ID PTC1_MOUSE Reviewed; 1434 AA. AC Q61115; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Protein patched homolog 1; DE Short=PTC; DE Short=PTC1; GN Name=Ptch1; Synonyms=Ptch; 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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX PubMed=8595881; DOI=10.1101/gad.10.3.301; RA Goodrich L.V., Johnson R.L., Milenkovic L., McMahon J.A., Scott M.P.; RT "Conservation of the hedgehog/patched signaling pathway from flies to mice: RT induction of a mouse patched gene by Hedgehog."; RL Genes Dev. 10:301-312(1996). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1181 AND SER-1183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] RP FUNCTION, AND INTERACTION WITH IHH. RX PubMed=21537345; DOI=10.1038/cr.2011.76; RA Ma G., Yu J., Xiao Y., Chan D., Gao B., Hu J., He Y., Guo S., Zhou J., RA Zhang L., Gao L., Zhang W., Kang Y., Cheah K.S., Feng G., Guo X., Wang Y., RA Zhou C.Z., He L.; RT "Indian hedgehog mutations causing brachydactyly type A1 impair Hedgehog RT signal transduction at multiple levels."; RL Cell Res. 21:1343-1357(2011). RN [4] RP INTERACTION WITH GPR37L1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=24062445; DOI=10.1073/pnas.1314819110; RA Marazziti D., Di Pietro C., Golini E., Mandillo S., La Sala G., RA Matteoni R., Tocchini-Valentini G.P.; RT "Precocious cerebellum development and improved motor functions in mice RT lacking the astrocyte cilium-, patched 1-associated Gpr37l1 receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 110:16486-16491(2013). RN [5] RP UBIQUITINATION AT LYS-1413, AND MUTAGENESIS OF LYS-1413. RX PubMed=25092867; DOI=10.1128/mcb.00960-14; RA Chen X.L., Chinchilla P., Fombonne J., Ho L., Guix C., Keen J.H., RA Mehlen P., Riobo N.A.; RT "Patched-1 proapoptotic activity is downregulated by modification of K1413 RT by the E3 ubiquitin-protein ligase Itchy homolog."; RL Mol. Cell. Biol. 34:3855-3866(2014). CC -!- FUNCTION: Acts as a receptor for sonic hedgehog (SHH), indian hedgehog CC (IHH) and desert hedgehog (DHH). Associates with the smoothened protein CC (SMO) to transduce the hedgehog's proteins signal. Seems to have a CC tumor suppressor function, as inactivation of this protein is probably CC a necessary, if not sufficient step for tumorigenesis. CC {ECO:0000269|PubMed:21537345}. CC -!- SUBUNIT: Interacts with SNX17 (By similarity). Interacts with IHH CC (PubMed:21537345). Interacts with G-protein coupled receptor GPR37L1 CC (PubMed:24062445). {ECO:0000250|UniProtKB:Q13635, CC ECO:0000269|PubMed:21537345, ECO:0000269|PubMed:24062445}. CC -!- INTERACTION: CC Q61115; Q96EY1: DNAJA3; Xeno; NbExp=2; IntAct=EBI-15619523, EBI-356767; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24062445}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Detected in cerebellar Bergmann glia cells (at CC protein level) (PubMed:24062445). In the developing embryo, first CC detected within the ventral neural tube and later in the somites and CC limb buds (PubMed:8595881). Expression in the limb buds is restricted CC to the posterior ectoderm surrounding the zone of polarizing activity CC (PubMed:8595881). In the adult, expression is seen in brain, lung, CC liver, kidney and ocular tissues; lower levels in heart, skeletal CC muscle, and testis (PubMed:8595881). {ECO:0000269|PubMed:24062445, CC ECO:0000269|PubMed:8595881}. CC -!- DEVELOPMENTAL STAGE: Expressed at very low levels at 7 dpc, is most CC strongly expressed between 11 and 15 dpc, and persists at moderate CC levels at 17 dpc (PubMed:8595881). Also expressed in the adult CC (PubMed:8595881). {ECO:0000269|PubMed:8595881}. CC -!- INDUCTION: Activated by Sonic hedgehog. CC -!- PTM: Glycosylation is necessary for SHH binding. {ECO:0000250}. CC -!- PTM: In the absence of Hh ligands, ubiquitination by ITCH at Lys-1413 CC promotes endocytosis and both proteasomal and lysosomal degradation. CC {ECO:0000269|PubMed:25092867}. CC -!- SIMILARITY: Belongs to the patched family. {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; U46155; AAC98798.1; -; mRNA. DR CCDS; CCDS26592.1; -. DR PIR; T30172; T30172. DR RefSeq; NP_032983.1; NM_008957.3. DR RefSeq; XP_006517222.1; XM_006517159.3. DR PDB; 6MG8; EM; 3.60 A; A=1-1291. DR PDB; 7K65; EM; 3.40 A; A=1-1291. DR PDB; 7V6Y; EM; 3.50 A; A=2-1175. DR PDB; 7V6Z; EM; 3.64 A; A=2-1175. DR PDBsum; 6MG8; -. DR PDBsum; 7K65; -. DR PDBsum; 7V6Y; -. DR PDBsum; 7V6Z; -. DR AlphaFoldDB; Q61115; -. DR EMDB; EMD-22689; -. DR EMDB; EMD-31753; -. DR EMDB; EMD-31754; -. DR EMDB; EMD-9111; -. DR SMR; Q61115; -. DR BioGRID; 202444; 4. DR DIP; DIP-60268N; -. DR IntAct; Q61115; 1. DR STRING; 10090.ENSMUSP00000021921; -. DR GlyCosmos; Q61115; 6 sites, No reported glycans. DR GlyGen; Q61115; 6 sites. DR iPTMnet; Q61115; -. DR PhosphoSitePlus; Q61115; -. DR jPOST; Q61115; -. DR PaxDb; 10090-ENSMUSP00000021921; -. DR ProteomicsDB; 291582; -. DR Antibodypedia; 4435; 787 antibodies from 40 providers. DR DNASU; 19206; -. DR Ensembl; ENSMUST00000021921.11; ENSMUSP00000021921.6; ENSMUSG00000021466.13. DR GeneID; 19206; -. DR KEGG; mmu:19206; -. DR UCSC; uc007qxv.1; mouse. DR AGR; MGI:105373; -. DR CTD; 5727; -. DR MGI; MGI:105373; Ptch1. DR VEuPathDB; HostDB:ENSMUSG00000021466; -. DR eggNOG; KOG1935; Eukaryota. DR GeneTree; ENSGT00940000159011; -. DR InParanoid; Q61115; -. DR OMA; HLYDTEW; -. DR OrthoDB; 1219406at2759; -. DR PhylomeDB; Q61115; -. DR TreeFam; TF106489; -. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5632681; Ligand-receptor interactions. DR Reactome; R-MMU-5632684; Hedgehog 'on' state. DR Reactome; R-MMU-5635838; Activation of SMO. DR BioGRID-ORCS; 19206; 8 hits in 82 CRISPR screens. DR ChiTaRS; Ptch1; mouse. DR PRO; PR:Q61115; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q61115; Protein. DR Bgee; ENSMUSG00000021466; Expressed in associated mesenchyme of midgut and 442 other cell types or tissues. DR ExpressionAtlas; Q61115; baseline and differential. DR GO; GO:0045177; C:apical part of cell; ISO:MGI. DR GO; GO:0044295; C:axonal growth cone; ISO:MGI. DR GO; GO:0005901; C:caveola; ISO:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI. DR GO; GO:0005576; C:extracellular region; TAS:Roslin. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; ISO:MGI. DR GO; GO:0030332; F:cyclin binding; IPI:BHF-UCL. DR GO; GO:0097108; F:hedgehog family protein binding; ISO:MGI. DR GO; GO:0008158; F:hedgehog receptor activity; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; IDA:Roslin. DR GO; GO:0005113; F:patched binding; IDA:Roslin. DR GO; GO:0044877; F:protein-containing complex binding; IDA:BHF-UCL. DR GO; GO:0005119; F:smoothened binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; NAS:Roslin. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0007420; P:brain development; IMP:BHF-UCL. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI. DR GO; GO:0061005; P:cell differentiation involved in kidney development; IGI:MGI. DR GO; GO:0001709; P:cell fate determination; IGI:MGI. DR GO; GO:0072203; P:cell proliferation involved in metanephros development; IMP:MGI. DR GO; GO:0071397; P:cellular response to cholesterol; IEP:BHF-UCL. DR GO; GO:0071679; P:commissural neuron axon guidance; ISO:MGI. DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI. DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI. DR GO; GO:0048568; P:embryonic organ development; IGI:MGI. DR GO; GO:0009957; P:epidermal cell fate specification; IGI:MGI. DR GO; GO:0008544; P:epidermis development; IMP:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI. DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI. DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI. DR GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI. DR GO; GO:0035108; P:limb morphogenesis; ISO:MGI. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0030879; P:mammary gland development; IMP:MGI. DR GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:MGI. DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:MGI. DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl. DR GO; GO:0051782; P:negative regulation of cell division; IMP:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:CACAO. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:MGI. DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0021997; P:neural plate axis specification; IMP:BHF-UCL. DR GO; GO:0001843; P:neural tube closure; IMP:MGI. DR GO; GO:0001841; P:neural tube formation; IDA:Roslin. DR GO; GO:0021532; P:neural tube patterning; ISO:MGI. DR GO; GO:0007389; P:pattern specification process; IMP:MGI. DR GO; GO:0060037; P:pharyngeal system development; ISO:MGI. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:CACAO. DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IGI:MGI. DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI. DR GO; GO:0016485; P:protein processing; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0040008; P:regulation of growth; IMP:MGI. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI. DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL. DR GO; GO:0010157; P:response to chlorate; IDA:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IDA:Roslin. DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl. DR GO; GO:0061053; P:somite development; IMP:BHF-UCL. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI. DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR003392; Ptc/Disp. DR InterPro; IPR000731; SSD. DR InterPro; IPR004766; TM_rcpt_patched. DR NCBIfam; TIGR00918; 2A060602; 1. DR PANTHER; PTHR46022; PROTEIN PATCHED; 1. DR PANTHER; PTHR46022:SF5; PROTEIN PATCHED HOMOLOG 1; 1. DR Pfam; PF02460; Patched; 1. DR Pfam; PF12349; Sterol-sensing; 1. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. DR PROSITE; PS50156; SSD; 1. DR Genevisible; Q61115; MM. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Glycoprotein; Isopeptide bond; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1..1434 FT /note="Protein patched homolog 1" FT /id="PRO_0000205965" FT TOPO_DOM 1..86 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 108..422 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 423..443 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 444..458 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 459..479 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 480..487 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 488..508 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 509..533 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 534..554 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 555..563 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 564..584 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 585..734 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 735..755 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 756..1013 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1014..1034 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1035..1039 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1040..1060 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1061..1069 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1070..1090 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1091..1107 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1108..1128 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1129..1140 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1141..1161 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1162..1434 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 424..584 FT /note="SSD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1175..1219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1257..1348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1368..1396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1179..1193 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1199..1219 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1264..1285 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1288..1312 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1332..1348 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1181 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 335 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 400 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 861 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 986 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CROSSLNK 1413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:25092867" FT MUTAGEN 1413 FT /note="K->R: Accumulates at the plasma membrane, increased FT half-life and increased CASP9-mediated cell death." FT /evidence="ECO:0000269|PubMed:25092867" FT HELIX 61..82 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 86..99 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 100..103 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 134..138 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 140..152 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 158..172 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 202..209 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 217..220 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 222..227 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 274..278 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:7V6Y" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:7V6Y" FT HELIX 305..309 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 336..343 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 346..352 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 355..362 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 375..395 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 402..408 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 412..420 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 425..443 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 445..450 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 453..477 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 484..487 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 489..512 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 515..517 FT /evidence="ECO:0007829|PDB:7V6Y" FT HELIX 519..521 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 522..548 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 554..576 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 578..587 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 718..725 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 728..731 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 733..753 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 763..765 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 769..771 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 772..783 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 787..793 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 798..800 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 802..811 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 812..814 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 822..824 FT /evidence="ECO:0007829|PDB:7V6Y" FT HELIX 830..850 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 864..873 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 879..881 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 886..889 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 895..897 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 905..915 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 917..923 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 943..946 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 957..964 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 971..988 FT /evidence="ECO:0007829|PDB:7K65" FT TURN 989..991 FT /evidence="ECO:0007829|PDB:7K65" FT STRAND 994..998 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 999..1001 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1006..1008 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1010..1033 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1036..1060 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1066..1078 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1079..1081 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1084..1091 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1097..1124 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1125..1128 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1132..1137 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1139..1153 FT /evidence="ECO:0007829|PDB:7K65" FT HELIX 1156..1163 FT /evidence="ECO:0007829|PDB:7K65" SQ SEQUENCE 1434 AA; 159273 MW; A5E9189E633173D0 CRC64; MASAGNAAGA LGRQAGGGRR RRTGGPHRAA PDRDYLHRPS YCDAAFALEQ ISKGKATGRK APLWLRAKFQ RLLFKLGCYI QKNCGKFLVV GLLIFGAFAV GLKAANLETN VEELWVEVGG RVSRELNYTR QKIGEEAMFN PQLMIQTPKE EGANVLTTEA LLQHLDSALQ ASRVHVYMYN RQWKLEHLCY KSGELITETG YMDQIIEYLY PCLIITPLDC FWEGAKLQSG TAYLLGKPPL RWTNFDPLEF LEELKKINYQ VDSWEEMLNK AEVGHGYMDR PCLNPADPDC PATAPNKNST KPLDVALVLN GGCQGLSRKY MHWQEELIVG GTVKNATGKL VSAHALQTMF QLMTPKQMYE HFRGYDYVSH INWNEDRAAA ILEAWQRTYV EVVHQSVAPN STQKVLPFTT TTLDDILKSF SDVSVIRVAS GYLLMLAYAC LTMLRWDCSK SQGAVGLAGV LLVALSVAAG LGLCSLIGIS FNAATTQVLP FLALGVGVDD VFLLAHAFSE TGQNKRIPFE DRTGECLKRT GASVALTSIS NVTAFFMAAL IPIPALRAFS LQAAVVVVFN FAMVLLIFPA ILSMDLYRRE DRRLDIFCCF TSPCVSRVIQ VEPQAYTEPH SNTRYSPPPP YTSHSFAHET HITMQSTVQL RTEYDPHTHV YYTTAEPRSE ISVQPVTVTQ DNLSCQSPES TSSTRDLLSQ FSDSSLHCLE PPCTKWTLSS FAEKHYAPFL LKPKAKVVVI LLFLGLLGVS LYGTTRVRDG LDLTDIVPRE TREYDFIAAQ FKYFSFYNMY IVTQKADYPN IQHLLYDLHK SFSNVKYVML EENKQLPQMW LHYFRDWLQG LQDAFDSDWE TGRIMPNNYK NGSDDGVLAY KLLVQTGSRD KPIDISQLTK QRLVDADGII NPSAFYIYLT AWVSNDPVAY AASQANIRPH RPEWVHDKAD YMPETRLRIP AAEPIEYAQF PFYLNGLRDT SDFVEAIEKV RVICNNYTSL GLSSYPNGYP FLFWEQYISL RHWLLLSISV VLACTFLVCA VFLLNPWTAG IIVMVLALMT VELFGMMGLI GIKLSAVPVV ILIASVGIGV EFTVHVALAF LTAIGDKNHR AMLALEHMFA PVLDGAVSTL LGVLMLAGSE FDFIVRYFFA VLAILTVLGV LNGLVLLPVL LSFFGPCPEV SPANGLNRLP TPSPEPPPSV VRFAVPPGHT NNGSDSSDSE YSSQTTVSGI SEELRQYEAQ QGAGGPAHQV IVEATENPVF ARSTVVHPDS RHQPPLTPRQ QPHLDSGSLS PGRQGQQPRR DPPREGLRPP PYRPRRDAFE ISTEGHSGPS NRDRSGPRGA RSHNPRNPTS TAMGSSVPSY CQPITTVTAS ASVTVAVHPP PGPGRNPRGG PCPGYESYPE TDHGVFEDPH VPFHVRCERR DSKVEVIELQ DVECEERPWG SSSN //