ID   IHH_TRIHE               Reviewed;          58 AA.
AC   P79866;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Indian hedgehog protein;
DE            Short=IHH;
DE   Flags: Fragment;
GN   Name=ihh;
OS   Trigonostigma heteromorpha (Harlequin rasbora) (Rasbora heteromorpha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Rasborinae; Trigonostigma.
OX   NCBI_TaxID=432397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Muscle;
RX   PubMed=8917540; DOI=10.1073/pnas.93.23.13036;
RA   Zardoya R., Abouheif E., Meyer A.;
RT   "Evolutionary analyses of hedgehog and Hoxd-10 genes in fish species
RT   closely related to the zebrafish.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13036-13041(1996).
CC   -!- FUNCTION: Intercellular signal essential for a variety of patterning
CC       events during development. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted,
CC       extracellular space {ECO:0000250}. Note=Indian hedgehog protein N-
CC       product: Cell membrane; Lipid-anchor; Extracellular side. The N-
CC       terminal peptide remains associated with the cell surface. Indian
CC       hedgehog protein C-product: Secreted, extracellular space. The C-
CC       terminal peptide diffuses from the cell. {ECO:0000250}.
CC   -!- DOMAIN: The indian hedgehog protein N-product binds calcium and zinc
CC       ions; this stabilizes the protein fold and is essential for protein-
CC       protein interactions mediated by this domain. {ECO:0000250}.
CC   -!- PTM: The C-terminal domain displays an autoproteolysis activity and a
CC       cholesterol transferase activity. Both activities result in the
CC       cleavage of the full-length protein and covalent attachment of a
CC       cholesterol moiety to the C-terminal of the newly generated N-terminal
CC       fragment (N-product). The N-product is the active species in both local
CC       and long-range signaling, whereas the C-product has no signaling
CC       activity (By similarity). {ECO:0000250}.
CC   -!- PTM: Cholesterylation is required for N-product targeting to lipid
CC       rafts and multimerization. {ECO:0000250}.
CC   -!- PTM: N-palmitoylation is required for N-product multimerization and
CC       full activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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DR   EMBL; U51383; AAB38610.1; -; Genomic_DNA.
DR   AlphaFoldDB; P79866; -.
DR   SMR; P79866; -.
DR   GO; GO:0005615; C:extracellular space; 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-KW.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR001657; Hedgehog.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR000320; Hedgehog_signalling_dom.
DR   InterPro; IPR033385; IHH.
DR   PANTHER; PTHR11889:SF39; PTHR11889:SF39; 1.
DR   Pfam; PF01085; HH_signal; 1.
DR   PRINTS; PR00632; SONICHHOG.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Calcium; Cell membrane; Developmental protein;
KW   Hydrolase; Lipoprotein; Membrane; Metal-binding; Palmitate; Protease;
KW   Secreted; Zinc.
FT   CHAIN           <1..>58
FT                   /note="Indian hedgehog protein"
FT                   /id="PRO_0000058748"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q14623"
FT   NON_TER         1
FT   NON_TER         58
SQ   SEQUENCE   58 AA;  6628 MW;  2CC8F53CF7056809 CRC64;
     VMNLWPGVRL RVTEGWDEDG HHSEESLHYE GRAVDITASD RDRNKYAMLA RLAVEAGF