NR1H3_MOUSE
ID NR1H3_MOUSE Reviewed; 445 AA.
AC Q9Z0Y9; Q9QUH7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Oxysterols receptor LXR-alpha;
DE AltName: Full=Liver X receptor alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 3;
GN Name=Nr1h3; Synonyms=Lxra;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=10675617; DOI=10.1016/s0378-1119(99)00555-7;
RA Alberti S., Steffensen K.R., Gustafsson J.-A.;
RT "Structural characterisation of the mouse nuclear oxysterol receptor genes
RT LXRalpha and LXRbeta.";
RL Gene 243:93-103(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10890879; DOI=10.1073/pnas.100519097;
RA Tamura K., Chen Y.E., Horiuchi M., Chen Q., Daviet L., Yang Z.,
RA Lopez-Ilasaca M., Mu H., Pratt R.E., Dzau V.J.;
RT "LXRalpha functions as a cAMP-responsive transcriptional regulator of gene
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8513-8518(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION IN METABOLISM REGULATION.
RX PubMed=18055760; DOI=10.1124/mol.107.040741;
RA Wada T., Kang H.S., Angers M., Gong H., Bhatia S., Khadem S., Ren S.,
RA Ellis E., Strom S.C., Jetten A.M., Xie W.;
RT "Identification of oxysterol 7alpha-hydroxylase (Cyp7b1) as a novel
RT retinoid-related orphan receptor alpha (RORalpha) (NR1F1) target gene and a
RT functional cross-talk between RORalpha and liver X receptor (NR1H3).";
RL Mol. Pharmacol. 73:891-899(2008).
RN [5]
RP FUNCTION.
RX PubMed=19520913; DOI=10.1126/science.1168974;
RA Zelcer N., Hong C., Boyadjian R., Tontonoz P.;
RT "LXR regulates cholesterol uptake through Idol-dependent ubiquitination of
RT the LDL receptor.";
RL Science 325:100-104(2009).
RN [6]
RP FUNCTION.
RX PubMed=20427281; DOI=10.1074/jbc.m110.123729;
RA Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
RA Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J.,
RA van Berkel T.J., Tontonoz P., Zelcer N.;
RT "The E3 ubiquitin ligase IDOL induces the degradation of the low density
RT lipoprotein receptor family members VLDLR and ApoER2.";
RL J. Biol. Chem. 285:19720-19726(2010).
RN [7]
RP FUNCTION.
RX PubMed=24206663; DOI=10.1016/j.cmet.2013.10.002;
RA Rong X., Albert C.J., Hong C., Duerr M.A., Chamberlain B.T., Tarling E.J.,
RA Ito A., Gao J., Wang B., Edwards P.A., Jung M.E., Ford D.A., Tontonoz P.;
RT "LXRs regulate ER stress and inflammation through dynamic modulation of
RT membrane phospholipid composition.";
RL Cell Metab. 18:685-697(2013).
RN [8]
RP FUNCTION.
RX PubMed=25806685; DOI=10.7554/elife.06557;
RA Rong X., Wang B., Dunham M.M., Hedde P.N., Wong J.S., Gratton E.,
RA Young S.G., Ford D.A., Tontonoz P.;
RT "Lpcat3-dependent production of arachidonoyl phospholipids is a key
RT determinant of triglyceride secretion.";
RL Elife 4:0-0(2015).
RN [9]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=27383786; DOI=10.1038/nature18628;
RA Hsieh J., Koseki M., Molusky M.M., Yakushiji E., Ichi I., Westerterp M.,
RA Iqbal J., Chan R.B., Abramowicz S., Tascau L., Takiguchi S., Yamashita S.,
RA Welch C.L., Di Paolo G., Hussain M.M., Lefkowitch J.H., Rader D.J.,
RA Tall A.R.;
RT "TTC39B deficiency stabilizes LXR reducing both atherosclerosis and
RT steatohepatitis.";
RL Nature 535:303-307(2016).
RN [10]
RP FUNCTION.
RX PubMed=28846071; DOI=10.1172/jci93616;
RA Rong X., Wang B., Palladino E.N., de Aguiar Vallim T.Q., Ford D.A.,
RA Tontonoz P.;
RT "ER phospholipid composition modulates lipogenesis during feeding and in
RT obesity.";
RL J. Clin. Invest. 127:3640-3651(2017).
RN [11] {ECO:0007744|PDB:2ACL}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 203-445.
RX PubMed=16107141; DOI=10.1021/jm050532w;
RA Jaye M.C., Krawiec J.A., Campobasso N., Smallwood A., Qiu C., Lu Q.,
RA Kerrigan J.J., De Los Frailes Alvaro M., Laffitte B., Liu W.S.,
RA Marino J.P. Jr., Meyer C.R., Nichols J.A., Parks D.J., Perez P.,
RA Sarov-Blat L., Seepersaud S.D., Steplewski K.M., Thompson S.K., Wang P.,
RA Watson M.A., Webb C.L., Haigh D., Caravella J.A., Macphee C.H.,
RA Willson T.M., Collins J.L.;
RT "Discovery of substituted maleimides as liver X receptor agonists and
RT determination of a ligand-bound crystal structure.";
RL J. Med. Chem. 48:5419-5422(2005).
RN [12] {ECO:0007744|PDB:3FAL}
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 200-445.
RX PubMed=18800767; DOI=10.1021/jm800612u;
RA Chao E.Y., Caravella J.A., Watson M.A., Campobasso N., Ghisletti S.,
RA Billin A.N., Galardi C., Wang P., Laffitte B.A., Iannone M.A.,
RA Goodwin B.J., Nichols J.A., Parks D.J., Stewart E., Wiethe R.W.,
RA Williams S.P., Smallwood A., Pearce K.H., Glass C.K., Willson T.M.,
RA Zuercher W.J., Collins J.L.;
RT "Structure-guided design of N-phenyl tertiary amines as transrepression-
RT selective liver X receptor modulators with anti-inflammatory activity.";
RL J. Med. Chem. 51:5758-5765(2008).
RN [13] {ECO:0007744|PDB:3FC6}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 200-445.
RX PubMed=19167885; DOI=10.1016/j.bmcl.2009.01.004;
RA Washburn D.G., Hoang T.H., Campobasso N., Smallwood A., Parks D.J.,
RA Webb C.L., Frank K.A., Nord M., Duraiswami C., Evans C., Jaye M.,
RA Thompson S.K.;
RT "Synthesis and SAR of potent LXR agonists containing an indole
RT pharmacophore.";
RL Bioorg. Med. Chem. Lett. 19:1097-1100(2009).
CC -!- FUNCTION: Nuclear receptor that exhibits a ligand-dependent
CC transcriptional activation activity (PubMed:18055760, PubMed:19520913,
CC PubMed:20427281). Interaction with retinoic acid receptor (RXR) shifts
CC RXR from its role as a silent DNA-binding partner to an active ligand-
CC binding subunit in mediating retinoid responses through target genes
CC defined by LXRES. LXRES are DR4-type response elements characterized by
CC direct repeats of two similar hexanuclotide half-sites spaced by four
CC nucleotides. Plays an important role in the regulation of cholesterol
CC homeostasis, regulating cholesterol uptake through MYLIP-dependent
CC ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with
CC RORA for the regulation of genes involved in liver metabolism (By
CC similarity). Induces LPCAT3-dependent phospholipid remodeling in
CC endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1
CC processing and lipogenesis (PubMed:28846071, PubMed:25806685). Via
CC LPCAT3, triggers the incorporation of arachidonate into
CC phosphatidylcholines of ER membranes, increasing membrane dynamics and
CC enabling triacylglycerols transfer to nascent very low-density
CC lipoprotein (VLDL) particles (PubMed:25806685). Via LPCAT3 also
CC counteracts lipid-induced ER stress response and inflammation, likely
CC by modulating SRC kinase membrane compartmentalization and limiting the
CC synthesis of lipid inflammatory mediators (PubMed:24206663).
CC {ECO:0000250|UniProtKB:Q13133, ECO:0000269|PubMed:18055760,
CC ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281,
CC ECO:0000269|PubMed:24206663, ECO:0000269|PubMed:25806685,
CC ECO:0000269|PubMed:28846071}.
CC -!- SUBUNIT: Heterodimer of NR1H3 and RXR (retinoic acid receptor).
CC Interacts with CCAR2 (via N-terminus) in a ligand-independent manner.
CC Interacts with SIRT1 and this interaction is inhibited by CCAR2 (By
CC similarity). {ECO:0000250|UniProtKB:Q13133}.
CC -!- INTERACTION:
CC Q9Z0Y9; O88559: Men1; NbExp=3; IntAct=EBI-5276764, EBI-3990176;
CC Q9Z0Y9; Q96EB6: SIRT1; Xeno; NbExp=2; IntAct=EBI-5276764, EBI-1802965;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:27383786}. Cytoplasm {ECO:0000269|PubMed:27383786}.
CC -!- PTM: Ubiquitinated leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:27383786}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ132599; CAB51952.1; -; Genomic_DNA.
DR EMBL; AJ132600; CAB51952.1; JOINED; Genomic_DNA.
DR EMBL; AJ132601; CAB51923.1; -; mRNA.
DR EMBL; AF085745; AAD16050.1; -; mRNA.
DR EMBL; AL691450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16426.1; -.
DR RefSeq; NP_001171201.1; NM_001177730.1.
DR RefSeq; NP_038867.2; NM_013839.4.
DR RefSeq; XP_006499229.1; XM_006499166.2.
DR RefSeq; XP_006499230.1; XM_006499167.2.
DR RefSeq; XP_006499231.1; XM_006499168.3.
DR PDB; 2ACL; X-ray; 2.80 A; B/D/F/H=203-445.
DR PDB; 3FAL; X-ray; 2.36 A; B/D=200-445.
DR PDB; 3FC6; X-ray; 2.06 A; B/D=200-445.
DR PDBsum; 2ACL; -.
DR PDBsum; 3FAL; -.
DR PDBsum; 3FC6; -.
DR AlphaFoldDB; Q9Z0Y9; -.
DR SMR; Q9Z0Y9; -.
DR BioGRID; 204449; 8.
DR ComplexPortal; CPX-708; RXRalpha-LXRalpha nuclear hormone receptor complex.
DR ComplexPortal; CPX-717; RXRbeta-LXRalpha nuclear hormone receptor complex.
DR CORUM; Q9Z0Y9; -.
DR DIP; DIP-62095N; -.
DR IntAct; Q9Z0Y9; 8.
DR MINT; Q9Z0Y9; -.
DR STRING; 10090.ENSMUSP00000106988; -.
DR BindingDB; Q9Z0Y9; -.
DR ChEMBL; CHEMBL2189152; -.
DR GuidetoPHARMACOLOGY; 602; -.
DR iPTMnet; Q9Z0Y9; -.
DR PhosphoSitePlus; Q9Z0Y9; -.
DR MaxQB; Q9Z0Y9; -.
DR PaxDb; Q9Z0Y9; -.
DR PRIDE; Q9Z0Y9; -.
DR ProteomicsDB; 295518; -.
DR Antibodypedia; 13611; 584 antibodies from 39 providers.
DR DNASU; 22259; -.
DR Ensembl; ENSMUST00000002177; ENSMUSP00000002177; ENSMUSG00000002108.
DR Ensembl; ENSMUST00000111354; ENSMUSP00000106986; ENSMUSG00000002108.
DR Ensembl; ENSMUST00000111356; ENSMUSP00000106988; ENSMUSG00000002108.
DR GeneID; 22259; -.
DR KEGG; mmu:22259; -.
DR UCSC; uc008kvc.2; mouse.
DR CTD; 10062; -.
DR MGI; MGI:1352462; Nr1h3.
DR VEuPathDB; HostDB:ENSMUSG00000002108; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159068; -.
DR HOGENOM; CLU_007368_12_4_1; -.
DR InParanoid; Q9Z0Y9; -.
DR OMA; DFPVASH; -.
DR OrthoDB; 1137281at2759; -.
DR PhylomeDB; Q9Z0Y9; -.
DR TreeFam; TF352167; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR BioGRID-ORCS; 22259; 2 hits in 75 CRISPR screens.
DR EvolutionaryTrace; Q9Z0Y9; -.
DR PRO; PR:Q9Z0Y9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z0Y9; protein.
DR Bgee; ENSMUSG00000002108; Expressed in right kidney and 117 other tissues.
DR ExpressionAtlas; Q9Z0Y9; baseline and differential.
DR Genevisible; Q9Z0Y9; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0032810; F:sterol response element binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:BHF-UCL.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IMP:BHF-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IGI:BHF-UCL.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0032369; P:negative regulation of lipid transport; ISO:MGI.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IMP:BHF-UCL.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:MGI.
DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0090341; P:negative regulation of secretion of lysosomal enzymes; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; ISO:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0032570; P:response to progesterone; ISO:MGI.
DR GO; GO:0055092; P:sterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR023257; Liver_X_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR02034; LIVERXRECPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..445
FT /note="Oxysterols receptor LXR-alpha"
FT /id="PRO_0000053536"
FT DOMAIN 207..445
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 93..168
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 96..116
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 132..156
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..94
FT /note="Transactivation AF-1; required for ligand-
FT independent transactivation function"
FT /evidence="ECO:0000250|UniProtKB:Q13133"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..445
FT /note="Transactivation AF-2; required for ligand-dependent
FT transactivation function; mediates interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:Q13133"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62685"
FT CONFLICT 399
FT /note="P -> R (in Ref. 1; CAB51952/CAB51923)"
FT /evidence="ECO:0000305"
FT HELIX 206..227
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 245..272
FT /evidence="ECO:0007829|PDB:3FC6"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 281..301
FT /evidence="ECO:0007829|PDB:3FC6"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:3FC6"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:3FC6"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3FC6"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3FC6"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 331..347
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 373..394
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 401..428
FT /evidence="ECO:0007829|PDB:3FC6"
FT HELIX 435..441
FT /evidence="ECO:0007829|PDB:3FC6"
SQ SEQUENCE 445 AA; 50418 MW; 1A426DF38D935731 CRC64;
MSLWLEASMP DVSPDSATEL WKTEPQDAGD QGGNTCILRE EARMPQSTGV ALGIGLESAE
PTALLPRAET LPEPTELRPQ KRKKGPAPKM LGNELCSVCG DKASGFHYNV LSCEGCKGFF
RRSVIKGARY VCHSGGHCPM DTYMRRKCQE CRLRKCRQAG MREECVLSEE QIRLKKLKRQ
EEEQAQATSV SPRVSSPPQV LPQLSPEQLG MIEKLVAAQQ QCNRRSFSDR LRVTPWPIAP
DPQSREARQQ RFAHFTELAI VSVQEIVDFA KQLPGFLQLS REDQIALLKT SAIEVMLLET
SRRYNPGSES ITFLKDFSYN REDFAKAGLQ VEFINPIFEF SRAMNELQLN DAEFALLIAI
SIFSADRPNV QDQLQVERLQ HTYVEALHAY VSINHPHDPL MFPRMLMKLV SLRTLSSVHS
EQVFALRLQD KKLPPLLSEI WDVHE
