ID A0A922HG47_DERFA Unreviewed; 582 AA. AC A0A922HG47; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-NOV-2024, entry version 7. DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812}; GN ORFNames=DERF_016016 {ECO:0000313|EMBL:KAH9491287.1}; OS Dermatophagoides farinae (American house dust mite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea; OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides. OX NCBI_TaxID=6954 {ECO:0000313|EMBL:KAH9491287.1, ECO:0000313|Proteomes:UP000790347}; RN [1] {ECO:0000313|EMBL:KAH9491287.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Derf {ECO:0000313|EMBL:KAH9491287.1}; RC TISSUE=Whole organism {ECO:0000313|EMBL:KAH9491287.1}; RA Yim A.K.Y., Chan T.F., Ji K.M., Liu X.Y., Zhou J.W., Li R.Q., Yang K.Y., RA Li J., Li M., Law P.T.W., Wu Y.L., Cai Z.L., Qin H., Bao Y., Leung R.K.K., RA Ng P.K.S., Zou J., Zhong X.J., Ran P.X., Zhong N.S., Liu Z.G., Tsui S.K.W.; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAH9491287.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Derf {ECO:0000313|EMBL:KAH9491287.1}; RC TISSUE=Whole organism {ECO:0000313|EMBL:KAH9491287.1}; RA Xiong Q., Wan A.T.-Y., Liu X.-Y., Fung C.S.-H., Xiao X., Malainual N., RA Hou J., Wang L., Wang M., Yang K., Cui Y., Leung E., Nong W., Shin S.-K., RA Au S., Jeong K.Y., Chew F.T., Hui J., Leung T.F., Tungtrongchitr A., RA Zhong N., Liu Z., Tsui S.; RT "Comparative Genomics Reveals Insights into the Divergent Evolution of RT Astigmatic Mites and Household Pest Adaptations."; RL Res Sq 0:0-0(2022). CC -!- FUNCTION: The C-terminal part of the hedgehog protein precursor CC displays an autoproteolysis activity that results in the cleavage of CC the full-length protein into two parts (N-product and C-product). In CC addition, the C-terminal part displays a cholesterol transferase CC activity that results by the covalent attachment of a cholesterol CC moiety to the C-terminal of the newly generated N-product. Once CC cleaved, the C-product has no signaling activity and diffuses from the CC cell. {ECO:0000256|ARBA:ARBA00045369}. 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=glycyl-L-cysteinyl-[protein] + cholesterol + 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: Interacts with shf. {ECO:0000256|ARBA:ARBA00011490}. 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:KAH9491287.1}. 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; ASGP02000009; KAH9491287.1; -; Genomic_DNA. DR Proteomes; UP000790347; 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:0016015; F:morphogen activity; IEA:UniProtKB-KW. 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:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-KW. DR GO; GO:0001708; P:cell fate specification; IEA:TreeGrafter. DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro. DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter. DR GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:TreeGrafter. DR GO; GO:0048731; P:system development; IEA:UniProt. DR CDD; cd00081; Hint; 1. DR FunFam; 2.170.16.10:FF:000001; Indian hedgehog; 1. DR FunFam; 3.30.1380.10:FF:000001; Indian hedgehog; 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; IPR050387; Hedgehog_Signaling. 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:SF31; PROTEIN HEDGEHOG; 1. DR Pfam; PF01085; HH_signal; 1. DR Pfam; PF01079; Hint; 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}; 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 Morphogen {ECO:0000256|ARBA:ARBA00023301}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812}; KW Reference proteome {ECO:0000313|Proteomes:UP000790347}; KW Segmentation polarity protein {ECO:0000256|ARBA:ARBA00022716}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 339..444 FT /note="Hint" FT /evidence="ECO:0000259|SMART:SM00306" FT DOMAIN 460..504 FT /note="Hint" FT /evidence="ECO:0000259|SMART:SM00305" FT REGION 104..138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..129 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 582 AA; 67344 MW; F9075C0B806ABE5B CRC64; MTNNDNIAIN DHYHDQQIWQ KSSNFINNNQ NHHHHHHNNN DNQCNRSIIM IDNETNHQYN KLNEIRTKSN DIIINVRLKM IDTLKFIIWL LPLSFMFEMK RSQQKSNQHQ LNSHHHHHQN HHRPYHHRSR SSSSSSTISI IDHQQQLMSI IIIIMLIIQQ SQLTMSCGPG RGGSRRRSPR KLIPLVFKQH VPNVSENTLG ASGLNEGPIT RNHRRFKELV PNYNQDILFK DEEGTGADRL MTQRLKEKLN TLAISVMNQW PGVRLRVTEG WDEDGSHASN SLHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES RFHIHCSVKS EKSESARNGG CFDQNSTVIG HNGQTINIDN LRIGDEILTM NPATGHLEYS SIIMFLDRNP SIERLYYEIE TEFGRMITAT PSHLLFISDT GNIDDKHEEF VSKIEMNQYL FVVMNQSDNQ NKSVAAAVAE TTPRLERIIR ISTKKSKGIY APLTVTGTIV VNNIVASCYA IINSQQLSHL SFIPIRWLYQ FIKFGDYLSQ QLHVHHSQLI IRTTKQSDQS PSPSSLPIGI HWYPRLLYTM FNYFIPNDYI YQ //