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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_RAT                 Reviewed;         437 AA.
Q63673;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 154.
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 {ECO:0000312|RGD:3673}; Synonyms=Vhh-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Embryonic floor plate;
PubMed=8124714; DOI=10.1016/0092-8674(94)90514-2;
Roelink H., Augsburger A., Heemskerk J., Korzh V., Norlin S.,
Ruiz i Altaba A., Tanabe Y., Placzek M., Edlund T., Jessell T.M.,
Dodd J.;
"Floor plate and motor neuron induction by vhh-1, a vertebrate homolog
of hedgehog expressed by the notochord.";
Cell 76:761-775(1994).
[2]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11395778; DOI=10.1038/35079648;
Zeng X., Goetz J.A., Suber L.M., Scott W.J. Jr., Schreiner C.M.,
Robbins D.J.;
"A freely diffusible form of Sonic hedgehog mediates long-range
signalling.";
Nature 411:716-720(2001).
-!- 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}.
-!- 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 (By
similarity). 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}.
-!- 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,
ECO:0000269|PubMed:11395778}.
-!- 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 node, notochord, floor plate,
and posterior limb bud mesenchyme. {ECO:0000269|PubMed:8124714}.
-!- 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}.
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; L27340; AAA20999.1; -; mRNA.
PIR; B53193; B53193.
RefSeq; NP_058917.1; NM_017221.1.
UniGene; Rn.10432; -.
ProteinModelPortal; Q63673; -.
SMR; Q63673; -.
STRING; 10116.ENSRNOP00000008497; -.
MEROPS; C46.002; -.
PaxDb; Q63673; -.
PRIDE; Q63673; -.
GeneID; 29499; -.
KEGG; rno:29499; -.
CTD; 6469; -.
RGD; 3673; Shh.
eggNOG; KOG3638; Eukaryota.
eggNOG; ENOG410XQA3; LUCA.
HOGENOM; HOG000233428; -.
HOVERGEN; HBG005480; -.
InParanoid; Q63673; -.
KO; K11988; -.
PhylomeDB; Q63673; -.
PRO; PR:Q63673; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0030133; C:transport vesicle; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0043237; F:laminin-1 binding; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0008209; P:androgen metabolic process; ISS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; ISS:UniProtKB.
GO; GO:0048468; P:cell development; ISS:UniProtKB.
GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISS:UniProtKB.
GO; GO:0071679; P:commissural neuron axon guidance; IMP:RGD.
GO; GO:0007502; P:digestive tract mesoderm development; IDA:RGD.
GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; ISS:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEP:RGD.
GO; GO:0030900; P:forebrain development; ISS:UniProtKB.
GO; GO:0061196; P:fungiform papilla development; IMP:RGD.
GO; GO:0061198; P:fungiform papilla formation; IMP:RGD.
GO; GO:0061197; P:fungiform papilla morphogenesis; IMP:RGD.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0030902; P:hindbrain development; ISS:UniProtKB.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0030539; P:male genitalia development; ISS:UniProtKB.
GO; GO:0048808; P:male genitalia morphogenesis; IMP:RGD.
GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
GO; GO:0030901; P:midbrain development; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:2000357; P:negative regulation of kidney smooth muscle cell differentiation; ISS:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:2000062; P:negative regulation of ureter smooth muscle cell differentiation; ISS:UniProtKB.
GO; GO:0045060; P:negative thymic T cell selection; ISS:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
GO; GO:0001841; P:neural tube formation; IMP:RGD.
GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; ISS:UniProtKB.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:RGD.
GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; ISS:UniProtKB.
GO; GO:2000358; P:positive regulation of kidney smooth muscle cell differentiation; ISS:UniProtKB.
GO; GO:2000729; P:positive regulation of mesenchymal cell proliferation involved in ureter development; ISS:UniProtKB.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:0032901; P:positive regulation of neurotrophin production; IMP:RGD.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IDA:RGD.
GO; GO:0060406; P:positive regulation of penile erection; IMP:RGD.
GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IDA:RGD.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:RGD.
GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:2000063; P:positive regulation of ureter smooth muscle cell differentiation; ISS:UniProtKB.
GO; GO:0045059; P:positive thymic T cell selection; ISS:UniProtKB.
GO; GO:0030850; P:prostate gland development; IEP:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IDA:RGD.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IEP:RGD.
GO; GO:0030162; P:regulation of proteolysis; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; IMP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IDA:MGI.
GO; GO:0048864; P:stem cell development; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0021978; P:telencephalon regionalization; IMP:RGD.
GO; GO:0048538; P:thymus development; ISS:UniProtKB.
GO; GO:0043586; P:tongue development; IMP:RGD.
GO; GO:0043587; P:tongue morphogenesis; IMP:RGD.
GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
GO; GO:0021521; P:ventral spinal cord interneuron specification; IDA:MGI.
GO; GO:0022006; P:zona limitans intrathalamica formation; IDA:RGD.
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 24 {ECO:0000250|UniProtKB:Q15465}.
CHAIN 25 437 Sonic hedgehog protein.
/FTId=PRO_0000013214.
CHAIN 25 198 Sonic hedgehog protein N-product.
/FTId=PRO_0000013215.
MOTIF 33 39 Cardin-Weintraub.
{ECO:0000250|UniProtKB:Q62226}.
COMPBIAS 383 387 Poly-Gly.
METAL 90 90 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 91 91 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 91 91 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 96 96 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 126 126 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q15465}.
METAL 127 127 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 127 127 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 130 130 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 132 132 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 141 141 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 148 148 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 183 183 Zinc. {ECO:0000250|UniProtKB:Q15465}.
SITE 198 199 Cleavage; by autolysis.
SITE 244 244 Involved in cholesterol transfer.
{ECO:0000250}.
SITE 268 268 Involved in auto-cleavage. {ECO:0000250}.
SITE 271 271 Essential for auto-cleavage.
{ECO:0000250}.
LIPID 25 25 N-palmitoyl cysteine. {ECO:0000250}.
LIPID 198 198 Cholesterol glycine ester. {ECO:0000250}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 437 AA; 47630 MW; 0DBFC19F0D1662A0 CRC64;
MLLLLARCFL VALASSLLVC PGLACGPGRG FGKRQHPKKL TPLAYKQFIP NVAEKTLGAS
GRYEGKITRN SERFKELTPN YNPDIIFKDE ENTGADRLMT QRCKDKLNAL AISVMNQWPG
VKLRVTEGWD EDGHHSEESL HYEGRAVDIT TSDRDRSKYG MLARLAVEAG FDWVYYESKA
RIHCSVKAEN SVAAKSDGCF PGSATVHLEQ GGTKLVKDLS PGDRVLAADD QGRLLYSDFL
TFLDRDEGAK KVFYVIETRE PRERLLLTAA HLLFVAPHND SGPTPGPSPL FASRVRPGQR
VYVVAERGGD RRLLPAAVHS VTLREEAAGA YAPLTADGTI LINRVLASCY AVIEEHSWAH
RAFAPFRLAH ALLAALAPAR TDGGGGGSIP APQSVAEARG AGPPAGIHWY SQLLYHIGTW
LLDSETLHPL GMAVKSS


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