TWHH_DEVPA
ID TWHH_DEVPA Reviewed; 53 AA.
AC O13253; O13223;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Tiggy-winkle hedgehog protein;
DE Flags: Fragment;
GN Name=twhh;
OS Devario pathirana (Barred danio) (Danio pathirana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Devario.
OX NCBI_TaxID=46779;
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. Involved in dorso-ventral patterning of the
CC brain and in early patterning of the developing eyes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}. Note=Tiggy-winkle hedgehog protein
CC N-product: Cell membrane; Lipid-anchor; Extracellular side. The N-
CC terminal peptide remains associated with the cell surface. Tiggy-winkle
CC hedgehog protein C-product: Secreted, extracellular space. The C-
CC terminal peptide diffuses from the cell. {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). This covalent modification appears to play an
CC essential role in restricting the spatial distribution of the protein
CC activity to the cell surface. The N-product is the active species in
CC both local and long-range signaling, whereas the C-product has no
CC signaling activity (By similarity). {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; U68240; AAB38680.1; -; Genomic_DNA.
DR AlphaFoldDB; O13253; -.
DR SMR; O13253; -.
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 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; Membrane; Metal-binding; Protease; Secreted; Zinc.
FT CHAIN <1..>53
FT /note="Tiggy-winkle hedgehog protein"
FT /id="PRO_0000058756"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT NON_TER 1
FT NON_TER 53
SQ SEQUENCE 53 AA; 6063 MW; 23B2874EC9A10268 CRC64;
NSLAISVMNQ WPGVKLRVTE GWDEDGHHFE ESLHYEGRAV DITTSDRDKS KYG
