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Sonic hedgehog protein (SHH) (Fragments)

 SHH_DEVAE               Reviewed;         121 AA.
O13234; O13190; O13199; O13239;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
22-NOV-2017, entry version 85.
RecName: Full=Sonic hedgehog protein;
Short=SHH;
Flags: Fragments;
Name=shh;
Devario aequipinnatus (Giant danio) (Danio aequipinnatus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Devario.
NCBI_TaxID=46778;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Muscle;
PubMed=8917540; DOI=10.1073/pnas.93.23.13036;
Zardoya R., Abouheif E., Meyer A.;
"Evolutionary analyses of hedgehog and Hoxd-10 genes in fish species
closely related to the zebrafish.";
Proc. Natl. Acad. Sci. U.S.A. 93:13036-13041(1996).
-!- FUNCTION: Intercellular signal essential for a variety of
patterning events during development. Signal produced by the
notochord that induces somite patterning, dorso-ventral patterning
of the brain and early patterning of the developing eyes. Displays
floor plate-inducing activity. Binds to the patched (PTC)
receptor, which functions in association with smoothened (SMO), to
activate the transcription of target genes. In the absence of SHH,
PTC represses the constitutive signaling activity of SMO (By
similarity). {ECO:0000250}.
-!- SUBUNIT: N-product is active as a multimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Sonic hedgehog protein C-product: Secreted,
extracellular space. Sonic hedgehog protein N-product: Cell
membrane; Lipid-anchor. The C-terminal peptide diffuses from the
cell, while the N-product either remains associated with lipid
rafts at the cell surface, or forms freely diffusible active
multimers with its hydrophobic lipid-modified N- and C-termini
buried inside. {ECO:0000250}.
-!- DOMAIN: The sonic hedgehog protein N-product binds calcium and
zinc ions; this stabilizes the protein fold and is essential for
protein-protein interactions mediated by this domain.
{ECO:0000250}.
-!- PTM: The C-terminal domain displays an autoproteolysis activity
and a cholesterol transferase activity. Both activities result in
the cleavage of the full-length protein and covalent attachment of
a cholesterol moiety to the C-terminal of the newly generated N-
terminal fragment (N-product). The N-product is the active species
in both local and long-range signaling, whereas the C-product has
no signaling activity.
-!- PTM: Cholesterylation is required for N-product targeting to lipid
rafts and multimerization. {ECO:0000250}.
-!- PTM: N-palmitoylation is required for N-product multimerization
and full activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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EMBL; U51344; AAB38566.1; -; Genomic_DNA.
EMBL; U51363; AAB38586.1; -; Genomic_DNA.
ProteinModelPortal; O13234; -.
SMR; O13234; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
Gene3D; 3.30.1380.10; -; 2.
InterPro; IPR001657; Hedgehog.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR000320; Hedgehog_signalling_dom.
Pfam; PF01085; HH_signal; 1.
PRINTS; PR00632; SONICHHOG.
SUPFAM; SSF55166; SSF55166; 1.
3: Inferred from homology;
Autocatalytic cleavage; Calcium; Cell membrane; Developmental protein;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Palmitate; Protease;
Secreted; Zinc.
CHAIN <1 >121 Sonic hedgehog protein.
/FTId=PRO_0000058724.
METAL 60 60 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 61 61 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 61 61 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 76 76 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q15465}.
METAL 77 77 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 77 77 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 80 80 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 82 82 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 91 91 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 98 98 Zinc. {ECO:0000250|UniProtKB:Q15465}.
NON_CONS 63 64 {ECO:0000305}.
NON_TER 1 1
NON_TER 121 121
SEQUENCE 121 AA; 14012 MW; A58A2DE40573825C CRC64;
YGRRRHPKKL TPLAYKQFIP NVAEKTLGAS GRYEGKITRN SERFKELTPN YNPDIIFKDE
ENTVMNHWPG VKLRVTEGWD EDGHHFEESL HYEGRAVDIT TSDRDKSKYG TLSRLAVEAG
F


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