|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Limb bud;
DOI=10.1016/0092-8674(93)90626-2; PubMed=8269518 [NCBI, ExPASy, EBI, Israel, Japan]
Riddle R.D.,
Johnson R.L.,
Laufer E.,
Tabin C.;
"Sonic hedgehog mediates the polarizing activity of the ZPA.";
Cell 75:1401-1416(1993).
|
[2]
|
FUNCTION, AND AUTOPROTEOLYTIC CLEAVAGE.
DOI=10.1016/0092-8674(95)90397-6; PubMed=7736596 [NCBI, ExPASy, EBI, Israel, Japan]
Roelink H.,
Porter J.A.,
Chiang C.,
Tanabe Y.,
Chang D.T.,
Beachy P.A.,
Jessell T.M.;
"Floor plate and motor neuron induction by different concentrations of the amino-terminal cleavage product of sonic hedgehog autoproteolysis.";
Cell 81:445-455(1995).
|
|
|
|
- FUNCTION: 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. Also regulates another target, the gli oncogene. Intercellular signal essential for a variety of patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Displays both floor plate- and motor neuron-inducing activity. The threshold concentration of N-product required for motor neuron induction is 5-fold lower than that required for floor plate induction.
- SUBUNIT: N-product is active as a multimer (By similarity).
- SUBCELLULAR LOCATION: Sonic hedgehog protein C-product: Secreted, extracellular space (By similarity). Note=The C-terminal peptide diffuses from the cell (By similarity).
- SUBCELLULAR LOCATION: Sonic hedgehog protein N-product: Cell membrane; Lipid-anchor (By similarity). Note=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 (By similarity).
- TISSUE SPECIFICITY: Expressed in the posterior limb bud mesenchyme, the Hensen node, the notochord, and the floor plate of the neural tube.
- DEVELOPMENTAL STAGE: First detectable at stage 17 during the initiation of limb bud formation. From that point onwards, the expression pattern exactly matches the location of the zone of polarizing activity (ZPA).
- INDUCTION: By retinoic acid.
- 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 (By similarity).
- PTM: N-palmitoylation of Cys-27 by HHAT is required for N-product multimerization and full activity (By similarity).
- SIMILARITY: Belongs to the hedgehog family.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 425 AA [This is the length of the unprocessed precursor] |
Molecular weight: 46474 Da [This is the MW of the unprocessed precursor] |
CRC64: DA9627443D4A0173 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MVEMLLLTRI LLVGFICALL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG
70 80 90 100 110 120
ASGRYEGKIT RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW
130 140 150 160 170 180
PGVKLRVTEG WDEDGHHSEE SLHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES
190 200 210 220 230 240
KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EHGGTKLVKD LSPGDRVLAA DADGRLLYSD
250 260 270 280 290 300
FLTFLDRMDS SRKLFYVIET RQPRARLLLT AAHLLFVAPQ HNQSEATGST SGQALFASNV
310 320 330 340 350 360
KPGQRVYVLG EGGQQLLPAS VHSVSLREEA SGAYAPLTAQ GTILINRVLA SCYAVIEEHS
370 380 390 400 410 420
WAHWAFAPFR LAQGLLAALC PDGAIPTAAT TTTGIHWYSR LLYRIGSWVL DGDALHPLGM
VAPAS
|
Q91035 in FASTA format |
|