mRNA.
DR CCDS; CCDS9936.1; -.
DR RefSeq; NP_057501.2; NM_016417.2.
DR PDB; 2MMZ; NMR; -; A=35-150.
DR PDB; 2WUL; X-ray; 2.40 A; A/B/C/D=35-150.
DR PDBsum; 2MMZ; -.
DR PDBsum; 2WUL; -.
DR AlphaFoldDB; Q86SX6; -.
DR BMRB; Q86SX6; -.
DR SMR; Q86SX6; -.
DR BioGRID; 119386; 75.
DR ComplexPortal; CPX-6862; Mitochondrial BOLA1-GLRX5 iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-6863; Mitochondrial BOLA3-GLRX5 iron-sulfur cluster assembly complex.
DR DIP; DIP-50654N; -.
DR IntAct; Q86SX6; 18.
DR MINT; Q86SX6; -.
DR STRING; 9606.ENSP00000328570; -.
DR iPTMnet; Q86SX6; -.
DR PhosphoSitePlus; Q86SX6; -.
DR BioMuta; GLRX5; -.
DR DMDM; 83288163; -.
DR EPD; Q86SX6; -.
DR jPOST; Q86SX6; -.
DR MassIVE; Q86SX6; -.
DR MaxQB; Q86SX6; -.
DR PaxDb; Q86SX6; -.
DR PeptideAtlas; Q86SX6; -.
DR PRIDE; Q86SX6; -.
DR ProteomicsDB; 69646; -.
DR TopDownProteomics; Q86SX6; -.
DR Antibodypedia; 47425; 150 antibodies from 25 providers.
DR DNASU; 51218; -.
DR Ensembl; ENST00000331334.5; ENSP00000328570.4; ENSG00000182512.5.
DR GeneID; 51218; -.
DR KEGG; hsa:51218; -.
DR MANE-Select; ENST00000331334.5; ENSP00000328570.4; NM_016417.3; NP_057501.2.
DR UCSC; uc001yem.2; human.
DR CTD; 51218; -.
DR DisGeNET; 51218; -.
DR GeneCards; GLRX5; -.
DR HGNC; HGNC:20134; GLRX5.
DR HPA; ENSG00000182512; Tissue enhanced (skeletal).
DR MalaCards; GLRX5; -.
DR MIM; 609588; gene.
DR MIM; 616859; phenotype.
DR MIM; 616860; phenotype.
DR neXtProt; NX_Q86SX6; -.
DR OpenTargets; ENSG00000182512; -.
DR Orphanet; 255132; Adult-onset autosomal recessive sideroblastic anemia.
DR Orphanet; 401866; Childhood-onset spasticity with hyperglycinemia.
DR PharmGKB; PA134992547; -.
DR VEuPathDB; HostDB:ENSG00000182512; -.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075082; -.
DR HOGENOM; CLU_026126_2_0_1; -.
DR InParanoid; Q86SX6; -.
DR OMA; GCDILMQ; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q86SX6; -.
DR TreeFam; TF318988; -.
DR PathwayCommons; Q86SX6; -.
DR Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR SignaLink; Q86SX6; -.
DR BioGRID-ORCS; 51218; 341 hits in 1082 CRISPR screens.
DR EvolutionaryTrace; Q86SX6; -.
DR GeneWiki; GLRX5; -.
DR GenomeRNAi; 51218; -.
DR Pharos; Q86SX6; Tbio.
DR PRO; PR:Q86SX6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86SX6; protein.
DR Bgee; ENSG00000182512; Expressed in trabecular bone tissue and 204 other tissues.
DR ExpressionAtlas; Q86SX6; baseline and differential.
DR Genevisible; Q86SX6; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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; IGI:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IC:ComplexPortal.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IGI:UniProtKB.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IGI:UniProtKB.
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; 3D-structure; Disease variant; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Phosphoprotein; Redox-active center; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 32..157
FT /note="Glutaredoxin-related protein 5, mitochondrial"
FT /id="PRO_0000141650"
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:0000269|PubMed:21029046"
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:0000269|PubMed:21029046"
FT BINDING 97..101
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21029046"
FT BINDING 109
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21029046"
FT BINDING 122..123
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21029046"
FT MOD_RES 59
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y14"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y14"
FT VARIANT 51
FT /note="Missing (in SPAHGC; no effect on protein abundance
FT in patient cells; probably reduced activity in iron-sulfur
FT cluster assembly that results in reduced production of the
FT lipoate cofactor and protein lipoylation;
FT dbSNP:rs869320757)"
FT /evidence="ECO:0000269|PubMed:24334290, ECO:0000305"
FT /id="VAR_076672"
FT VARIANT 101
FT /note="K -> Q (in SIDBA3; deficiency in Fe-S cluster
FT synthesis; does not impair ISCU binding;
FT dbSNP:rs869312752)"
FT /evidence="ECO:0000269|PubMed:25342667,
FT ECO:0000269|PubMed:26100117"
FT /id="VAR_074550"
FT VARIANT 146
FT /note="A -> T (in dbSNP:rs11628901)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16110529"
FT /id="VAR_026125"
FT VARIANT 148
FT /note="L -> S (in SIDBA3; deficiency in Fe-S cluster
FT synthesis; does not impair ISCU binding;
FT dbSNP:rs765487627)"
FT /evidence="ECO:0000269|PubMed:25342667,
FT ECO:0000269|PubMed:26100117"
FT /id="VAR_074551"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2WUL"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:2WUL"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2WUL"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:2WUL"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2WUL"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2WUL"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2WUL"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2WUL"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2WUL"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:2WUL"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2WUL"
SQ SEQUENCE 157 AA; 16628 MW; 5E6873BD5DE91F86 CRC64;
MSGSLGRAAA ALLRWGRGAG GGGLWGPGVR AAGSGAGGGG SAEQLDALVK KDKVVVFLKG
TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG
GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK
