ETHE1_HUMAN
ID ETHE1_HUMAN Reviewed; 254 AA.
AC O95571; Q96HR0; Q9H001;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Persulfide dioxygenase ETHE1, mitochondrial;
DE EC=1.13.11.18 {ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459, ECO:0000269|PubMed:25596185};
DE AltName: Full=Ethylmalonic encephalopathy protein 1;
DE AltName: Full=Hepatoma subtracted clone one protein;
DE AltName: Full=Sulfur dioxygenase ETHE1;
DE Flags: Precursor;
GN Name=ETHE1; Synonyms=HSCO;
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], SUBCELLULAR LOCATION, INTERACTION WITH RELA,
RP FUNCTION, AND ABSENCE OF GLYOXALASE II ACTIVITY.
RC TISSUE=Liver;
RX PubMed=12398897; DOI=10.1016/s1535-6108(02)00152-6;
RA Higashitsuji H., Higashitsuji H., Nagao T., Nonoguchi K., Fujii S.,
RA Itoh K., Fujita J.;
RT "A novel protein overexpressed in hepatoma accelerates export of NF-kappa B
RT from the nucleus and inhibits p53-dependent apoptosis.";
RL Cancer Cell 2:335-346(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP FUNCTION, ABSENCE OF GLYOXALASE II ACTIVITY, AND VARIANTS EE CYS-38;
RP ALA-136; TRP-163 AND ARG-185.
RX PubMed=14732903; DOI=10.1086/381653;
RA Tiranti V., D'Adamo P., Briem E., Ferrari G., Mineri R., Lamantea E.,
RA Mandel H., Balestri P., Garcia-Silva M.-T., Vollmer B., Rinaldo P.,
RA Hahn S.H., Leonard J., Rahman S., Dionisi-Vici C., Garavaglia B.,
RA Gasparini P., Zeviani M.;
RT "Ethylmalonic encephalopathy is caused by mutations in ETHE1, a gene
RT encoding a mitochondrial matrix protein.";
RL Am. J. Hum. Genet. 74:239-252(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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, CATALYTIC ACTIVITY, COFACTOR, ROLE IN DISEASE, SUBCELLULAR
RP LOCATION, TRANSIT PEPTIDE CLEAVAGE SITE, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH TST.
RX PubMed=19136963; DOI=10.1038/nm.1907;
RA Tiranti V., Viscomi C., Hildebrandt T., Di Meo I., Mineri R., Tiveron C.,
RA Levitt M.D., Prelle A., Fagiolari G., Rimoldi M., Zeviani M.;
RT "Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity
RT in ethylmalonic encephalopathy.";
RL Nat. Med. 15:200-205(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, ACTIVITY REGULATION, AND CHARACTERIZATION OF VARIANTS EE ILE-152
RP AND ASN-196.
RX PubMed=23144459; DOI=10.1074/jbc.m112.407411;
RA Kabil O., Banerjee R.;
RT "Characterization of patient mutations in human persulfide dioxygenase
RT (ETHE1) involved in H2S catabolism.";
RL J. Biol. Chem. 287:44561-44567(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
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 [11] {ECO:0007744|PDB:4CHL}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 21-254 IN COMPLEX WITH IRON,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=25596185; DOI=10.1093/hmg/ddv007;
RA Pettinati I., Brem J., McDonough M.A., Schofield C.J.;
RT "Crystal structure of human persulfide dioxygenase: structural basis of
RT ethylmalonic encephalopathy.";
RL Hum. Mol. Genet. 24:2458-2469(2015).
RN [12]
RP VARIANTS EE PRO-55; ALA-136; ILE-152; GLN-163; TRP-163; LYS-164; ARG-185
RP AND ASN-196, AND CHARACTERIZATION OF VARIANTS EE PRO-55 AND LYS-164.
RX PubMed=18593870; DOI=10.1136/jmg.2008.058271;
RA Mineri R., Rimoldi M., Burlina A.B., Koskull S., Perletti C., Heese B.,
RA von Dobeln U., Mereghetti P., Di Meo I., Invernizzi F., Zeviani M.,
RA Uziel G., Tiranti V.;
RT "Identification of new mutations in the ETHE1 gene in a cohort of 14
RT patients presenting with ethylmalonic encephalopathy.";
RL J. Med. Genet. 45:473-478(2008).
CC -!- FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen
CC sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide
CC (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide
CC residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of
CC the persulfide, once it has been transferred to a thiophilic acceptor,
CC such as glutathione (R-SSH). Plays an important role in metabolic
CC homeostasis in mitochondria by metabolizing hydrogen sulfide and
CC preventing the accumulation of supraphysiological H(2)S levels that
CC have toxic effects, due to the inhibition of cytochrome c oxidase.
CC First described as a protein that can shuttle between the nucleus and
CC the cytoplasm and suppress p53-induced apoptosis by sequestering the
CC transcription factor RELA/NFKB3 in the cytoplasm and preventing its
CC accumulation in the nucleus (PubMed:12398897).
CC {ECO:0000269|PubMed:12398897, ECO:0000269|PubMed:14732903,
CC ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) +
CC sulfite; Xref=Rhea:RHEA:12981, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905; EC=1.13.11.18;
CC Evidence={ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459,
CC ECO:0000269|PubMed:25596185};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459,
CC ECO:0000269|PubMed:25596185};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:19136963,
CC ECO:0000269|PubMed:23144459, ECO:0000269|PubMed:25596185};
CC -!- ACTIVITY REGULATION: Glutathione increases enzyme activity.
CC {ECO:0000269|PubMed:23144459}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for glutathione persulfide (GSSH)
CC {ECO:0000269|PubMed:23144459};
CC Vmax=113 umol/min/mg enzyme (in the presence of equimolar amounts of
CC GSSH and GSH and at 22 degrees Celsius)
CC {ECO:0000269|PubMed:23144459};
CC -!- SUBUNIT: Homodimer (PubMed:25596185). Monomer (PubMed:23144459).
CC Interacts with TST (PubMed:19136963). May interact with RELA
CC (PubMed:12398897). {ECO:0000269|PubMed:12398897,
CC ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459,
CC ECO:0000269|PubMed:25596185}.
CC -!- INTERACTION:
CC O95571; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-715318, EBI-12006308;
CC O95571; O95571: ETHE1; NbExp=3; IntAct=EBI-715318, EBI-715318;
CC O95571; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-715318, EBI-739467;
CC O95571; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-715318, EBI-12196745;
CC O95571; Q99757: TXN2; NbExp=3; IntAct=EBI-715318, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12398897}. Nucleus
CC {ECO:0000269|PubMed:12398897}. Mitochondrion matrix
CC {ECO:0000269|PubMed:14732903}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14732903}.
CC -!- DISEASE: Ethylmalonic encephalopathy (EE) [MIM:602473]: Autosomal
CC recessive disorder characterized by neurodevelopmental delay and
CC regression, recurrent petechiae, acrocyanosis, diarrhea, leading to
CC death in the first decade of life. It is also associated with
CC persistent lactic acidemia and ethylmalonic and methylsuccinic
CC aciduria. {ECO:0000269|PubMed:14732903, ECO:0000269|PubMed:18593870,
CC ECO:0000269|PubMed:23144459}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09063.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D83198; BAA34595.2; -; mRNA.
DR EMBL; AC018758; AAG09063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC008250; AAH08250.1; -; mRNA.
DR CCDS; CCDS12622.1; -.
DR RefSeq; NP_001307796.1; NM_001320867.1.
DR RefSeq; NP_001307797.1; NM_001320868.1.
DR RefSeq; NP_001307798.1; NM_001320869.1.
DR RefSeq; NP_055112.2; NM_014297.4.
DR RefSeq; XP_005258744.1; XM_005258687.3.
DR PDB; 4CHL; X-ray; 2.61 A; A/B=21-254.
DR PDBsum; 4CHL; -.
DR AlphaFoldDB; O95571; -.
DR SASBDB; O95571; -.
DR SMR; O95571; -.
DR BioGRID; 117034; 48.
DR IntAct; O95571; 12.
DR MINT; O95571; -.
DR STRING; 9606.ENSP00000292147; -.
DR iPTMnet; O95571; -.
DR MetOSite; O95571; -.
DR PhosphoSitePlus; O95571; -.
DR SwissPalm; O95571; -.
DR BioMuta; ETHE1; -.
DR UCD-2DPAGE; O95571; -.
DR EPD; O95571; -.
DR jPOST; O95571; -.
DR MassIVE; O95571; -.
DR MaxQB; O95571; -.
DR PaxDb; O95571; -.
DR PeptideAtlas; O95571; -.
DR PRIDE; O95571; -.
DR ProteomicsDB; 50945; -.
DR Antibodypedia; 31059; 267 antibodies from 26 providers.
DR DNASU; 23474; -.
DR Ensembl; ENST00000292147.7; ENSP00000292147.1; ENSG00000105755.8.
DR GeneID; 23474; -.
DR KEGG; hsa:23474; -.
DR MANE-Select; ENST00000292147.7; ENSP00000292147.1; NM_014297.5; NP_055112.2.
DR UCSC; uc002owp.3; human.
DR CTD; 23474; -.
DR DisGeNET; 23474; -.
DR GeneCards; ETHE1; -.
DR GeneReviews; ETHE1; -.
DR HGNC; HGNC:23287; ETHE1.
DR HPA; ENSG00000105755; Tissue enhanced (intestine).
DR MalaCards; ETHE1; -.
DR MIM; 602473; phenotype.
DR MIM; 608451; gene.
DR neXtProt; NX_O95571; -.
DR OpenTargets; ENSG00000105755; -.
DR Orphanet; 51188; Ethylmalonic encephalopathy.
DR PharmGKB; PA134879650; -.
DR VEuPathDB; HostDB:ENSG00000105755; -.
DR eggNOG; KOG0814; Eukaryota.
DR GeneTree; ENSGT00940000159046; -.
DR HOGENOM; CLU_030571_7_0_1; -.
DR InParanoid; O95571; -.
DR OMA; DYKGDTV; -.
DR OrthoDB; 1203911at2759; -.
DR PhylomeDB; O95571; -.
DR TreeFam; TF312952; -.
DR BioCyc; MetaCyc:ENSG00000105755-MON; -.
DR PathwayCommons; O95571; -.
DR Reactome; R-HSA-1614517; Sulfide oxidation to sulfate.
DR SABIO-RK; O95571; -.
DR SignaLink; O95571; -.
DR BioGRID-ORCS; 23474; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; ETHE1; human.
DR GeneWiki; ETHE1; -.
DR GenomeRNAi; 23474; -.
DR Pharos; O95571; Tbio.
DR PRO; PR:O95571; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95571; protein.
DR Bgee; ENSG00000105755; Expressed in mucosa of transverse colon and 192 other tissues.
DR ExpressionAtlas; O95571; baseline and differential.
DR Genevisible; O95571; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0070813; P:hydrogen sulfide metabolic process; IDA:UniProtKB.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Dioxygenase; Disease variant; Iron;
KW Metal-binding; Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..7
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19136963"
FT CHAIN 8..254
FT /note="Persulfide dioxygenase ETHE1, mitochondrial"
FT /id="PRO_0000012289"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25596185,
FT ECO:0007744|PDB:4CHL"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25596185,
FT ECO:0007744|PDB:4CHL"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25596185,
FT ECO:0007744|PDB:4CHL"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 172
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT MOD_RES 172
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT VARIANT 38
FT /note="Y -> C (in EE; dbSNP:rs1555765564)"
FT /evidence="ECO:0000269|PubMed:14732903"
FT /id="VAR_023395"
FT VARIANT 55
FT /note="L -> P (in EE; reduces protein stability;
FT dbSNP:rs182983506)"
FT /evidence="ECO:0000269|PubMed:18593870"
FT /id="VAR_069507"
FT VARIANT 136
FT /note="T -> A (in EE; dbSNP:rs1284200516)"
FT /evidence="ECO:0000269|PubMed:14732903,
FT ECO:0000269|PubMed:18593870"
FT /id="VAR_023396"
FT VARIANT 152
FT /note="T -> I (in EE; reduces protein stability, iron
FT content and enzyme activity; dbSNP:rs1317633085)"
FT /evidence="ECO:0000269|PubMed:18593870,
FT ECO:0000269|PubMed:23144459"
FT /id="VAR_069508"
FT VARIANT 163
FT /note="R -> Q (in EE; dbSNP:rs745656120)"
FT /evidence="ECO:0000269|PubMed:18593870"
FT /id="VAR_069509"
FT VARIANT 163
FT /note="R -> W (in EE; dbSNP:rs28940289)"
FT /evidence="ECO:0000269|PubMed:14732903,
FT ECO:0000269|PubMed:18593870"
FT /id="VAR_023397"
FT VARIANT 164
FT /note="T -> K (in EE; reduces protein stability;
FT dbSNP:rs1268640442)"
FT /evidence="ECO:0000269|PubMed:18593870"
FT /id="VAR_069510"
FT VARIANT 185
FT /note="L -> R (in EE; dbSNP:rs387906987)"
FT /evidence="ECO:0000269|PubMed:14732903,
FT ECO:0000269|PubMed:18593870"
FT /id="VAR_023398"
FT VARIANT 196
FT /note="D -> N (in EE; reduces protein stability and
FT affinity for substrate; dbSNP:rs763799125)"
FT /evidence="ECO:0000269|PubMed:18593870,
FT ECO:0000269|PubMed:23144459"
FT /id="VAR_069511"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:4CHL"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4CHL"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4CHL"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4CHL"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:4CHL"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:4CHL"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:4CHL"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4CHL"
SQ SEQUENCE 254 AA; 27873 MW; 52073D52A487ACD4 CRC64;
MAEAVLRVAR RQLSQRGGSG APILLRQMFE PVSCTFTYLL GDRESREAVL IDPVLETAPR
DAQLIKELGL RLLYAVNTHC HADHITGSGL LRSLLPGCQS VISRLSGAQA DLHIEDGDSI
RFGRFALETR ASPGHTPGCV TFVLNDHSMA FTGDALLIRG CGRTDFQQGC AKTLYHSVHE
KIFTLPGDCL IYPAHDYHGF TVSTVEEERT LNPRLTLSCE EFVKIMGNLN LPKPQQIDFA
VPANMRCGVQ TPTA
