ID A0A7K9X6B4_9GRUI Unreviewed; 425 AA. AC A0A7K9X6B4; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 29-MAY-2024, entry version 14. DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812}; DE Flags: Fragment; GN Name=Shh {ECO:0000313|EMBL:NXI92852.1}; GN ORFNames=PSOCRE_R04203 {ECO:0000313|EMBL:NXI92852.1}; OS Psophia crepitans (common trumpeter). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Gruiformes; Psophiidae; Psophia. OX NCBI_TaxID=54359 {ECO:0000313|EMBL:NXI92852.1, ECO:0000313|Proteomes:UP000587472}; RN [1] {ECO:0000313|EMBL:NXI92852.1, ECO:0000313|Proteomes:UP000587472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-001-60 {ECO:0000313|EMBL:NXI92852.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXI92852.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog CC protein N-product is a morphogen which is essential for a variety of CC patterning events during development. {ECO:0000256|RuleBase:RU280812}. CC -!- FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog CC protein precursor displays an autoproteolysis activity that results in CC the cleavage of the full-length protein into two parts (N-product and CC C-product). In addition, the C-terminal part displays a cholesterol CC transferase activity that results by the covalent attachment of a CC cholesterol moiety to the C-terminal of the newly generated N-product. CC {ECO:0000256|RuleBase:RU280812}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]- CC C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl- CC [protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA- CC COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, CC ChEBI:CHEBI:143140; Evidence={ECO:0000256|ARBA:ARBA00034065}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; CC Evidence={ECO:0000256|ARBA:ARBA00034065}; CC -!- SUBUNIT: Multimer. {ECO:0000256|ARBA:ARBA00034131}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004586}. Membrane CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004635}. CC -!- SUBCELLULAR LOCATION: [Sonic hedgehog protein]: Endoplasmic reticulum CC membrane {ECO:0000256|RuleBase:RU280812}. Golgi apparatus membrane CC {ECO:0000256|RuleBase:RU280812}. CC -!- SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane CC {ECO:0000256|RuleBase:RU280812}; Lipid-anchor CC {ECO:0000256|RuleBase:RU280812}. CC -!- SIMILARITY: Belongs to the hedgehog family. CC {ECO:0000256|ARBA:ARBA00010649, ECO:0000256|RuleBase:RU280812}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NXI92852.1}. 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; VWZZ01002220; NXI92852.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7K9X6B4; -. DR Proteomes; UP000587472; Unassembled WGS sequence. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:TreeGrafter. DR GO; GO:0005113; F:patched binding; IEA:TreeGrafter. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0048513; P:animal organ development; IEA:UniProt. DR GO; GO:0048468; P:cell development; IEA:UniProt. DR GO; GO:0001708; P:cell fate specification; IEA:TreeGrafter. DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro. DR GO; GO:0009790; P:embryo development; IEA:UniProt. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt. DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:TreeGrafter. DR GO; GO:0007389; P:pattern specification process; IEA:UniProt. DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt. DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProt. DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter. DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:TreeGrafter. DR GO; GO:0009888; P:tissue development; IEA:UniProt. DR GO; GO:0035295; P:tube development; IEA:UniProt. DR CDD; cd00081; Hint; 1. DR Gene3D; 3.30.1380.10; -; 1. DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1. DR InterPro; IPR001657; Hedgehog. DR InterPro; IPR001767; Hedgehog_Hint. DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf. DR InterPro; IPR000320; Hedgehog_signalling_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR006141; Intein_N. DR PANTHER; PTHR11889; HEDGEHOG; 1. DR PANTHER; PTHR11889:SF36; SONIC HEDGEHOG PROTEIN; 1. DR Pfam; PF01085; HH_signal; 1. DR Pfam; PF01079; Hint; 1. DR PIRSF; PIRSF009400; Peptidase_C46; 1. DR PRINTS; PR00632; SONICHHOG. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, KW ECO:0000256|RuleBase:RU280812}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR009400-2}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|RuleBase:RU280812}; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473, KW ECO:0000256|RuleBase:RU280812}; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU280812}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034, KW ECO:0000256|RuleBase:RU280812}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU280812}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280812}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR009400-2}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812}; KW Reference proteome {ECO:0000313|Proteomes:UP000587472}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR009400-2}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..425 FT /note="Hedgehog protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5029675991" FT DOMAIN 199..309 FT /note="Hint" FT /evidence="ECO:0000259|SMART:SM00306" FT DOMAIN 312..357 FT /note="Hint" FT /evidence="ECO:0000259|SMART:SM00305" FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 128 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 129 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 129 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2" FT SITE 200..201 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1" FT SITE 246 FT /note="Involved in cholesterol transfer" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1" FT SITE 270 FT /note="Involved in auto-cleavage" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1" FT SITE 273 FT /note="Essential for auto-cleavage" FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXI92852.1" FT NON_TER 425 FT /evidence="ECO:0000313|EMBL:NXI92852.1" SQ SEQUENCE 425 AA; 46572 MW; AF755EAA68F51E94 CRC64; MDEMLLLTRI LLVGFICALL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG ASGRYEGKIT RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW PGVKLRVTEG WDEDGHHSEE ALHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EQGGTKLVKD LSPGDRVLAA DAEGRLLYSD FLAFLDREDG SHKLFYVIET RQPRARLLLT AAHLVFVAPQ HNQSQEGTPS SRALFASHIR PGQRVYVLGE GGQQLLPAAV HSVSLREEAS GAYAPLTAQG TILINRVLAS CYAVIEEHSW AHWAFAPFRL LQGMLAALCP SAGGVPVGAP ADSGIHWYSR LLYRIGSWVL DSDSLHPLGM VVPSS //