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Sonic hedgehog protein (SHH) (HHG-1) (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) (Sonic hedgehog protein 19 kDa product)]

 SHH_MOUSE               Reviewed;         437 AA.
Q62226;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 2.
22-APR-2020, entry version 202.
RecName: Full=Sonic hedgehog protein;
Short=SHH;
AltName: Full=HHG-1;
AltName: Full=Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains {ECO:0000303|PubMed:24522195};
Short=ShhNC {ECO:0000303|PubMed:24522195};
Contains:
RecName: Full=Sonic hedgehog protein N-product;
Short=ShhN;
AltName: Full=Shh N-terminal processed signaling domains {ECO:0000303|PubMed:24522195};
Short=ShhNp {ECO:0000303|PubMed:24522195};
AltName: Full=Sonic hedgehog protein 19 kDa product;
Flags: Precursor;
Name=Shh {ECO:0000312|MGI:MGI:98297}; Synonyms=Hhg1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=7916661; DOI=10.1016/0092-8674(93)90627-3;
Echelard Y., Epstein D.J., St Jacques B., Shen L., Mohler J., McMahon J.A.,
McMahon A.P.;
"Sonic hedgehog, a member of a family of putative signaling molecules, is
implicated in the regulation of CNS polarity.";
Cell 75:1417-1430(1993).
[2]
SEQUENCE REVISION TO 122.
McMahon A.P.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC PROCESSING, AND AUTOCATALYTIC
CLEAVAGE.
PubMed=7720571;
Chang D.T., Lopez A., von Kessler D.P., Chiang C., Simandl B.K., Zhao R.,
Seldin M.F., Fallon J.F., Beachy P.A.;
"Products, genetic linkage and limb patterning activity of a murine
hedgehog gene.";
Development 120:3339-3353(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEOLYTIC PROCESSING, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
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).
[7]
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).
[8]
CHOLESTERYLATION AT GLY-198, AND FUNCTION.
PubMed=8824192; DOI=10.1126/science.274.5285.255;
Porter J.A., Young K.E., Beachy P.A.;
"Cholesterol modification of hedgehog signaling proteins in animal
development.";
Science 274:255-259(1996).
[9]
PALMITOYLATION AT CYS-25, AND MUTAGENESIS OF CYS-25.
PubMed=11486055; DOI=10.1126/science.1064437;
Chamoun Z., Mann R.K., Nellen D., von Kessler D.P., Bellotto M.,
Beachy P.A., Basler K.;
"Skinny hedgehog, an acyltransferase required for palmitoylation and
activity of the hedgehog signal.";
Science 293:2080-2084(2001).
[10]
FUNCTION.
PubMed=11430830; DOI=10.1016/s1097-2765(01)00271-4;
Briscoe J., Chen Y., Jessell T.M., Struhl G.;
"A hedgehog-insensitive form of patched provides evidence for direct long-
range morphogen activity of sonic hedgehog in the neural tube.";
Mol. Cell 7:1279-1291(2001).
[11]
FUNCTION IN CEREBELLAR DEVELOPMENT.
PubMed=14687547; DOI=10.1016/s0896-6273(03)00769-4;
Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D.,
Rosenfeld M.G., Hamilton B.A.;
"RORalpha coordinates reciprocal signaling in cerebellar development
through sonic hedgehog and calcium-dependent pathways.";
Neuron 40:1119-1131(2003).
[12]
FUNCTION IN AXON GUIDANCE.
PubMed=12679031; DOI=10.1016/s0092-8674(03)00199-5;
Charron F., Stein E., Jeong J., McMahon A.P., Tessier-Lavigne M.;
"The morphogen sonic hedgehog is an axonal chemoattractant that
collaborates with netrin-1 in midline axon guidance.";
Cell 113:11-23(2003).
[13]
FUNCTION IN LIMB DEVELOPMENT.
PubMed=15315762; DOI=10.1016/j.cell.2004.07.023;
Ahn S., Joyner A.L.;
"Dynamic changes in the response of cells to positive hedgehog signaling
during mouse limb patterning.";
Cell 118:505-516(2004).
[14]
PALMITOYLATION AT CYS-25, MUTAGENESIS OF CYS-25, SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=15075292; DOI=10.1101/gad.1185804;
Chen M.-H., Li Y.-J., Kawakami T., Xu S.-M., Chuang P.-T.;
"Palmitoylation is required for the production of a soluble multimeric
Hedgehog protein complex and long-range signaling in vertebrates.";
Genes Dev. 18:641-659(2004).
[15]
MUTAGENESIS OF GLY-32; ASP-89; GLN-101; ASN-116; TRP-118 AND GLU-189.
PubMed=16282375; DOI=10.1073/pnas.0507848102;
Maity T., Fuse N., Beachy P.A.;
"Molecular mechanisms of Sonic hedgehog mutant effects in
holoprosencephaly.";
Proc. Natl. Acad. Sci. U.S.A. 102:17026-17031(2005).
[16]
INTERACTION WITH HHATL.
PubMed=18081866; DOI=10.1111/j.1742-4658.2007.06202.x;
Abe Y., Kita Y., Niikura T.;
"Mammalian Gup1, a homolog of Saccharomyces cerevisiae glycerol
uptake/transporter 1, acts as a negative regulator for N-terminal
palmitoylation of Sonic hedgehog.";
FEBS J. 275:318-331(2008).
[17]
INTERACTION WITH GPC3.
PubMed=18477453; DOI=10.1016/j.devcel.2008.03.006;
Capurro M.I., Xu P., Shi W., Li F., Jia A., Filmus J.;
"Glypican-3 inhibits Hedgehog signaling during development by competing
with patched for Hedgehog binding.";
Dev. Cell 14:700-711(2008).
[18]
REVIEW, AND FUNCTION.
PubMed=21357747; DOI=10.1083/jcb.201008090;
Chen X., Tukachinsky H., Huang C.H., Jao C., Chu Y.R., Tang H.Y.,
Mueller B., Schulman S., Rapoport T.A., Salic A.;
"Processing and turnover of the Hedgehog protein in the endoplasmic
reticulum.";
J. Cell Biol. 192:825-838(2011).
[19]
INTERACTION WITH DISP1 AND SCUBE2, SUBUNIT, AND CAUTION.
PubMed=22902404; DOI=10.1016/j.celrep.2012.07.010;
Tukachinsky H., Kuzmickas R.P., Jao C.Y., Liu J., Salic A.;
"Dispatched and scube mediate the efficient secretion of the cholesterol-
modified hedgehog ligand.";
Cell Rep. 2:308-320(2012).
[20]
INTERACTION WITH SCUBE2, SUBUNIT, AND CAUTION.
PubMed=22677548; DOI=10.1101/gad.191866.112;
Creanga A., Glenn T.D., Mann R.K., Saunders A.M., Talbot W.S., Beachy P.A.;
"Scube/You activity mediates release of dually lipid-modified Hedgehog
signal in soluble form.";
Genes Dev. 26:1312-1325(2012).
[21]
PTM, AND DOMAIN.
PubMed=23118222; DOI=10.1074/jbc.m112.356667;
Ohlig S., Pickhinke U., Sirko S., Bandari S., Hoffmann D., Dreier R.,
Farshi P., Goetz M., Grobe K.;
"An emerging role of Sonic hedgehog shedding as a modulator of heparan
sulfate interactions.";
J. Biol. Chem. 287:43708-43719(2012).
[22]
PTM, INTERACTION WITH SCUBE2, AND SUBUNIT.
PubMed=24522195; DOI=10.1242/jcs.137695;
Jakobs P., Exner S., Schuermann S., Pickhinke U., Bandari S., Ortmann C.,
Kupich S., Schulz P., Hansen U., Seidler D.G., Grobe K.;
"Scube2 enhances proteolytic Shh processing from the surface of Shh-
producing cells.";
J. Cell Sci. 127:1726-1737(2014).
[23]
REVIEW, AND FUNCTION.
PubMed=24863049; DOI=10.1002/dneu.22193;
Pal K., Mukhopadhyay S.;
"Primary cilium and sonic hedgehog signaling during neural tube patterning:
role of GPCRs and second messengers.";
Dev. Neurobiol. 75:337-348(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 34-195 IN COMPLEX WITH ZINC IONS.
PubMed=7477329; DOI=10.1038/378212a0;
Hall T.M.T., Porter J.A., Beachy P.A., Leahy D.J.;
"A potential catalytic site revealed by the 1.7-A crystal structure of the
amino-terminal signalling domain of Sonic hedgehog.";
Nature 378:212-216(1995).
[25]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 26-189 IN COMPLEX WITH CDON;
CALCIUM AND ZINC IONS, DOMAIN, AND INTERACTION WITH CDON.
PubMed=18794898; DOI=10.1038/nature07358;
McLellan J.S., Zheng X., Hauk G., Ghirlando R., Beachy P.A., Leahy D.J.;
"The mode of Hedgehog binding to Ihog homologues is not conserved across
different phyla.";
Nature 455:979-983(2008).
[26]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 40-191 IN COMPLEX WITH HHIP;
CALCIUM AND ZINC IONS, DOMAIN, AND INTERACTION WITH HHIP.
PubMed=19561611; DOI=10.1038/nsmb.1607;
Bishop B., Aricescu A.R., Harlos K., O'Callaghan C.A., Jones E.Y.,
Siebold C.;
"Structural insights into hedgehog ligand sequestration by the human
hedgehog-interacting protein HHIP.";
Nat. Struct. Mol. Biol. 16:698-703(2009).
[27]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 26-189 IN COMPLEX WITH CALCIUM AND
ZINC IONS, DOMAIN, AND INTERACTION WITH BOC AND CDON.
PubMed=20519495; DOI=10.1074/jbc.m110.131680;
Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
"All mammalian Hedgehog proteins interact with cell adhesion molecule,
down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved
manner.";
J. Biol. Chem. 285:24584-24590(2010).
-!- FUNCTION: [Sonic hedgehog protein]: The C-terminal part of the sonic
hedgehog protein precursor displays an autoproteolysis and a
cholesterol transferase activity (PubMed:8824192, PubMed:7891723). 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
(PubMed:8824192). Both activities occur in the reticulum endoplasmic
(PubMed:21357747). Once cleaved, ShhC is degraded in the endoplasmic
reticulum (PubMed:21357747). {ECO:0000269|PubMed:7736596,
ECO:0000269|PubMed:7891723, ECO:0000269|PubMed:8824192,
ECO:0000305|PubMed:21357747}.
-!- 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:11430830, PubMed:24863049). Involved in the patterning of the
anterior-posterior axis of the developing limb bud (PubMed:15315762).
Essential for axon guidance (PubMed:12679031). 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:0000269|PubMed:14687547, ECO:0000269|PubMed:7736596,
ECO:0000303|PubMed:24522195}.
-!- SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates HHAT-
mediated palmitoylation of the SHH N-terminus (PubMed:18081866). ShhNp
is active as a multimer (PubMed:24522195). Interacts with BOC and CDON
(PubMed:18794898). Interacts with HHIP (By similarity). Interacts with
DISP1 via its cholesterol anchor (PubMed:22902404, PubMed:22677548).
Interacts with SCUBE2 (PubMed:24522195, PubMed:22677548). Interacts
with glypican GPC3 (PubMed:18477453). {ECO:0000250|UniProtKB:Q15465,
ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:18081866,
ECO:0000269|PubMed:18477453, ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:22677548, ECO:0000269|PubMed:24522195,
ECO:0000269|PubMed:7477329}.
-!- INTERACTION:
Q62226; Q4KMG0: CDON; Xeno; NbExp=7; IntAct=EBI-15610166, EBI-7016840;
Q62226; Q96QV1-1: HHIP; Xeno; NbExp=4; IntAct=EBI-15610166, EBI-15791478;
-!- SUBCELLULAR LOCATION: [Sonic hedgehog protein N-product]: Cell membrane
{ECO:0000269|PubMed:7891723}; Lipid-anchor
{ECO:0000269|PubMed:7891723}. Note=The dual-lipidated sonic hedgehog
protein N-product (ShhNp) is firmly tethered to the cell membrane where
it forms multimers (PubMed:24522195). 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:0000269|PubMed:24522195, ECO:0000305|PubMed:22677548}.
-!- TISSUE SPECIFICITY: Expressed in a number of embryonic tissues
including the notochord, ventral neural tube, floor plate, lung bud,
zone of polarizing activity and posterior distal mesenchyme of limbs.
In the adult, expressed in lung and neural retina.
-!- DEVELOPMENTAL STAGE: First detectable during gastrulation.
-!- 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:0000269|PubMed:18794898, ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
-!- DOMAIN: [Sonic hedgehog protein N-product]: The Cardin-Weintraub (CW)
motif is required for heparan sulfate binding of the solubilized ShhNp
(PubMed:23118222). The N-terminal palmitoylated peptide is cleaved at
the heparan sulfate-binding Cardin-Weintraub (CW) motif site
(PubMed:24522195). The cleavage reduced the interactions with heparan
sulfate. The cleavage is enhanced by SCUBE2 (PubMed:24522195).
{ECO:0000269|PubMed:23118222, ECO:0000269|PubMed:24522195}.
-!- PTM: [Sonic hedgehog protein]: The C-terminal domain displays an
autoproteolysis activity and a cholesterol transferase activity
(PubMed:7891723, PubMed:7736596, PubMed:8824192). 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)(PubMed:7891723, PubMed:7736596,
PubMed:8824192). Cholesterylation is required for the sonic hedgehog
protein N-product targeting to lipid rafts and multimerization
(PubMed:24522195, PubMed:8824192). ShhN is the active species in both
local and long-range signaling, whereas the C-product (ShhC) is
degraded in the reticulum endoplasmic (PubMed:21357747).
{ECO:0000269|PubMed:7720571, ECO:0000269|PubMed:7736596,
ECO:0000269|PubMed:7891723, ECO:0000269|PubMed:8824192,
ECO:0000305|PubMed:21357747, ECO:0000305|PubMed:24522195}.
-!- PTM: [Sonic hedgehog protein N-product]: N-palmitoylation by HHAT of
ShhN is required for sonic hedgehog protein N-product multimerization
and full activity (PubMed:11486055, PubMed:15075292). It is a
prerequisite for the membrane-proximal positioning and the subsequent
shedding of this N-terminal peptide (PubMed:24522195).
{ECO:0000269|PubMed:11486055, ECO:0000269|PubMed:15075292,
ECO:0000269|PubMed:24522195}.
-!- PTM: [Sonic hedgehog protein N-product]: The lipidated N- and C-
terminal peptides of ShhNp can be cleaved (shedding)(PubMed:24522195).
The N-terminal palmitoylated peptide is cleaved at the Cardin-Weintraub
(CW) motif site (PubMed:24522195). The cleavage reduced the
interactions with heparan sulfate (PubMed:23118222). The cleavage is
enhanced by SCUBE2. {ECO:0000269|PubMed:23118222,
ECO:0000269|PubMed:24522195}.
-!- MISCELLANEOUS: Mice overexpressing Shh display digit duplications in
both forelimbs and hindlimbs. {ECO:0000269|PubMed:15315762}.
-!- 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:0000269|PubMed:24522195, ECO:0000305|PubMed:22677548,
ECO:0000305|PubMed:22902404}.
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EMBL; X76290; CAA53922.1; -; mRNA.
EMBL; AK077688; BAC36956.1; -; mRNA.
EMBL; BC063087; AAH63087.1; -; mRNA.
CCDS; CCDS19146.1; -.
PIR; A49425; A49425.
RefSeq; NP_033196.1; NM_009170.3.
PDB; 1VHH; X-ray; 1.70 A; A=34-195.
PDB; 2WFX; X-ray; 3.20 A; A=40-191.
PDB; 2WG4; X-ray; 3.15 A; A=40-191.
PDB; 3D1M; X-ray; 1.70 A; A/B=26-189.
PDB; 3N1R; X-ray; 2.13 A; A=40-195.
PDB; 4C4M; X-ray; 1.74 A; A=40-195.
PDB; 4C4N; X-ray; 2.36 A; A/B=40-195.
PDBsum; 1VHH; -.
PDBsum; 2WFX; -.
PDBsum; 2WG4; -.
PDBsum; 3D1M; -.
PDBsum; 3N1R; -.
PDBsum; 4C4M; -.
PDBsum; 4C4N; -.
SMR; Q62226; -.
BioGrid; 203220; 10.
DIP; DIP-48537N; -.
IntAct; Q62226; 7.
STRING; 10090.ENSMUSP00000002708; -.
BindingDB; Q62226; -.
ChEMBL; CHEMBL5387; -.
DrugCentral; Q62226; -.
MEROPS; C46.002; -.
iPTMnet; Q62226; -.
PhosphoSitePlus; Q62226; -.
SwissPalm; Q62226; -.
MaxQB; Q62226; -.
PaxDb; Q62226; -.
PRIDE; Q62226; -.
Antibodypedia; 4514; 572 antibodies.
Ensembl; ENSMUST00000002708; ENSMUSP00000002708; ENSMUSG00000002633.
GeneID; 20423; -.
KEGG; mmu:20423; -.
UCSC; uc008wua.2; mouse.
CTD; 6469; -.
MGI; MGI:98297; Shh.
eggNOG; KOG3638; Eukaryota.
eggNOG; ENOG410XQA3; LUCA.
GeneTree; ENSGT00940000159119; -.
HOGENOM; CLU_034686_0_0_1; -.
InParanoid; Q62226; -.
KO; K11988; -.
OMA; YAVIEDH; -.
OrthoDB; 1169356at2759; -.
PhylomeDB; Q62226; -.
TreeFam; TF106458; -.
Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
Reactome; R-MMU-5362798; Release of Hh-Np from the secreting cell.
Reactome; R-MMU-5632681; Ligand-receptor interactions.
Reactome; R-MMU-5635838; Activation of SMO.
EvolutionaryTrace; Q62226; -.
PRO; PR:Q62226; -.
Proteomes; UP000000589; Chromosome 5.
RNAct; Q62226; protein.
Bgee; ENSMUSG00000002633; Expressed in urinary bladder urothelium and 376 other tissues.
Genevisible; Q62226; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
GO; GO:0030133; C:transport vesicle; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
GO; GO:0043237; F:laminin-1 binding; IDA:MGI.
GO; GO:0005113; F:patched binding; IPI:Roslin.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0048856; P:anatomical structure development; IMP:MGI.
GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
GO; GO:0008209; P:androgen metabolic process; IMP:MGI.
GO; GO:0001525; P:angiogenesis; IDA:MGI.
GO; GO:0048645; P:animal organ formation; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:Roslin.
GO; GO:0060840; P:artery development; IMP:MGI.
GO; GO:0007411; P:axon guidance; IDA:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IDA:MGI.
GO; GO:0007596; P:blood coagulation; IMP:MGI.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IDA:MGI.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0060447; P:bud outgrowth involved in lung branching; IMP:MGI.
GO; GO:0043010; P:camera-type eye development; IDA:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IMP:BHF-UCL.
GO; GO:0048468; P:cell development; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IGI:MGI.
GO; GO:0001708; P:cell fate specification; IDA:MGI.
GO; GO:0008283; P:cell population proliferation; IGI:MGI.
GO; GO:0021924; P:cell proliferation in external granule layer; IDA:MGI.
GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IDA:UniProtKB.
GO; GO:0071679; P:commissural neuron axon guidance; ISO:MGI.
GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IMP:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0007502; P:digestive tract mesoderm development; ISO:MGI.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
GO; GO:0071542; P:dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
GO; GO:0007398; P:ectoderm development; IMP:MGI.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:Roslin.
GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI.
GO; GO:0006897; P:endocytosis; IDA:MGI.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IMP:MGI.
GO; GO:0060738; P:epithelial-mesenchymal signaling involved in prostate gland development; IGI:MGI.
GO; GO:0030010; P:establishment of cell polarity; IDA:MGI.
GO; GO:0030900; P:forebrain development; IGI:MGI.
GO; GO:0021871; P:forebrain regionalization; IMP:MGI.
GO; GO:0048859; P:formation of anatomical boundary; IMP:MGI.
GO; GO:0061196; P:fungiform papilla development; ISO:MGI.
GO; GO:0061198; P:fungiform papilla formation; ISO:MGI.
GO; GO:0061197; P:fungiform papilla morphogenesis; ISO:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0030902; P:hindbrain development; IMP:MGI.
GO; GO:0007442; P:hindgut morphogenesis; IMP:MGI.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0060459; P:left lung development; IMP:MGI.
GO; GO:0060174; P:limb bud formation; IMP:MGI.
GO; GO:0060173; P:limb development; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0060428; P:lung epithelium development; IMP:MGI.
GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IMP:BHF-UCL.
GO; GO:0030539; P:male genitalia development; IMP:MGI.
GO; GO:0048808; P:male genitalia morphogenesis; ISO:MGI.
GO; GO:0010463; P:mesenchymal cell proliferation; IMP:MGI.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IDA:MGI.
GO; GO:0060783; P:mesenchymal smoothened signaling pathway involved in prostate gland development; IMP:MGI.
GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; IMP:UniProtKB.
GO; GO:0001656; P:metanephros development; IMP:UniProtKB.
GO; GO:0030901; P:midbrain development; IGI:MGI.
GO; GO:0045445; P:myoblast differentiation; IDA:MGI.
GO; GO:0014902; P:myotube differentiation; IMP:MGI.
GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:Roslin.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IDA:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
GO; GO:0090370; P:negative regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:1904339; P:negative regulation of dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:2000357; P:negative regulation of kidney smooth muscle cell differentiation; IDA:UniProtKB.
GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IMP:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:MGI.
GO; GO:2000062; P:negative regulation of ureter smooth muscle cell differentiation; IDA:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IMP:BHF-UCL.
GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
GO; GO:0001841; P:neural tube formation; ISO:MGI.
GO; GO:0007405; P:neuroblast proliferation; IDA:MGI.
GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
GO; GO:0042476; P:odontogenesis; IDA:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0014003; P:oligodendrocyte development; IDA:MGI.
GO; GO:0048709; P:oligodendrocyte differentiation; IGI:MGI.
GO; GO:0002076; P:osteoblast development; IDA:MGI.
GO; GO:0031016; P:pancreas development; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IMP:MGI.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:Roslin.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
GO; GO:0051781; P:positive regulation of cell division; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IDA:MGI.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:MGI.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IDA:MGI.
GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IMP:BHF-UCL.
GO; GO:2000358; P:positive regulation of kidney smooth muscle cell differentiation; IDA:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:2000729; P:positive regulation of mesenchymal cell proliferation involved in ureter development; IMP:UniProtKB.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
GO; GO:0032901; P:positive regulation of neurotrophin production; ISO:MGI.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IDA:MGI.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISO:MGI.
GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
GO; GO:0061189; P:positive regulation of sclerotome development; ISO:MGI.
GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IMP:MGI.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:MGI.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:BHF-UCL.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IMP:MGI.
GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000063; P:positive regulation of ureter smooth muscle cell differentiation; IMP:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI.
GO; GO:0045059; P:positive thymic T cell selection; IMP:BHF-UCL.
GO; GO:0060516; P:primary prostatic bud elongation; IDA:MGI.
GO; GO:0060523; P:prostate epithelial cord elongation; IDA:MGI.
GO; GO:0030850; P:prostate gland development; IMP:MGI.
GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0060782; P:regulation of mesenchymal cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0042481; P:regulation of odontogenesis; IMP:BHF-UCL.
GO; GO:0060685; P:regulation of prostatic bud formation; IDA:MGI.
GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0030162; P:regulation of proteolysis; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0030323; P:respiratory tube development; IMP:MGI.
GO; GO:0048678; P:response to axon injury; ISO:MGI.
GO; GO:0045471; P:response to ethanol; ISO:MGI.
GO; GO:0060458; P:right lung development; IMP:MGI.
GO; GO:0060021; P:roof of mouth development; IMP:MGI.
GO; GO:0060662; P:salivary gland cavitation; IDA:MGI.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IDA:MGI.
GO; GO:0061053; P:somite development; IMP:BHF-UCL.
GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:MGI.
GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
GO; GO:0048864; P:stem cell development; IMP:BHF-UCL.
GO; GO:0051146; P:striated muscle cell differentiation; IDA:MGI.
GO; GO:0014706; P:striated muscle tissue development; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:BHF-UCL.
GO; GO:0021978; P:telencephalon regionalization; IMP:MGI.
GO; GO:0021794; P:thalamus development; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:BHF-UCL.
GO; GO:0030878; P:thyroid gland development; IMP:MGI.
GO; GO:0043586; P:tongue development; ISO:MGI.
GO; GO:0043587; P:tongue morphogenesis; ISO:MGI.
GO; GO:0060438; P:trachea development; IMP:MGI.
GO; GO:0060439; P:trachea morphogenesis; IMP:MGI.
GO; GO:1905327; P:tracheoesophageal septum formation; IMP:MGI.
GO; GO:0001944; P:vasculature development; IMP:MGI.
GO; GO:0001570; P:vasculogenesis; IDA:MGI.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
GO; GO:0021521; P:ventral spinal cord interneuron specification; ISO:MGI.
GO; GO:0022006; P:zona limitans intrathalamica formation; ISO:MGI.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR001657; Hedgehog.
InterPro; IPR001767; Hedgehog_Hint.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR000320; Hedgehog_signalling_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;
3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
Developmental protein; Glycoprotein; Hydrolase; Lipoprotein; Membrane;
Metal-binding; Palmitate; Protease; Reference proteome; Signal; Zinc.
SIGNAL 1..24
/evidence="ECO:0000250|UniProtKB:Q15465"
CHAIN 25..437
/note="Sonic hedgehog protein"
/id="PRO_0000013211"
CHAIN 25..198
/note="Sonic hedgehog protein N-product"
/id="PRO_0000013212"
MOTIF 33..39
/note="Cardin-Weintraub"
/evidence="ECO:0000269|PubMed:23118222"
COMPBIAS 383..387
/note="Poly-Gly"
METAL 90
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 91
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 91
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 96
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 126
/note="Calcium 1; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 127
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 127
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 130
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 132
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495"
METAL 141
/note="Zinc"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329"
METAL 148
/note="Zinc"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329"
METAL 183
/note="Zinc"
/evidence="ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329"
SITE 198..199
/note="Cleavage; by autolysis"
/evidence="ECO:0000250"
SITE 244
/note="Involved in cholesterol transfer"
/evidence="ECO:0000250"
SITE 268
/note="Involved in auto-cleavage"
/evidence="ECO:0000250"
SITE 271
/note="Essential for auto-cleavage"
/evidence="ECO:0000250"
LIPID 25
/note="N-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:11486055,
ECO:0000269|PubMed:15075292"
LIPID 198
/note="Cholesterol glycine ester"
/evidence="ECO:0000269|PubMed:8824192"
CARBOHYD 279
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
MUTAGEN 25
/note="C->S: Strongly reduces effects of in vivo
overexpression; impairs multimer formation; does not affect
subcellular location to lipid rafts. Homozygous mice are
characterized by a smaller size and holoprosencephaly at
10.5 dpc, and shortening of limbs at 13.5 dpc. They die
soon after birth."
/evidence="ECO:0000269|PubMed:11486055,
ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:23118222"
MUTAGEN 32
/note="G->R: Introduces a cleavage site for a furin-like
protease resulting in abnormal protein processing; cleavage
at this site removes 11 amino acids from the N-terminal
domain and reduces affinity of Shh for Ptch1 and signaling
potency in assays using chicken embryo neural plate
explants and mouse C3H10T1/2 stem cells."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 89
/note="D->V: Moderately reduces Ptch1 binding in vitro and
signaling potency in chicken embryo neural plate explant
assays compared with wild-type sequence."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 101
/note="Q->H: Does not affect signaling activity in any of
Shh signaling assays and causes no apparent defects in
cholesterol-mediated autoprocessing reactions."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 116
/note="N->K: Shows no change in activities at different
temperatures."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 118
/note="W->G: Causes a failure of Shh processing leading to
retention of the immature glycosylated protein within the
endoplasmic reticulum of transfected cells; causes a
temperature-dependent conformational change that allows Shh
to bind Ptch1 at 4 or 32 degrees Celsius but not at 37
degrees Celsius; drastically reduces signaling potency in
chicken embryo neural plate explant assays."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 118
/note="W->R: Causes a failure of Shh processing leading to
retention of the immature glycosylated protein within the
endoplasmic reticulum of transfected cells; causes a
temperature-dependent conformational change that allows Shh
to bind Ptch1 at 4 or 32 degrees Celsius but not at 37
degrees Celsius; drastically reduces signaling potency in
chicken embryo neural plate explant assays."
/evidence="ECO:0000269|PubMed:16282375"
MUTAGEN 189
/note="E->Q: Does not affect signaling activity in any of
Shh signaling assays and causes no apparent defects in
cholesterol-mediated autoprocessing reactions."
/evidence="ECO:0000269|PubMed:16282375"
STRAND 48..52
/evidence="ECO:0000244|PDB:1VHH"
TURN 57..60
/evidence="ECO:0000244|PDB:1VHH"
STRAND 69..71
/evidence="ECO:0000244|PDB:3N1R"
HELIX 72..76
/evidence="ECO:0000244|PDB:1VHH"
STRAND 85..87
/evidence="ECO:0000244|PDB:1VHH"
STRAND 92..94
/evidence="ECO:0000244|PDB:1VHH"
HELIX 95..97
/evidence="ECO:0000244|PDB:1VHH"
HELIX 101..117
/evidence="ECO:0000244|PDB:1VHH"
STRAND 123..127
/evidence="ECO:0000244|PDB:1VHH"
STRAND 131..135
/evidence="ECO:0000244|PDB:2WG4"
HELIX 140..143
/evidence="ECO:0000244|PDB:1VHH"
STRAND 146..151
/evidence="ECO:0000244|PDB:1VHH"
HELIX 156..158
/evidence="ECO:0000244|PDB:1VHH"
HELIX 159..168
/evidence="ECO:0000244|PDB:1VHH"
STRAND 172..178
/evidence="ECO:0000244|PDB:1VHH"
STRAND 181..185
/evidence="ECO:0000244|PDB:1VHH"
HELIX 189..192
/evidence="ECO:0000244|PDB:1VHH"
SEQUENCE 437 AA; 47773 MW; D0EB72F08E7860EF CRC64;
MLLLLARCFL VILASSLLVC PGLACGPGRG FGKRRHPKKL TPLAYKQFIP NVAEKTLGAS
GRYEGKITRN SERFKELTPN YNPDIIFKDE ENTGADRLMT QRCKDKLNAL AISVMNQWPG
VKLRVTEGWD EDGHHSEESL HYEGRAVDIT TSDRDRSKYG MLARLAVEAG FDWVYYESKA
HIHCSVKAEN SVAAKSGGCF PGSATVHLEQ GGTKLVKDLR PGDRVLAADD QGRLLYSDFL
TFLDRDEGAK KVFYVIETLE PRERLLLTAA HLLFVAPHND SGPTPGPSAL FASRVRPGQR
VYVVAERGGD RRLLPAAVHS VTLREEEAGA YAPLTAHGTI LINRVLASCY AVIEEHSWAH
RAFAPFRLAH ALLAALAPAR TDGGGGGSIP AAQSATEARG AEPTAGIHWY SQLLYHIGTW
LLDSETMHPL GMAVKSS


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Catalog number Product name Quantity
orb80579 Human Sonic HedgeHog His tag protein Sonic HedgeHog Recombinant Human produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids and having a molecular mass of 20.7k 5
orb80580 Mouse Sonic HedgeHog protein Sonic Hedgehog Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The 5
orb80100 Human Sonic HedgeHog protein Sonic HedgeHog Recombinant Human produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19,683 Dalton 5
100-153 Sonic Hedgehog Human Host: E. coli Sonic Hedgehog 25
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18-272-196208 Sonic Hedgehog - Goat polyclonal to Sonic Hedgehog Polyclonal 0.05 mg
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ER601 Sonic hedgehog protein Elisa Kit 96T
EH605 Sonic hedgehog protein Elisa Kit 96T
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orb80100 Human Sonic HedgeHog protein Proteins 5
orb80580 Mouse Sonic HedgeHog protein Proteins 5
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Pathways :
WP116: Hedgehog Signaling Pathway
WP73: G Protein Signaling Pathways
WP1353: Hedgehog Signaling Pathway
WP2032: TSH signaling pathway
WP2292: Chemokine signaling pathway
WP813: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP905: Hedgehog Signaling Pathway
WP47: Hedgehog Signaling Pathway
WP1049: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP574: Hedgehog Signaling Pathway
WP492: Hedgehog Signaling Pathway
WP790: Hedgehog Signaling Pathway
WP232: G Protein Signaling Pathways
WP1022: Hedgehog Signaling Pathway
WP2203: TSLP Signaling Pathway
WP1141: Hedgehog Signaling Pathway
WP211: BMP signaling pathway
WP35: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP1672: Mismatch repair
WP1531: Vitamin D synthesis
WP346: Protein Modifications

Related Genes :
[Shh Hhg1] Sonic hedgehog protein (SHH) (HHG-1) (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) (Sonic hedgehog protein 19 kDa product)]
[SHH] Sonic hedgehog protein (SHH) (HHG-1) (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)]
[shha shh vhh1] Sonic hedgehog protein A (SHHA) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) (VHH-1) [Cleaved into: Sonic hedgehog protein A N-product (Shh N-terminal processed signaling domains) (ShhNp) (Sonic hedgehog protein N-product) (ShhN)]
[Shh Vhh-1] 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] 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] Sonic hedgehog protein (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) (VHH-1) (X-SHH) [Cleaved into: Sonic hedgehog protein N-product (ShhN) (Shh N-terminal processed signaling domains) (ShhNp)]
[IHH] Indian hedgehog protein (IHH) (HHG-2) [Cleaved into: Indian hedgehog protein N-product; Indian hedgehog protein C-product]
[shhb twhh] Tiggy-winkle hedgehog protein (TWHH) (Sonic hedgehog protein B) (SHHB) [Cleaved into: Tiggy-winkle hedgehog protein N-product; Tiggy-winkle hedgehog protein C-product]
[DHH] Desert hedgehog protein (DHH) (HHG-3) [Cleaved into: Desert hedgehog protein N-product; Desert hedgehog protein C-product]
[SHH] Sonic hedgehog protein (SHH) [Cleaved into: Sonic hedgehog protein N-product; Sonic hedgehog protein C-product]
[SHH] Sonic hedgehog signaling molecule
[SHH] Sonic hedgehog signaling molecule
[SHH] Sonic hedgehog signaling molecule
[SHH] Sonic hedgehog signaling molecule
[SHH] Sonic hedgehog signaling molecule
[hh CG4637] Protein hedgehog [Cleaved into: Protein hedgehog N-product (Hh-Np) (N-Hh); Protein hedgehog C-product (Hh-Cp) (C-Hh)]
[Hhat Skn] Protein-cysteine N-palmitoyltransferase HHAT (EC 2.3.1.-) (Hedgehog acyltransferase) (Skinny hedgehog protein)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Kmt2a All1 Hrx Mll Mll1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[SHH] Hedgehog protein
[SHH] Hedgehog protein
[SHH] Hedgehog protein
[Shh rCG_56752] Hedgehog protein
[SHH] Hedgehog protein
[SHH] Hedgehog protein
[HHAT MART2 SKI1] Protein-cysteine N-palmitoyltransferase HHAT (EC 2.3.1.-) (Hedgehog acyltransferase) (Melanoma antigen recognized by T-cells 2) (MART-2) (Skinny hedgehog protein 1)
[Creb3l1 Oasis] Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1 (Oasis N-terminal fragment) (OA-N)]
[Gli3] Transcriptional activator GLI3 (GLI3 form of 190 kDa) (GLI3-190) (GLI3 full-length protein) (GLI3FL) [Cleaved into: Transcriptional repressor GLI3R (GLI3 C-terminally truncated form) (GLI3 form of 83 kDa) (GLI3-83)]
[SHH] Hedgehog protein
[SHH] Hedgehog protein

Bibliography :