SMO_DROME
ID SMO_DROME Reviewed; 1036 AA.
AC P91682; B7FNK1; Q9VPM8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein smoothened;
DE AltName: Full=SMOH;
DE AltName: Full=Smooth;
DE AltName: Full=dSMO;
DE Flags: Precursor;
GN Name=smo; ORFNames=CG11561;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8706127; DOI=10.1016/s0092-8674(00)80094-x;
RA Alcedo J., Ayzenzon M., von Ohlen T., Noll M., Hooper J.E.;
RT "The Drosophila smoothened gene encodes a seven-pass membrane protein, a
RT putative receptor for the hedgehog signal.";
RL Cell 86:221-232(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8700230; DOI=10.1038/382547a0;
RA van den Heuvel M., Ingham P.W.;
RT "smoothened encodes a receptor-like serpentine protein required for
RT hedgehog signalling.";
RL Nature 382:547-551(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15616566; DOI=10.1038/nature03179;
RA Jia J., Tong C., Wang B., Luo L., Jiang J.;
RT "Hedgehog signalling activity of Smoothened requires phosphorylation by
RT protein kinase A and casein kinase I.";
RL Nature 432:1045-1050(2004).
RN [7]
RP INTERACTION WITH COS.
RX PubMed=15691767; DOI=10.1016/j.devcel.2005.01.001;
RA Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.;
RT "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and
RT proteolytic processing of Cubitus interruptus.";
RL Dev. Cell 8:267-278(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-659; SER-667;
RP SER-670; SER-673; SER-687; SER-690 AND SER-693, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP STRUCTURE BY NMR OF 85-202, AND DISULFIDE BONDS.
RX PubMed=24351982; DOI=10.1038/ncomms3965;
RA Rana R., Carroll C.E., Lee H.J., Bao J., Marada S., Grace C.R.,
RA Guibao C.D., Ogden S.K., Zheng J.J.;
RT "Structural insights into the role of the Smoothened cysteine-rich domain
RT in Hedgehog signalling.";
RL Nat. Commun. 4:2965-2974(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
CC -!- FUNCTION: Segment polarity protein required for correct patterning of
CC every segment. G protein-coupled receptor that associates with the
CC patched protein (ptc) to transduce the hedgehog (hh) signal through the
CC activation of an inhibitory G-protein. In the absence of hh, ptc
CC represses the constitutive signaling activity of smo through fused
CC (fu). Essential component of a hh-signaling pathway which regulates the
CC Duox-dependent gut immune response to bacterial uracil; required to
CC activate Cad99C-dependent endosome formation, norpA-dependent Ca2+
CC mobilization and p38 MAPK, which are essential steps in the Duox-
CC dependent production of reactive oxygen species (ROS) in response to
CC intestinal bacterial infection (PubMed:25639794).
CC -!- SUBUNIT: Interacts with cos. {ECO:0000269|PubMed:15691767}.
CC -!- INTERACTION:
CC P91682; O16844: cos; NbExp=6; IntAct=EBI-142245, EBI-102069;
CC P91682; P91682: smo; NbExp=8; IntAct=EBI-142245, EBI-142245;
CC P91682; P68198: Ubi-p63E; NbExp=4; IntAct=EBI-142245, EBI-86340;
CC P91682; Q9VDD8: Usp8; NbExp=4; IntAct=EBI-142245, EBI-153542;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15616566};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, though the
CC levels vary.
CC -!- PTM: Phosphorylation by CkIalpha and PKA regulates smo accumulation at
CC the cell surface and its signaling activity in response to hh.
CC {ECO:0000269|PubMed:15616566}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown severely reduces adult
CC survival following the ingestion of E.carotovora. Abolishes Cad99C-
CC dependent formation of endosomes and DUOX-dependent up-regulation of
CC reactive oxygen species (ROS) in the intestines of adults fed bacteria-
CC derived uracil. {ECO:0000269|PubMed:25639794}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-9, Met-13 or Met-14 is the
CC initiator. {ECO:0000305}.
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DR EMBL; U87613; AAC33180.1; -; Genomic_DNA.
DR EMBL; AF030334; AAB84275.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51518.2; -; Genomic_DNA.
DR EMBL; BT053691; ACK77608.1; -; mRNA.
DR PIR; S71804; S71804.
DR RefSeq; NP_523443.1; NM_078719.4.
DR PDB; 2MAH; NMR; -; A=85-202.
DR PDBsum; 2MAH; -.
DR AlphaFoldDB; P91682; -.
DR SMR; P91682; -.
DR BioGRID; 59452; 68.
DR DIP; DIP-19956N; -.
DR IntAct; P91682; 9.
DR STRING; 7227.FBpp0077788; -.
DR TCDB; 9.A.14.16.6; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P91682; 7 sites.
DR iPTMnet; P91682; -.
DR PaxDb; P91682; -.
DR DNASU; 33196; -.
DR EnsemblMetazoa; FBtr0078129; FBpp0077788; FBgn0003444.
DR GeneID; 33196; -.
DR KEGG; dme:Dmel_CG11561; -.
DR UCSC; CG11561-RA; d. melanogaster.
DR CTD; 6608; -.
DR FlyBase; FBgn0003444; smo.
DR VEuPathDB; VectorBase:FBgn0003444; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000157206; -.
DR HOGENOM; CLU_007873_3_0_1; -.
DR InParanoid; P91682; -.
DR OMA; HGPRKNS; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; P91682; -.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209338; Assembly of the 'signalling complexes'.
DR Reactome; R-DME-216119; Activation of CI.
DR Reactome; R-DME-216217; Activation of SMO.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-DME-5635838; Activation of SMO.
DR SignaLink; P91682; -.
DR BioGRID-ORCS; 33196; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33196; -.
DR PRO; PR:P91682; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003444; Expressed in wing disc and 50 other tissues.
DR ExpressionAtlas; P91682; baseline and differential.
DR Genevisible; P91682; DM.
DR GO; GO:0005929; C:cilium; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005113; F:patched binding; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0048099; P:anterior/posterior lineage restriction, imaginal disc; TAS:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0071679; P:commissural neuron axon guidance; IBA:GO_Central.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IGI:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; TAS:FlyBase.
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 membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1036
FT /note="Protein smoothened"
FT /id="PRO_0000013019"
FT TOPO_DOM 32..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..206
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 678..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:24351982"
FT DISULFID 100..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:24351982"
FT DISULFID 139..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:24351982"
FT DISULFID 172..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:24351982"
FT DISULFID 218..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 242..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 339..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 513..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2MAH"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:2MAH"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2MAH"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2MAH"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2MAH"
SQ SEQUENCE 1036 AA; 116552 MW; 7797FC71A539A87A CRC64;
MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE LEPINGTLNY
RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC FGSKLPYELS SLDLTDFHTE
KELNDKLNDY YALKHVPKCW AAIQPFLCAV FKPKCEKING EDMVYLPSYE MCRITMEPCR
ILYNTTFFPK FLRCNETLFP TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV
RCKDPLYTDD EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL
IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL TAGMVWFVFL
TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA FSEVDGNSIV GICFVGYINH
SMRAGLLLGP LCGVILIGGY FITRGMVMLF GLKHFANDIK STSASNKIHL IIMRMGVCAL
LTLVFILVAI ACHVTEFRHA DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL
LCLFSSGIVM STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK
GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL TGAATGNSSS
HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK TKVASRSRGK HGGSSSNRRT
QRRRDYIAAA TGKSSRRRES STSVESQVIA LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS
MKRRTANAGL DPSILNEFLQ KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ
EISEDDHDGI KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN
PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH SRNSKTSCDV
GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF GGTELQGLLG HSHRHQREPT
FMSESDKLKM LLLPSK
