SQOR_HUMAN
ID SQOR_HUMAN Reviewed; 450 AA.
AC Q9Y6N5; Q9UQM8;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial {ECO:0000305};
DE Short=SQOR {ECO:0000312|HGNC:HGNC:20390};
DE EC=1.8.5.8 {ECO:0000269|PubMed:22852582};
DE AltName: Full=Sulfide dehydrogenase-like;
DE AltName: Full=Sulfide quinone oxidoreductase {ECO:0000312|HGNC:HGNC:20390};
DE Flags: Precursor;
GN Name=SQOR {ECO:0000312|HGNC:HGNC:20390};
GN Synonyms=SQRDL {ECO:0000312|HGNC:HGNC:20390}; ORFNames=CGI-44;
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].
RC TISSUE=Brain;
RX PubMed=10224084; DOI=10.1074/jbc.274.19.13250;
RA Vande Weghe J.G., Ow D.W.;
RT "A fission yeast gene for mitochondrial sulfide oxidation.";
RL J. Biol. Chem. 274:13250-13257(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-264.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=22852582; DOI=10.1021/bi300778t;
RA Jackson M.R., Melideo S.L., Jorns M.S.;
RT "Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen
RT sulfide metabolism and produces a sulfane sulfur metabolite.";
RL Biochemistry 51:6804-6815(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
RP KINETICS.
RX PubMed=25225291; DOI=10.1074/jbc.m114.602664;
RA Libiad M., Yadav P.K., Vitvitsky V., Martinov M., Banerjee R.;
RT "Organization of the human mitochondrial hydrogen sulfide oxidation
RT pathway.";
RL J. Biol. Chem. 289:30901-30910(2014).
RN [7]
RP IDENTIFICATION BY 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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ENZYME KINETICS.
RX PubMed=29715001; DOI=10.1021/acschembio.8b00258;
RA Landry A.P., Ballou D.P., Banerjee R.;
RT "Modulation of catalytic promiscuity during hydrogen sulfide oxidation.";
RL ACS Chem. Biol. 13:1651-1658(2018).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SQORD, VARIANT SQORD LYS-213,
RP AND CHARACTERIZATION OF VARIANT SQORD LYS-213.
RX PubMed=32160317; DOI=10.1002/jimd.12232;
RA Friederich M.W., Elias A.F., Kuster A., Laugwitz L., Larson A.A.,
RA Landry A.P., Ellwood-Digel L., Mirsky D.M., Dimmock D., Haven J., Jiang H.,
RA MacLean K.N., Styren K., Schoof J., Goujon L., Lefrancois T.,
RA Friederich M., Coughlin C.R. II, Banerjee R., Haack T.B., Van Hove J.L.K.;
RT "Pathogenic variants in SQOR encoding sulfide:quinone oxidoreductase are a
RT potentially treatable cause of Leigh disease.";
RL J. Inherit. Metab. Dis. 43:1024-1036(2020).
RN [11] {ECO:0007744|PDB:6MO6, ECO:0007744|PDB:6MP5}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 42-450 IN COMPLEX WITH FAD,
RP COFACTOR, ACTIVE SITE, AND DISULFIDE BOND.
RX PubMed=30905673; DOI=10.1016/j.str.2019.03.002;
RA Jackson M.R., Loll P.J., Jorns M.S.;
RT "X-ray structure of human sulfide:quinone oxidoreductase: insights into the
RT mechanism of mitochondrial hydrogen sulfide oxidation.";
RL Structure 27:794-805.e4(2019).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of
CC a quinone, such as ubiquinone-10, giving rise to thiosulfate and
CC ultimately to sulfane (molecular sulfur) atoms. Requires an additional
CC electron acceptor; can use sulfite, sulfide or cyanide (in vitro)
CC (PubMed:22852582). It is believed the in vivo electron acceptor is
CC glutathione (PubMed:25225291,PubMed:29715001).
CC {ECO:0000269|PubMed:22852582, ECO:0000269|PubMed:25225291,
CC ECO:0000269|PubMed:29715001, ECO:0000269|PubMed:32160317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 =
CC thiosulfate + ubiquinol-10; Xref=Rhea:RHEA:38359, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:33542,
CC ChEBI:CHEBI:46245, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000269|PubMed:22852582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38360;
CC Evidence={ECO:0000269|PubMed:22852582};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + glutathione + H(+) + hydrogen sulfide = a quinol +
CC S-sulfanylglutathione; Xref=Rhea:RHEA:55156, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29919, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905, ChEBI:CHEBI:132124; EC=1.8.5.8;
CC Evidence={ECO:0000269|PubMed:25225291, ECO:0000269|PubMed:29715001,
CC ECO:0000269|PubMed:32160317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55157;
CC Evidence={ECO:0000269|PubMed:25225291, ECO:0000269|PubMed:29715001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H(+) + hydrogen sulfide + ubiquinone-10 = S-
CC sulfanylglutathione + ubiquinol-10; Xref=Rhea:RHEA:62608,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, ChEBI:CHEBI:46245,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58905, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000269|PubMed:29715001};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62609;
CC Evidence={ECO:0000269|PubMed:29715001};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:22852582, ECO:0000269|PubMed:30905673};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22852582,
CC ECO:0000269|PubMed:30905673};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for sulfide (with sulfite as electron acceptor)
CC {ECO:0000269|PubMed:22852582};
CC KM=10 uM for sulfide (with glutathione as electron acceptor)
CC {ECO:0000269|PubMed:25225291};
CC KM=5 uM for sulfide (with cysteine as electron acceptor)
CC {ECO:0000269|PubMed:25225291};
CC KM=0.22 mM for sulfite {ECO:0000269|PubMed:25225291};
CC KM=22 mM for glutathione {ECO:0000269|PubMed:25225291};
CC KM=23 uM for cysteine {ECO:0000269|PubMed:25225291};
CC Vmax=476 umol/min/mg enzyme with sulfite as electron acceptor
CC {ECO:0000269|PubMed:25225291};
CC Vmax=144 umol/min/mg enzyme with glutathione as electron acceptor
CC {ECO:0000269|PubMed:25225291};
CC Vmax=120 umol/min/mg enzyme with cysteine as electron acceptor
CC {ECO:0000269|PubMed:25225291};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- DISEASE: Sulfide:quinone oxidoreductase deficiency (SQORD)
CC [MIM:619221]: An autosomal recessive disorder of hydrogen sulfide
CC metabolism characterized by a variable phenotype. Some patients present
CC with encephalopathy, clinical manifestations of Leigh syndrome, and may
CC have a fatal disease course. Others are asymptomatic. Additional
CC features may include lactic acidosis and decreased mitochondrial
CC respiratory chain complex IV activity in tissues.
CC {ECO:0000269|PubMed:32160317}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
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DR EMBL; AF042284; AAD41160.1; -; mRNA.
DR EMBL; AF151802; AAD34039.1; -; mRNA.
DR EMBL; BC016836; AAH16836.1; -; mRNA.
DR CCDS; CCDS10127.1; -.
DR RefSeq; NP_001258142.1; NM_001271213.1.
DR RefSeq; NP_067022.1; NM_021199.3.
DR PDB; 6MO6; X-ray; 2.59 A; A/B/C/D=42-450.
DR PDB; 6MP5; X-ray; 2.99 A; A/B/C/D=42-450.
DR PDB; 6OI5; X-ray; 2.81 A; A/B=42-450.
DR PDB; 6OI6; X-ray; 2.56 A; A/B=42-450.
DR PDB; 6OIB; X-ray; 2.03 A; A/B=42-450.
DR PDB; 6OIC; X-ray; 2.21 A; A/B=42-450.
DR PDB; 6WH6; X-ray; 2.25 A; A/B=42-450.
DR PDBsum; 6MO6; -.
DR PDBsum; 6MP5; -.
DR PDBsum; 6OI5; -.
DR PDBsum; 6OI6; -.
DR PDBsum; 6OIB; -.
DR PDBsum; 6OIC; -.
DR PDBsum; 6WH6; -.
DR AlphaFoldDB; Q9Y6N5; -.
DR SMR; Q9Y6N5; -.
DR BioGRID; 121806; 101.
DR IntAct; Q9Y6N5; 67.
DR MINT; Q9Y6N5; -.
DR STRING; 9606.ENSP00000260324; -.
DR ChEMBL; CHEMBL4523512; -.
DR iPTMnet; Q9Y6N5; -.
DR PhosphoSitePlus; Q9Y6N5; -.
DR SwissPalm; Q9Y6N5; -.
DR BioMuta; SQOR; -.
DR DMDM; 27151704; -.
DR EPD; Q9Y6N5; -.
DR jPOST; Q9Y6N5; -.
DR MassIVE; Q9Y6N5; -.
DR MaxQB; Q9Y6N5; -.
DR PaxDb; Q9Y6N5; -.
DR PeptideAtlas; Q9Y6N5; -.
DR PRIDE; Q9Y6N5; -.
DR ProteomicsDB; 86742; -.
DR Antibodypedia; 2131; 133 antibodies from 25 providers.
DR DNASU; 58472; -.
DR Ensembl; ENST00000260324.12; ENSP00000260324.7; ENSG00000137767.14.
DR Ensembl; ENST00000568606.5; ENSP00000456019.1; ENSG00000137767.14.
DR GeneID; 58472; -.
DR KEGG; hsa:58472; -.
DR MANE-Select; ENST00000260324.12; ENSP00000260324.7; NM_021199.4; NP_067022.1.
DR UCSC; uc001zvv.4; human.
DR CTD; 58472; -.
DR DisGeNET; 58472; -.
DR GeneCards; SQOR; -.
DR HGNC; HGNC:20390; SQOR.
DR HPA; ENSG00000137767; Tissue enhanced (intestine).
DR MalaCards; SQOR; -.
DR MIM; 617658; gene.
DR MIM; 619221; phenotype.
DR neXtProt; NX_Q9Y6N5; -.
DR OpenTargets; ENSG00000137767; -.
DR PharmGKB; PA134894920; -.
DR VEuPathDB; HostDB:ENSG00000137767; -.
DR eggNOG; KOG3851; Eukaryota.
DR GeneTree; ENSGT00390000019406; -.
DR HOGENOM; CLU_030742_2_1_1; -.
DR InParanoid; Q9Y6N5; -.
DR OMA; YKPAFMY; -.
DR OrthoDB; 1267127at2759; -.
DR PhylomeDB; Q9Y6N5; -.
DR TreeFam; TF314384; -.
DR BioCyc; MetaCyc:HS06393-MON; -.
DR BRENDA; 1.8.5.4; 2681.
DR BRENDA; 1.8.5.8; 2681.
DR PathwayCommons; Q9Y6N5; -.
DR Reactome; R-HSA-1614517; Sulfide oxidation to sulfate.
DR SignaLink; Q9Y6N5; -.
DR BioGRID-ORCS; 58472; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; SQRDL; human.
DR GenomeRNAi; 58472; -.
DR Pharos; Q9Y6N5; Tchem.
DR PRO; PR:Q9Y6N5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y6N5; protein.
DR Bgee; ENSG00000137767; Expressed in colonic mucosa and 189 other tissues.
DR ExpressionAtlas; Q9Y6N5; baseline and differential.
DR Genevisible; Q9Y6N5; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0070813; P:hydrogen sulfide metabolic process; IDA:UniProtKB.
DR GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; PTHR10632; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Disulfide bond; FAD;
KW Flavoprotein; Mitochondrion; Oxidoreductase; Phosphoprotein; Quinone;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..450
FT /note="Sulfide:quinone oxidoreductase, mitochondrial"
FT /id="PRO_0000022408"
FT ACT_SITE 201
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:30905673,
FT ECO:0000303|PubMed:22852582"
FT ACT_SITE 379
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:30905673,
FT ECO:0000303|PubMed:22852582"
FT BINDING 53..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT BINDING 344..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:30905673"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R112"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R112"
FT DISULFID 201..379
FT /evidence="ECO:0000269|PubMed:30905673"
FT VARIANT 213
FT /note="E -> K (in SQORD; severely decreased sulfide:quinone
FT oxidoreductase activity; severely reduced protein levels in
FT patient cells)"
FT /evidence="ECO:0000269|PubMed:32160317"
FT /id="VAR_085241"
FT VARIANT 264
FT /note="I -> T (in dbSNP:rs1044032)"
FT /evidence="ECO:0000269|PubMed:10810093"
FT /id="VAR_014959"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6WH6"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6OI6"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 225..236
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 256..267
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:6OIB"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6OI6"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:6OIB"
FT TURN 429..433
FT /evidence="ECO:0007829|PDB:6OIB"
FT HELIX 439..445
FT /evidence="ECO:0007829|PDB:6OIB"
SQ SEQUENCE 450 AA; 49961 MW; 943ABD4049E3634D CRC64;
MVPLVAVVSG PRAQLFACLL RLGTQQVGPL QLHTGASHAA RNHYEVLVLG GGSGGITMAA
RMKRKVGAEN VAIVEPSERH FYQPIWTLVG AGAKQLSSSG RPTASVIPSG VEWIKARVTE
LNPDKNCIHT DDDEKISYRY LIIALGIQLD YEKIKGLPEG FAHPKIGSNY SVKTVEKTWK
ALQDFKEGNA IFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRSKANIIFN TSLGAIFGVK
KYADALQEII QERNLTVNYK KNLIEVRADK QEAVFENLDK PGETQVISYE MLHVTPPMSP
PDVLKTSPVA DAAGWVDVDK ETLQHRRYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTI
SVIMKNQTPT KKYDGYTSCP LVTGYNRVIL AEFDYKAEPL ETFPFDQSKE RLSMYLMKAD
LMPFLYWNMM LRGYWGGPAF LRKLFHLGMS
