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HH_DROPE
ID   HH_DROPE                Reviewed;         481 AA.
AC   B4G2I8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein hedgehog {ECO:0000250|UniProtKB:Q02936};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q62226};
DE   Contains:
DE     RecName: Full=Protein hedgehog N-product {ECO:0000250|UniProtKB:Q02936};
DE   Flags: Precursor;
GN   Name=hh {ECO:0000250|UniProtKB:Q02936}; ORFNames=GL23598;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1] {ECO:0000312|EMBL:EDW24033.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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) (By similarity). In addition, the C-terminal part displays a
CC       cholesterol transferase activity that results by the covalent
CC       attachment of a cholesterol moiety to the C-terminal of the newly
CC       generated N-product (By similarity). Once cleaved, the C-product has no
CC       signaling activity and diffuses from the cell (By similarity).
CC       {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.
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. Establishes the anterior-
CC       posterior axis of the embryonic segments and patterns the larval
CC       imaginal disks. Binds to the patched (ptc) receptor, which functions in
CC       association with smoothened (smo), to activate the transcription of
CC       target genes wingless (wg), decapentaplegic (dpp) and ptc. In the
CC       absence of hh, ptc represses the constitutive signaling activity of smo
CC       through fused (fu). Essential component of a signaling pathway which
CC       regulates the Duox-dependent gut immune response to bacterial uracil;
CC       required to activate Cad99C-dependent endosome formation, norpA-
CC       dependent Ca2+ mobilization and p38 MAPK, which are essential steps in
CC       the Duox-dependent production of reactive oxygen species (ROS) in
CC       response to intestinal bacterial infection. During photoreceptor
CC       differentiation, it up-regulates transcription of Ubr3, which in turn
CC       promotes the hh-signaling pathway by mediating the ubiquitination and
CC       degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- CATALYTIC ACTIVITY: [Protein hedgehog]:
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:0000250|UniProtKB:Q62226};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC         Evidence={ECO:0000250|UniProtKB:Q62226};
CC   -!- SUBUNIT: Interacts with shf. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10
CC       and then at stage 11 shifts to the cytoplasm. Also secreted in either
CC       cleaved or uncleaved form to mediate signaling to other cells.
CC       {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane
CC       {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains
CC       associated with the cell surface. Heparan sulfate proteoglycans of the
CC       extracellular matrix play an essential role in diffusion. Lipophorin is
CC       required for diffusion, probably by acting as vehicle for its movement,
CC       explaining how it can spread over long distances despite its
CC       lipidation. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein
CC       precursor displays an autoproteolysis activity that results in the
CC       cleavage of the full-length protein into two parts (N-product and C-
CC       product) (By similarity). In addition, the C-terminal part displays a
CC       cholesterol transferase activity that results by the covalent
CC       attachment of a cholesterol moiety to the C-terminal of the newly
CC       generated N-product (By similarity). The N-product is the active
CC       species in both local and long-range signaling, whereas the C-product
CC       has no signaling activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465,
CC       ECO:0000250|UniProtKB:Q62226}.
CC   -!- PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-
CC       product targeting to lipid rafts and multimerization.
CC       {ECO:0000250|UniProtKB:Q62226}.
CC   -!- PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the
CC       hedgehog N-product, within the secretory pathway, is required for the
CC       embryonic and larval patterning activities of the hedgehog signal.
CC       {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000255}.
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DR   EMBL; CH479179; EDW24033.1; -; Genomic_DNA.
DR   RefSeq; XP_002013047.1; XM_002013011.1.
DR   AlphaFoldDB; B4G2I8; -.
DR   SMR; B4G2I8; -.
DR   STRING; 7234.FBpp0187705; -.
DR   MEROPS; C46.001; -.
DR   EnsemblMetazoa; FBtr0189213; FBpp0187705; FBgn0161188.
DR   GeneID; 6587458; -.
DR   KEGG; dpe:6587458; -.
DR   eggNOG; KOG3638; Eukaryota.
DR   HOGENOM; CLU_034686_0_0_1; -.
DR   OMA; APAVRGC; -.
DR   PhylomeDB; B4G2I8; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016015; F:morphogen activity; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR   GO; GO:0007367; P:segment polarity determination; ISS:UniProtKB.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   Gene3D; 3.30.1380.10; -; 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   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; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Calcium; Cell membrane; Cytoplasm;
KW   Developmental protein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Morphogen; Nucleus; Palmitate; Protease; Reference proteome;
KW   Segmentation polarity protein; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..92
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000383066"
FT   CHAIN           93..481
FT                   /note="Protein hedgehog"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT                   /id="PRO_0000383067"
FT   CHAIN           93..265
FT                   /note="Protein hedgehog N-product"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT                   /id="PRO_0000383068"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         193
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   SITE            265..266
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            311
FT                   /note="Involved in cholesterol transfer"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            334
FT                   /note="Involved in auto-cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            337
FT                   /note="Essential for auto-cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   LIPID           93
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   LIPID           265
FT                   /note="Cholesterol glycine ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
SQ   SEQUENCE   481 AA;  53482 MW;  22660B90C7D72BAE CRC64;
     MDNHNEVPMS MSAPWASAAR VTCLSLDAKC HRPCPSSISA SASASGCASD SAAIATTKLR
     HIAYTQRCSS RLTMLMTVLL LLLPLSFTPA HSCGPGRGLG RRRERNLYPL VLKQTIPNLS
     EYQSGASGPL EGEIKRDSPK FKDLVPNYNR DILFRDEEGT GADRLMTKRC KEKLNVLAYS
     VMNEWPGVRL LVTESWDEDH QHGQESLHYE GRAVTIATSD REPSRYGMLA RLAVEAGFDW
     VSYVSRRHIY CSVKSDSSIS SHVHGCFTPE STALLESGIT KPLSEIAIGD RVLSMGSNGQ
     PVYSEVILFM DRNLEQMQNF VELHTDGGAV LTVTPAHLIS VWHPERQQLD YVFADRVEEL
     NYVLVRDPQT GELRPQRVVR VGSVRSKGVV APLTREGTIV VNSVAASCYA VIDSQSLAHW
     GLAPMRILAM LQSWMPAKDQ LRSSQTEGVV SRAEQQNGIH WYANALYKVK DYVLPKSWRH
     D
 
 
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