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Sonic hedgehog protein (SHH) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) [Cleaved into: Sonic hedgehog protein N-product (ShhN) (Shh N-terminal processed signaling domains) (ShhNp)]

 SHH_CHICK               Reviewed;         425 AA.
Q91035;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 131.
RecName: Full=Sonic hedgehog protein;
Short=SHH;
AltName: Full=Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains {ECO:0000250|UniProtKB:Q62226};
Short=ShhNC {ECO:0000250|UniProtKB:Q62226};
Contains:
RecName: Full=Sonic hedgehog protein N-product;
Short=ShhN;
AltName: Full=Shh N-terminal processed signaling domains {ECO:0000250|UniProtKB:Q62226};
Short=ShhNp {ECO:0000250|UniProtKB:Q62226};
Flags: Precursor;
Name=SHH;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Limb bud;
PubMed=8269518; DOI=10.1016/0092-8674(93)90626-2;
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, PROTEOLYTIC PROCESSING, AND AUTOCATALYTIC CLEAVAGE.
PubMed=7736596; DOI=10.1016/0092-8674(95)90397-6;
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).
[3]
GLYCOSYLATION.
PubMed=7891723; DOI=10.1128/MCB.15.4.2294;
Bumcrot D.A., Takada R., McMahon A.P.;
"Proteolytic processing yields two secreted forms of sonic hedgehog.";
Mol. Cell. Biol. 15:2294-2303(1995).
-!- FUNCTION: Sonic hedgehog protein: The C-terminal part of the sonic
hedgehog protein precursor displays an autoproteolysis and a
cholesterol transferase activity (By similarity). Both activities
result in the cleavage of the full-length protein into two parts
(ShhN and ShhC) followed by the covalent attachment of a
cholesterol moiety to the C-terminal of the newly generated ShhN
(By similarity). Both activities occur in the reticulum
endoplasmic (By similarity). Once cleaved, ShhC is degraded in the
endoplasmic reticulum (By similarity).
{ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226,
ECO:0000269|PubMed:7736596}.
-!- FUNCTION: Sonic hedgehog protein N-product: The dually lipidated
sonic hedgehog protein N-product (ShhNp) is a morphogen which is
essential for a variety of patterning events during development.
Induces ventral cell fate in the neural tube and somites
(PubMed:7736596). Involved in the patterning of the anterior-
posterior axis of the developing limb bud (By similarity).
Essential for axon guidance (By similarity). Binds to the patched
(PTCH1) receptor, which functions in association with smoothened
(SMO), to activate the transcription of target genes (By
similarity). In the absence of SHH, PTCH1 represses the
constitutive signaling activity of SMO (By similarity).
{ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226,
ECO:0000269|PubMed:7736596}.
-!- SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates
HHAT-mediated palmitoylation of the SHH N-terminus (By
similarity). ShhNp is active as a multimer (By similarity).
Interacts with BOC and CDON (By similarity). Interacts with HHIP
(By similarity). Interacts with DISP1 via its cholesterol anchor
(By similarity). Interacts with SCUBE2 (By similarity).
{ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.
-!- SUBCELLULAR LOCATION: Sonic hedgehog protein N-product: Cell
membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor
{ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic
hedgehog protein N-product (ShhNp) is firmly tethered to the cell
membrane where it forms multimers (By similarity). Further
solubilization and release from the cell surface seem to be
achieved through different mechanisms, including the interaction
with DISP1 and SCUBE2, movement by lipoprotein particles,
transport by cellular extensions called cytonemes or by the
proteolytic removal of both terminal lipidated peptides.
{ECO:0000250|UniProtKB:Q62226}.
-!- 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.
-!- DOMAIN: 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|UniProtKB:Q62226}.
-!- DOMAIN: Sonic hedgehog protein N-product: The Cardin-Weintraub
(CW) motif is required for heparan sulfate binding of the
solubilized ShhNp (By similarity). The N-terminal palmitoylated
peptide is cleaved at the Heparan sulfate-binding Cardin-Weintraub
(CW) motif site (By similarity). The cleavage reduced the
interactions with heparan sulfate. The cleavage is enhanced by
SCUBE2 (By similarity). {ECO:0000250|UniProtKB:Q62226}.
-!- PTM: Sonic hedgehog protein: The C-terminal domain displays an
autoproteolysis activity and a cholesterol transferase activity
(By similarity). 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 (ShhN) (By similarity). Cholesterylation is required for
the sonic hedgehog protein N-product targeting to lipid rafts and
multimerization (By similarity). ShhN is the active species in
both local and long-range signaling, whereas the C-product (ShhC)
is degraded in the reticulum endoplasmic (By similarity).
{ECO:0000250|UniProtKB:Q62226, ECO:0000269|PubMed:7736596}.
-!- PTM: Sonic hedgehog protein N-product: N-palmitoylation by HHAT of
ShhN is required for sonic hedgehog protein N-product
multimerization and full activity (By similarity). It is a
prerequisite for the membrane-proximal positioning and the
subsequent shedding of this N-terminal peptide (By similarity).
{ECO:0000250|UniProtKB:Q62226}.
-!- PTM: Sonic hedgehog protein N-product: The lipidated N- and C-
terminal peptides of ShhNp can be cleaved (shedding) (By
similarity). The N-terminal palmitoylated peptide is cleaved at
the Cardin-Weintraub (CW) motif site (By similarity). The cleavage
reduced the interactions with heparan sulfate (By similarity). The
cleavage is enhanced by SCUBE2 (By similarity).
{ECO:0000250|UniProtKB:Q62226}.
-!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
-!- CAUTION: The several steps and mechanisms that permit controlled
Shh dispersion and gradient formation remain controversial. The
ShhNC C-terminal domain displays an autoproteolysis activity and a
cholesterol transferase activity resulting in the cleavage and
covalent attachment of a cholesterol moiety to the C-terminal of
the newly generated N-terminal fragment (ShhN). The protein is
further modified by covalent addition of palmitate at the N-
terminal of ShhN, resulting to the dual-lipidated Shh (ShhNp).
ShhNp is firmly tethered to the cell membrane where it forms
multimers. Further solubilization and release from the cell
surface seem to be achieved through different mechanisms,
including the interaction with DISP1 and SCUBE2, movement by
lipoprotein particles, transport by cellular extensions called
cytonemes or by proteolytic removal of both terminal lipidated
peptides. Once released, the fully processed Shh can signal within
embryonic tissues both at short and long-range.
{ECO:0000250|UniProtKB:Q62226}.
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EMBL; L28099; AAA72428.1; -; mRNA.
PIR; A49424; A49424.
RefSeq; NP_990152.1; NM_204821.1.
UniGene; Gga.345; -.
ProteinModelPortal; Q91035; -.
SMR; Q91035; -.
STRING; 9031.ENSGALP00000010292; -.
MEROPS; C46.002; -.
PaxDb; Q91035; -.
PRIDE; Q91035; -.
GeneID; 395615; -.
KEGG; gga:395615; -.
CTD; 6469; -.
eggNOG; KOG3638; Eukaryota.
eggNOG; ENOG410XQA3; LUCA.
HOGENOM; HOG000233428; -.
HOVERGEN; HBG005480; -.
InParanoid; Q91035; -.
KO; K11988; -.
PhylomeDB; Q91035; -.
PRO; PR:Q91035; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005576; C:extracellular region; NAS:Roslin.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0016015; F:morphogen activity; NAS:Roslin.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IDA:Roslin.
GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0001709; P:cell fate determination; NAS:AgBase.
GO; GO:0060573; P:cell fate specification involved in pattern specification; TAS:AgBase.
GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
GO; GO:0060591; P:chondroblast differentiation; IMP:AgBase.
GO; GO:0071679; P:commissural neuron axon guidance; IMP:AgBase.
GO; GO:0042733; P:embryonic digit morphogenesis; ISS:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; IDA:Roslin.
GO; GO:0009880; P:embryonic pattern specification; IMP:AgBase.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:AgBase.
GO; GO:0090269; P:fibroblast growth factor production; IDA:AgBase.
GO; GO:0021508; P:floor plate formation; IMP:AgBase.
GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IMP:AgBase.
GO; GO:0048877; P:homeostasis of number of retina cells; IMP:AgBase.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:AgBase.
GO; GO:0003408; P:optic cup formation involved in camera-type eye development; IMP:AgBase.
GO; GO:0021631; P:optic nerve morphogenesis; IMP:AgBase.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; ISS:UniProtKB.
GO; GO:0009951; P:polarity specification of dorsal/ventral axis; NAS:AgBase.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IDA:AgBase.
GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; IMP:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
GO; GO:0061075; P:positive regulation of neural retina development; IMP:AgBase.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:AgBase.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:AgBase.
GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IMP:AgBase.
GO; GO:0060786; P:regulation of cell differentiation involved in tissue homeostasis; TAS:AgBase.
GO; GO:0010468; P:regulation of gene expression; IMP:AgBase.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:AgBase.
GO; GO:0032526; P:response to retinoic acid; IDA:Roslin.
GO; GO:0001895; P:retina homeostasis; IMP:AgBase.
GO; GO:0003406; P:retinal pigment epithelium development; IMP:AgBase.
GO; GO:0097264; P:self proteolysis; IDA:AgBase.
GO; GO:0023052; P:signaling; IMP:AgBase.
GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:AgBase.
GO; GO:0009888; P:tissue development; IMP:AgBase.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR001657; Hedgehog.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR000320; Hedgehog_signalling_dom.
InterPro; IPR001767; Hint_dom.
InterPro; IPR003586; Hint_dom_C.
InterPro; IPR003587; Hint_dom_N.
InterPro; IPR036844; Hint_dom_sf.
InterPro; IPR006141; Intein_N.
Pfam; PF01085; HH_signal; 1.
Pfam; PF01079; Hint; 1.
PIRSF; PIRSF009400; Peptidase_C46; 1.
PRINTS; PR00632; SONICHHOG.
SMART; SM00305; HintC; 1.
SMART; SM00306; HintN; 1.
SUPFAM; SSF51294; SSF51294; 1.
SUPFAM; SSF55166; SSF55166; 1.
PROSITE; PS50817; INTEIN_N_TER; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Calcium; Cell membrane; Complete proteome;
Developmental protein; Glycoprotein; Hydrolase; Lipoprotein; Membrane;
Metal-binding; Palmitate; Protease; Reference proteome; Signal; Zinc.
SIGNAL 1 26 {ECO:0000250|UniProtKB:Q15465}.
CHAIN 27 425 Sonic hedgehog protein.
/FTId=PRO_0000013217.
CHAIN 27 200 Sonic hedgehog protein N-product.
/FTId=PRO_0000013218.
MOTIF 35 41 Cardin-Weintraub.
{ECO:0000250|UniProtKB:Q62226}.
COMPBIAS 390 393 Poly-Thr.
METAL 92 92 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 93 93 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 93 93 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 98 98 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 128 128 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q15465}.
METAL 129 129 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 129 129 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 132 132 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 134 134 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 143 143 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 150 150 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 185 185 Zinc. {ECO:0000250|UniProtKB:Q15465}.
SITE 200 201 Cleavage; by autolysis. {ECO:0000305}.
SITE 246 246 Involved in cholesterol transfer.
{ECO:0000250}.
SITE 270 270 Involved in auto-cleavage. {ECO:0000250}.
SITE 273 273 Essential for auto-cleavage.
{ECO:0000250}.
LIPID 27 27 N-palmitoyl cysteine. {ECO:0000250}.
LIPID 200 200 Cholesterol glycine ester. {ECO:0000250}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 425 AA; 46474 MW; DA9627443D4A0173 CRC64;
MVEMLLLTRI LLVGFICALL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG
ASGRYEGKIT RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW
PGVKLRVTEG WDEDGHHSEE SLHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES
KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EHGGTKLVKD LSPGDRVLAA DADGRLLYSD
FLTFLDRMDS SRKLFYVIET RQPRARLLLT AAHLLFVAPQ HNQSEATGST SGQALFASNV
KPGQRVYVLG EGGQQLLPAS VHSVSLREEA SGAYAPLTAQ GTILINRVLA SCYAVIEEHS
WAHWAFAPFR LAQGLLAALC PDGAIPTAAT TTTGIHWYSR LLYRIGSWVL DGDALHPLGM
VAPAS


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