DHI1_CAVPO
ID DHI1_CAVPO Reviewed; 300 AA.
AC Q6QLL4; Q9QZE1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase 1 {ECO:0000303|PubMed:10699594};
DE Short=11-DH;
DE Short=11-beta-HSD1 {ECO:0000303|PubMed:10699594};
DE EC=1.1.1.146 {ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
DE AltName: Full=7-oxosteroid reductase;
DE EC=1.1.1.201 {ECO:0000250|UniProtKB:P28845};
DE AltName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 1;
GN Name=HSD11B1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=10699594; DOI=10.1016/s0039-128x(99)00098-7;
RA Pu X., Yang K.;
RT "Guinea pig 11beta-hydroxysteroid dehydrogenase type 1: primary structure
RT and catalytic properties.";
RL Steroids 65:148-156(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Odermatt A., Kadereit B.;
RT "Guinea pig 11-beta-hydroxysteroid dehydrogenase type 1: species specific
RT properties.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 24-299 IN COMPLEX WITH NADP,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19507261; DOI=10.1002/pro.150;
RA Lawson A.J., Walker E.A., White S.A., Dafforn T.R., Stewart P.M.,
RA Ride J.P.;
RT "Mutations of key hydrophobic surface residues of 11 beta-hydroxysteroid
RT dehydrogenase type 1 increase solubility and monodispersity in a bacterial
RT expression system.";
RL Protein Sci. 18:1552-1563(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-297 IN COMPLEX WITH NADP, AND
RP HOMODIMERIZATION.
RX PubMed=15542590; DOI=10.1074/jbc.m412463200;
RA Ogg D., Elleby B., Norstroem C., Stefansson K., Abrahmsen L., Oppermann U.,
RA Svensson S.;
RT "The crystal structure of guinea pig 11beta-hydroxysteroid dehydrogenase
RT type 1 provides a model for enzyme-lipid bilayer interactions.";
RL J. Biol. Chem. 280:3789-3794(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-300 IN COMPLEX WITH NADP AND
RP SYNTHETIC INHIBITOR.
RX PubMed=19473839; DOI=10.1016/j.bmcl.2009.05.011;
RA Siu M., Johnson T.O., Wang Y., Nair S.K., Taylor W.D., Cripps S.J.,
RA Matthews J.J., Edwards M.P., Pauly T.A., Ermolieff J., Castro A.,
RA Hosea N.A., LaPaglia A., Fanjul A.N., Vogel J.E.;
RT "N-(Pyridin-2-yl) arylsulfonamide inhibitors of 11beta-hydroxysteroid
RT dehydrogenase type 1: Discovery of PF-915275.";
RL Bioorg. Med. Chem. Lett. 19:3493-3497(2009).
CC -!- FUNCTION: Controls the reversible conversion of biologically active
CC glucocorticoids such as cortisone to cortisol, and 11-
CC dehydrocorticosterone to corticosterone in the presence of NADP(H)
CC (PubMed:10699594, PubMed:19507261). Participates in the corticosteroid
CC receptor-mediated anti-inflammatory response, as well as metabolic and
CC homeostatic processes (By similarity). Bidirectional in vitro,
CC predominantly functions as a reductase in vivo, thereby increasing the
CC concentration of active glucocorticoids. It has broad substrate
CC specificity, besides glucocorticoids, it accepts other steroid and
CC sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids
CC such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-
CC oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and
CC 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-
CC 17-one), among others (By similarity). Catalyzes the stereo-specific
CC conversion of the major dietary oxysterol, 7-ketocholesterol (7-
CC oxocholesterol), into the more polar 7-beta-hydroxycholesterol
CC metabolite (By similarity). 7-oxocholesterol is one of the most
CC important oxysterols, it participates in several events such as
CC induction of apoptosis, accumulation in atherosclerotic lesions, lipid
CC peroxidation, and induction of foam cell formation (By similarity).
CC Mediates the 7-oxo reduction of 7-oxolithocholate mainly to
CC chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in
CC its free form and when conjugated to glycine or taurine, providing a
CC link between glucocorticoid activation and bile acid metabolism (By
CC similarity). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol
CC from 7-oxo-25-hydroxycholesterol in vitro, which acts as ligand for the
CC G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2
CC (EBI2) and may thereby regulate immune cell migration (By similarity).
CC {ECO:0000250|UniProtKB:P28845, ECO:0000250|UniProtKB:P50172,
CC ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:11388, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346,
CC ChEBI:CHEBI:47787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.146; Evidence={ECO:0000269|PubMed:10699594,
CC ECO:0000269|PubMed:19507261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11389;
CC Evidence={ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11390;
CC Evidence={ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cortisone + H(+) + NADPH = cortisol + NADP(+);
CC Xref=Rhea:RHEA:68616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962,
CC ChEBI:CHEBI:17650, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68617;
CC Evidence={ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68618;
CC Evidence={ECO:0000269|PubMed:10699594, ECO:0000269|PubMed:19507261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=corticosterone + NADP(+) = 11-dehydrocorticosterone + H(+) +
CC NADPH; Xref=Rhea:RHEA:42200, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78600;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42201;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42202;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:20233, ChEBI:CHEBI:15378, ChEBI:CHEBI:35349,
CC ChEBI:CHEBI:47789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.201; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20235;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxocholesterol + H(+) + NADPH = 7beta-hydroxycholesterol +
CC NADP(+); Xref=Rhea:RHEA:68656, ChEBI:CHEBI:15378, ChEBI:CHEBI:42989,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64294;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68657;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + NADP(+) = 7-oxolithocholate + H(+) +
CC NADPH; Xref=Rhea:RHEA:53820, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53822;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxolithocholate + H(+) + NADPH = NADP(+) + ursodeoxycholate;
CC Xref=Rhea:RHEA:47540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47541;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate + NADP(+) = 7-oxoglycolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:65056, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65058;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + taurochenodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:65060, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65062;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + tauroursodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:68980, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132028,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68982;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycoursodeoxycholate + NADP(+) = 7-oxoglycolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:68976, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132030,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68978;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxopregnenolone + H(+) + NADPH = 7beta-hydroxypregnenolone +
CC NADP(+); Xref=Rhea:RHEA:69436, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:183806, ChEBI:CHEBI:183807;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69437;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta,7alpha-dihydroxyandrost-5-en-17-one + NADP(+) = 3beta-
CC hydroxy-5-androstene-7,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:69440,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:81471, ChEBI:CHEBI:183808;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69441;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5-androstene-7,17-dione + H(+) + NADPH =
CC 3beta,7beta-dihydroxyandrost-5-en-17-one + NADP(+);
CC Xref=Rhea:RHEA:69452, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:183368, ChEBI:CHEBI:183808;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69453;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5alpha-androstane-7,17-dione + H(+) + NADPH =
CC 3beta,7beta-dihydroxy-5alpha-androstan-17-one + NADP(+);
CC Xref=Rhea:RHEA:69456, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:79834, ChEBI:CHEBI:183809;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69457;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.85 uM for cortisol {ECO:0000269|PubMed:10699594};
CC KM=2.77 uM for cortisone {ECO:0000269|PubMed:10699594};
CC KM=4.09 uM for cortisone {ECO:0000269|PubMed:19507261};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15542590,
CC ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed in all peripheral tissues, with
CC highest expression in liver, followed by kidney and lung, and very low
CC expression in heart, lung, spleen, stomach, small intestine, colon,
CC skin, skeletal muscle, and ovary. {ECO:0000269|PubMed:10699594}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF188005; AAF01249.1; -; mRNA.
DR EMBL; AY535424; AAS47491.1; -; mRNA.
DR RefSeq; NP_001166328.1; NM_001172857.1.
DR RefSeq; XP_013012714.1; XM_013157260.1.
DR PDB; 1XSE; X-ray; 2.50 A; A/B=24-297.
DR PDB; 3DWF; X-ray; 2.20 A; A/B/C/D=24-299.
DR PDB; 3G49; X-ray; 2.50 A; A/B/C/D=24-300.
DR PDB; 3LZ6; X-ray; 1.84 A; A/B/C/D=26-288.
DR PDBsum; 1XSE; -.
DR PDBsum; 3DWF; -.
DR PDBsum; 3G49; -.
DR PDBsum; 3LZ6; -.
DR AlphaFoldDB; Q6QLL4; -.
DR SMR; Q6QLL4; -.
DR STRING; 10141.ENSCPOP00000005042; -.
DR Ensembl; ENSCPOT00000005656; ENSCPOP00000005042; ENSCPOG00000005596.
DR GeneID; 100135542; -.
DR KEGG; cpoc:100135542; -.
DR CTD; 3290; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000160097; -.
DR InParanoid; Q6QLL4; -.
DR OMA; SMEDMTF; -.
DR OrthoDB; 906746at2759; -.
DR TreeFam; TF329114; -.
DR BRENDA; 1.1.1.146; 1225.
DR BRENDA; 1.1.1.B40; 1225.
DR SABIO-RK; Q6QLL4; -.
DR EvolutionaryTrace; Q6QLL4; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000005596; Expressed in liver and 8 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0047022; F:7-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Lipid metabolism;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Signal-anchor;
KW Steroid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..300
FT /note="11-beta-hydroxysteroid dehydrogenase 1"
FT /id="PRO_0000054618"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..300
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 41..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15542590,
FT ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261"
FT BINDING 92..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15542590,
FT ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261"
FT BINDING 119..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15542590,
FT ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15542590,
FT ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261"
FT BINDING 218..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15542590,
FT ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 22
FT /note="S -> P (in Ref. 1; AAF01249)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="V -> A (in Ref. 1; AAF01249)"
FT /evidence="ECO:0000305"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 181..203
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:3LZ6"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:3LZ6"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:3LZ6"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:3DWF"
SQ SEQUENCE 300 AA; 33226 MW; 8D8A9725F7A6D912 CRC64;
MAFLKKYLLT ILMVFLAYYY YSANEKFRPE MLQGKKVIVT GASKGIGREI AYHLAKMGAH
VVVTARSKEA LQKVVARCLE LGAASAHYIA GSMEDMTFAE EFVAEAGNLM GGLDMLILNH
VLYNRLTFFH GEIDNVRKSM EVNFHSFVVL SVAAMPMLMQ SQGSIAVVSS VAGKITYPLI
APYSASKFAL DGFFSTLRSE FLVNKVNVSI TLCILGLIDT ETAIKATSGI YLGPASPKEE
CALEIIKGTA LRQDEMYYVG SRWVPYLLGN PGRKIMEFLS AAEYNWDNVL SNEKLYGRWA
