PTC1_MOUSE
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 03-AUG-2022, entry version 172.
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}.
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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 SMR; Q61115; -.
DR BioGRID; 202444; 3.
DR DIP; DIP-60268N; -.
DR IntAct; Q61115; 1.
DR STRING; 10090.ENSMUSP00000021921; -.
DR GlyGen; Q61115; 6 sites.
DR iPTMnet; Q61115; -.
DR PhosphoSitePlus; Q61115; -.
DR jPOST; Q61115; -.
DR PaxDb; Q61115; -.
DR PRIDE; Q61115; -.
DR ProteomicsDB; 291582; -.
DR Antibodypedia; 4435; 706 antibodies from 40 providers.
DR DNASU; 19206; -.
DR Ensembl; ENSMUST00000021921; ENSMUSP00000021921; ENSMUSG00000021466.
DR GeneID; 19206; -.
DR KEGG; mmu:19206; -.
DR UCSC; uc007qxv.1; mouse.
DR CTD; 5727; -.
DR MGI; MGI:105373; Ptch1.
DR VEuPathDB; HostDB:ENSMUSG00000021466; -.
DR eggNOG; KOG1935; Eukaryota.
DR GeneTree; ENSGT00940000159011; -.
DR InParanoid; Q61115; -.
DR OMA; LTKECWF; -.
DR OrthoDB; 1190129at2759; -.
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; 7 hits in 77 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 438 other tissues.
DR ExpressionAtlas; Q61115; baseline and differential.
DR Genevisible; Q61115; MM.
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; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
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:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
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; IGI:BHF-UCL.
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:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
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:0045606; P:positive regulation of epidermal cell differentiation; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
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:0007224; P:smoothened signaling pathway; IDA:MGI.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IMP:MGI.
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 InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR InterPro; IPR004766; TM_rcpt_patched.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR TIGRFAMs; TIGR00918; 2A060602; 1.
DR PROSITE; PS50156; SSD; 1.
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
