SMO_MOUSE
ID SMO_MOUSE Reviewed; 793 AA.
AC P56726;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Smoothened homolog;
DE Short=SMO;
DE Flags: Precursor;
GN Name=Smo; Synonyms=Smoh;
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 [MRNA].
RX PubMed=9196051; DOI=10.1006/bbrc.1997.6750;
RA Akiyama H., Shigeno C., Hiraki Y., Shukunami C., Kohno H., Akagi M.,
RA Konishi J., Nakamura T.;
RT "Cloning of a mouse Smoothened cDNA and expression patterns of hedgehog
RT signalling molecules during chondrogenesis and cartilage differentiation in
RT clonal mouse EC cells, ATDC5.";
RL Biochem. Biophys. Res. Commun. 235:142-147(1997).
RN [2]
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 [3]
RP INTERACTION WITH ARRB2.
RX PubMed=15618519; DOI=10.1126/science.1104135;
RA Chen W., Ren X.R., Nelson C.D., Barak L.S., Chen J.K., Beachy P.A.,
RA de Sauvage F., Lefkowitz R.J.;
RT "Activity-dependent internalization of smoothened mediated by beta-arrestin
RT 2 and GRK2.";
RL Science 306:2257-2260(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GAS8.
RX PubMed=21659505; DOI=10.1074/jbc.m111.234666;
RA Evron T., Philipp M., Lu J., Meloni A.R., Burkhalter M., Chen W.,
RA Caron M.G.;
RT "Growth arrest specific 8 (Gas8) and G protein-coupled receptor kinase 2
RT (GRK2) cooperate in the control of Smoothened signaling.";
RL J. Biol. Chem. 286:27676-27686(2011).
RN [5]
RP ASSOCIATION WITH THE BBSOME COMPLEX, AND INTERACTION WITH BBS5 AND BBS7.
RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA Sheffield V.C.;
RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT Smoothened.";
RL PLoS Genet. 7:E1002358-E1002358(2011).
RN [6]
RP FUNCTION, INTERACTION WITH DLG5; KIF7 AND SDCBP, AND SUBCELLULAR LOCATION.
RX PubMed=25644602; DOI=10.1101/gad.252676.114;
RA Chong Y.C., Mann R.K., Zhao C., Kato M., Beachy P.A.;
RT "Bifurcating action of Smoothened in Hedgehog signaling is mediated by
RT Dlg5.";
RL Genes Dev. 29:262-276(2015).
CC -!- FUNCTION: G protein-coupled receptor that probably associates with the
CC patched protein (PTCH) to transduce the hedgehog's proteins signal.
CC Binding of sonic hedgehog (SHH) to its receptor patched is thought to
CC prevent normal inhibition by patched of smoothened (SMO) (By
CC similarity). Required for the accumulation of KIF7, GLI2 and GLI3 in
CC the cilia. Interacts with DLG5 at the ciliary base to induce the
CC accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation
CC (PubMed:25644602). {ECO:0000250|UniProtKB:Q99835,
CC ECO:0000269|PubMed:25644602}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ARRB2
CC (PubMed:15618519). Interacts with BBS5 and BBS7; the interactions are
CC indicative for the association of SMO with the BBsome complex to
CC facilitate ciliary localization of SMO (PubMed:22072986). Interacts
CC with KIF7, DLG5 and SDCBP (PubMed:25644602). Interacts with GAS8/DRC4
CC (PubMed:21659505). {ECO:0000250|UniProtKB:Q99835,
CC ECO:0000269|PubMed:15618519, ECO:0000269|PubMed:21659505,
CC ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:25644602}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC projection, cilium {ECO:0000269|PubMed:21659505,
CC ECO:0000269|PubMed:25644602}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC069469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS19965.1; -.
DR PIR; JC5539; JC5539.
DR RefSeq; NP_795970.3; NM_176996.4.
DR PDB; 6O3C; X-ray; 2.80 A; A=64-566.
DR PDBsum; 6O3C; -.
DR AlphaFoldDB; P56726; -.
DR SMR; P56726; -.
DR BioGRID; 235504; 28.
DR IntAct; P56726; 17.
DR STRING; 10090.ENSMUSP00000001812; -.
DR BindingDB; P56726; -.
DR ChEMBL; CHEMBL6080; -.
DR DrugCentral; P56726; -.
DR GuidetoPHARMACOLOGY; 239; -.
DR GlyGen; P56726; 3 sites.
DR iPTMnet; P56726; -.
DR PhosphoSitePlus; P56726; -.
DR PaxDb; P56726; -.
DR PRIDE; P56726; -.
DR ProteomicsDB; 258703; -.
DR ABCD; P56726; 1 sequenced antibody.
DR Antibodypedia; 31982; 605 antibodies from 38 providers.
DR DNASU; 319757; -.
DR Ensembl; ENSMUST00000001812; ENSMUSP00000001812; ENSMUSG00000001761.
DR GeneID; 319757; -.
DR KEGG; mmu:319757; -.
DR UCSC; uc009bef.2; mouse.
DR CTD; 6608; -.
DR MGI; MGI:108075; Smo.
DR VEuPathDB; HostDB:ENSMUSG00000001761; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000157206; -.
DR HOGENOM; CLU_007873_3_1_1; -.
DR InParanoid; P56726; -.
DR OMA; FLKCTPD; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; P56726; -.
DR TreeFam; TF106460; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5635838; Activation of SMO.
DR BioGRID-ORCS; 319757; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Smo; mouse.
DR PRO; PR:P56726; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P56726; protein.
DR Bgee; ENSMUSG00000001761; Expressed in undifferentiated genital tubercle and 102 other tissues.
DR ExpressionAtlas; P56726; baseline and differential.
DR Genevisible; P56726; MM.
DR GO; GO:0097731; C:9+0 non-motile cilium; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0005113; F:patched binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0048143; P:astrocyte activation; IMP:MGI.
DR GO; GO:0060413; P:atrial septum morphogenesis; IGI:MGI.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISO:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071397; P:cellular response to cholesterol; IEP:BHF-UCL.
DR GO; GO:0007417; P:central nervous system development; IGI:MGI.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISO:MGI.
DR GO; GO:0060242; P:contact inhibition; ISS:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IMP:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IGI:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IMP:MGI.
DR GO; GO:0048853; P:forebrain morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0070986; P:left/right axis specification; IMP:MGI.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:MGI.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISO:MGI.
DR GO; GO:0072285; P:mesenchymal to epithelial transition involved in metanephric renal vesicle formation; IMP:UniProtKB.
DR GO; GO:0007494; P:midgut development; IMP:BHF-UCL.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0051451; P:myoblast migration; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; IMP:UniProtKB.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0051799; P:negative regulation of hair follicle development; IMP:MGI.
DR GO; GO:2000346; P:negative regulation of hepatocyte proliferation; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0001755; P:neural crest cell migration; IGI:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IGI:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0061113; P:pancreas morphogenesis; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:CACAO.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:CACAO.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IGI:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:2000826; P:regulation of heart morphogenesis; IMP:BHF-UCL.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IMP:MGI.
DR GO; GO:0021910; P:smoothened signaling pathway involved in ventral spinal cord patterning; IMP:BHF-UCL.
DR GO; GO:0061053; P:somite development; IMP:BHF-UCL.
DR GO; GO:0021794; P:thalamus development; IMP:MGI.
DR GO; GO:0003323; P:type B pancreatic cell development; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0007371; P:ventral midline determination; IMP:BHF-UCL.
DR CDD; cd15030; 7tmF_SMO_homolog; 1.
DR CDD; cd07451; CRD_SMO; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR026544; SMO.
DR InterPro; IPR035683; SMO_7TM.
DR InterPro; IPR041771; SMO_CRD.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF35; PTHR11309:SF35; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..793
FT /note="Smoothened homolog"
FT /id="PRO_0000013016"
FT TOPO_DOM 33..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 69..185
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..573
FT /note="Interaction with BBS5 and BBS7"
FT /evidence="ECO:0000269|PubMed:22072986"
FT REGION 585..597
FT /note="Interaction with DLG5"
FT /evidence="ECO:0000269|PubMed:25644602"
FT REGION 674..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 82..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 122..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 151..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 197..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 221..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 318..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 494..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 54
FT /note="D -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Y -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="R -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:6O3C"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6O3C"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 228..258
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 266..286
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 317..348
FT /evidence="ECO:0007829|PDB:6O3C"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6O3C"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:6O3C"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 409..436
FT /evidence="ECO:0007829|PDB:6O3C"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 444..498
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 519..537
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:6O3C"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:6O3C"
SQ SEQUENCE 793 AA; 87450 MW; DEAD556A45F7C960 CRC64;
MAAGRPVRGP ELAPRRLLQL LLLVLLGGPG RGAALSGNVT GPGPHSASGS SRRDVPVTSP
PPPLLSHCGR AAHCEPLRYN VCLGSALPYG ATTTLLAGDS DSQEEAHGKL VLWSGLRNAP
RCWAVIQPLL CAVYMPKCEN DRVELPSRTL CQATRGPCAI VERERGWPDF LRCTPDHFPE
GCPNEVQNIK FNSSGQCEAP LVRTDNPKSW YEDVEGCGIQ CQNPLFTEAE HQDMHSYIAA
FGAVTGLCTL FTLATFVADW RNSNRYPAVI LFYVNACFFV GSIGWLAQFM DGARREIVCR
ADGTMRFGEP TSSETLSCVI IFVIVYYALM AGVVWFVVLT YAWHTSFKAL GTTYQPLSGK
TSYFHLLTWS LPFVLTVAIL AVAQVDGDSV SGICFVGYKN YRYRAGFVLA PIGLVLIVGG
YFLIRGVMTL FSIKSNHPGL LSEKAASKIN ETMLRLGIFG FLAFGFVLIT FSCHFYDFFN
QAEWERSFRD YVLCQANVTI GLPTKKPIPD CEIKNRPSLL VEKINLFAMF GTGIAMSTWV
WTKATLLIWR RTWCRLTGHS DDEPKRIKKS KMIAKAFSKR RELLQNPGQE LSFSMHTVSH
DGPVAGLAFD LNEPSADVSS AWAQHVTKMV ARRGAILPQD VSVTPVATPV PPEEQANMWL
VEAEISPELE KRLGRKKKRR KRKKEVCPLR PAPELHHSAP VPATSAVPRL PQLPRQKCLV
AANAWGTGES CRQGAWTLVS NPFCPEPSPH QDPFLPGASA PRVWAQGRLQ GLGSIHSRTN
LMEAEILDAD SDF
