IHH_RASPA
ID IHH_RASPA Reviewed; 58 AA.
AC P79871;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Indian hedgehog protein;
DE Short=IHH;
DE Flags: Fragment;
GN Name=ihh;
OS Rasbora paviana (Sidestripe rasbora).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Rasborinae; Rasbora.
OX NCBI_TaxID=38659;
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}.
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; U51378; AAB38611.1; -; Genomic_DNA.
DR AlphaFoldDB; P79871; -.
DR SMR; P79871; -.
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_0000058749"
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; 6688 MW; A438F53CEC1A1735 CRC64;
VMNLWPGVRL RVMEGWDEDG HHSEESLHYE GRAVDITTSD RDRNKYAMLA RLAVEAGF
