ID A0A3P6HQ98_MESCO Unreviewed; 427 AA. AC A0A3P6HQ98; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 03-MAY-2023, entry version 16. DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812}; GN ORFNames=MCOS_LOCUS3479 {ECO:0000313|EMBL:VDD77476.1}; OS Mesocestoides corti (Flatworm). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda; OC Eucestoda; Cyclophyllidea; Mesocestoididae; Mesocestoides. OX NCBI_TaxID=53468 {ECO:0000313|EMBL:VDD77476.1, ECO:0000313|Proteomes:UP000267029}; RN [1] {ECO:0000313|EMBL:VDD77476.1, ECO:0000313|Proteomes:UP000267029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Pathogen Informatics; RL Submitted (OCT-2018) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid- CC anchor {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 --------------------------------------------------------------------------- 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; UXSR01000802; VDD77476.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3P6HQ98; -. DR STRING; 53468.A0A3P6HQ98; -. DR Proteomes; UP000267029; Unassembled WGS sequence. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro. DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro. 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; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR PANTHER; PTHR11889; HEDGEHOG; 1. DR PANTHER; PTHR11889:SF31; PROTEIN HEDGEHOG; 1. DR Pfam; PF01085; HH_signal; 1. DR Pfam; PF01079; Hint; 1. DR PRINTS; PR00632; SONICHHOG. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, KW ECO:0000256|RuleBase:RU280812}; Calcium {ECO:0000256|ARBA:ARBA00022837}; 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|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 Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812}; KW Reference proteome {ECO:0000313|Proteomes:UP000267029}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 219..325 FT /note="Hint" FT /evidence="ECO:0000259|SMART:SM00306" SQ SEQUENCE 427 AA; 48243 MW; 52B906869CD16116 CRC64; MQKLVSLIHN TWPNNDVVLR ILDGWIRPPP TLLRQPKVVT KRGYTERRKQ TLQMSVPEDL VDYEPPKRFR QVTGYHSSNS LGVKVANTDS RVVMQRPRDG ANQSEATPGS SIQSPYSVYR SRYWGEELPV MGFDGYRRQQ QQLQQHPVMM EEFHYAGRAV DMILVDARSS GSSRRSSIYP GKLAQLAYYG ALFDWCYFAR QGHVHCSVKP DSIITSQWFG CFPGSAKALS TAGSPIPLSA LRVGDSIMTL DSATNTLRLT QVIAFIHRDE HQYSPWIEIV YVRAGASTTG TLRLTANHIV YRWVGEKTAV FASDVRPHDK IACDFARSDI LCQVKEVRFR NSTHADVGVY APLTLTGDMI VDGVYVSCFA HVHSEWLARL AMLPLRLKHA LFGVTSTVPQ TGVHRYADWL LQIARFLLPN QLFFSPL //