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   27-MAR-2024, entry version 194.
DE   RecName: Full=Protein smoothened;
DE            Short=dSMO;
DE   AltName: Full=SMOH;
DE   AltName: Full=Smooth;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24768000; DOI=10.1016/j.celrep.2014.03.052;
RA   Kuzhandaivel A., Schultz S.W., Alkhori L., Alenius M.;
RT   "Cilia-mediated hedgehog signaling in Drosophila.";
RL   Cell Rep. 7:672-680(2014).
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).
RN   [11] {ECO:0007744|PDB:2MAH}
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).
CC   -!- FUNCTION: Segment polarity protein required for correct patterning of
CC       every segment. G protein-coupled receptor which 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}. Cell projection, cilium
CC       {ECO:0000269|PubMed:24768000}.
CC   -!- TISSUE SPECIFICITY: Expressed in olfactory sensory neurons (at protein
CC       level). {ECO:0000269|PubMed:24768000}.
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   PDB; 8OIJ; X-ray; 2.00 A; C/D=970-1003.
DR   PDBsum; 2MAH; -.
DR   PDBsum; 8OIJ; -.
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   GlyCosmos; P91682; 7 sites, No reported glycans.
DR   GlyGen; P91682; 7 sites.
DR   iPTMnet; P91682; -.
DR   PaxDb; 7227-FBpp0077788; -.
DR   DNASU; 33196; -.
DR   EnsemblMetazoa; FBtr0078129; FBpp0077788; FBgn0003444.
DR   GeneID; 33196; -.
DR   KEGG; dme:Dmel_CG11561; -.
DR   UCSC; CG11561-RA; d. melanogaster.
DR   AGR; FB:FBgn0003444; -.
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; 2902735at2759; -.
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-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 cell types or tissues.
DR   ExpressionAtlas; P91682; baseline and differential.
DR   GO; GO:0005929; C:cilium; IDA:FlyBase.
DR   GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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:0030707; P:follicle cell of egg chamber development; IMP: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:0007389; P:pattern specification process; IBA:GO_Central.
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: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; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR035683; SMO_7TM.
DR   InterPro; IPR041771; SMO_CRD.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF35; SMOOTHENED HOMOLOG; 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; Frizzled cysteine-rich domain; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   Genevisible; P91682; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell projection; Developmental protein;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; 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, ECO:0007744|PDB:2MAH"
FT   DISULFID        100..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT                   ECO:0000269|PubMed:24351982, ECO:0007744|PDB:2MAH"
FT   DISULFID        139..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT                   ECO:0000269|PubMed:24351982, ECO:0007744|PDB:2MAH"
FT   DISULFID        172..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT                   ECO:0000269|PubMed:24351982, ECO:0007744|PDB:2MAH"
FT   DISULFID        218..238
FT                   /evidence="ECO:0000250|UniProtKB:Q99835"
FT   DISULFID        242..320
FT                   /evidence="ECO:0000250|UniProtKB:Q99835"
FT   DISULFID        339..413
FT                   /evidence="ECO:0000250|UniProtKB:Q99835"
FT   DISULFID        513..525
FT                   /evidence="ECO:0000250|UniProtKB:Q99835"
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"
FT   HELIX           977..988
FT                   /evidence="ECO:0007829|PDB:8OIJ"
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
//