##gff-version 3 Q62226 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15465 Q62226 UniProtKB Chain 25 437 . . . ID=PRO_0000013211;Note=Sonic hedgehog protein Q62226 UniProtKB Chain 25 198 . . . ID=PRO_0000013212;Note=Sonic hedgehog protein N-product Q62226 UniProtKB Motif 33 39 . . . Note=Cardin-Weintraub;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23118222;Dbxref=PMID:23118222 Q62226 UniProtKB Binding site 90 90 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 91 91 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 91 91 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 96 96 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 126 126 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 127 127 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 127 127 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 130 130 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 132 132 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495 Q62226 UniProtKB Binding site 141 141 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495,ECO:0000269|PubMed:7477329;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495,PMID:7477329 Q62226 UniProtKB Binding site 148 148 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495,ECO:0000269|PubMed:7477329;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495,PMID:7477329 Q62226 UniProtKB Binding site 183 183 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18794898,ECO:0000269|PubMed:19561611,ECO:0000269|PubMed:20519495,ECO:0000269|PubMed:7477329;Dbxref=PMID:18794898,PMID:19561611,PMID:20519495,PMID:7477329 Q62226 UniProtKB Site 198 199 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02936 Q62226 UniProtKB Site 244 244 . . . Note=Involved in cholesterol transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02936 Q62226 UniProtKB Site 268 268 . . . Note=Involved in auto-cleavage;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02936 Q62226 UniProtKB Site 271 271 . . . Note=Essential for auto-cleavage;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02936 Q62226 UniProtKB Lipidation 25 25 . . . Note=N-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486055,ECO:0000269|PubMed:15075292;Dbxref=PMID:11486055,PMID:15075292 Q62226 UniProtKB Lipidation 198 198 . . . Note=Cholesterol glycine ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8824192;Dbxref=PMID:8824192 Q62226 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q62226 UniProtKB Mutagenesis 25 25 . . . Note=Strongly reduces effects of in vivo overexpression%3B impairs multimer formation%3B does not affect subcellular location to lipid rafts. Homozygous mice are characterized by a smaller size and holoprosencephaly at 10.5 dpc%2C and shortening of limbs at 13.5 dpc. They die soon after birth. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486055,ECO:0000269|PubMed:15075292,ECO:0000269|PubMed:23118222;Dbxref=PMID:11486055,PMID:15075292,PMID:23118222 Q62226 UniProtKB Mutagenesis 32 32 . . . Note=Introduces a cleavage site for a furin-like protease resulting in abnormal protein processing%3B cleavage at this site removes 11 amino acids from the N-terminal domain and reduces affinity of Shh for Ptch1 and signaling potency in assays using chicken embryo neural plate explants and mouse C3H10T1/2 stem cells. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 89 89 . . . Note=Moderately reduces Ptch1 binding in vitro and signaling potency in chicken embryo neural plate explant assays compared with wild-type sequence. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 101 101 . . . Note=Does not affect signaling activity in any of Shh signaling assays and causes no apparent defects in cholesterol-mediated autoprocessing reactions. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 116 116 . . . Note=Shows no change in activities at different temperatures. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 118 118 . . . Note=Causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells%3B causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius%3B drastically reduces signaling potency in chicken embryo neural plate explant assays. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 118 118 . . . Note=Causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells%3B causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius%3B drastically reduces signaling potency in chicken embryo neural plate explant assays. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Mutagenesis 189 189 . . . Note=Does not affect signaling activity in any of Shh signaling assays and causes no apparent defects in cholesterol-mediated autoprocessing reactions. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16282375;Dbxref=PMID:16282375 Q62226 UniProtKB Beta strand 48 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Turn 57 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3N1R Q62226 UniProtKB Helix 72 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Helix 101 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 123 127 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 131 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WG4 Q62226 UniProtKB Helix 140 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 146 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Helix 159 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 172 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Beta strand 181 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH Q62226 UniProtKB Helix 189 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VHH