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Sonic hedgehog protein (SHH) (HHG-1) [Cleaved into: Sonic hedgehog protein N-product (Sonic hedgehog protein 19 kDa product); Sonic hedgehog protein C-product (Sonic hedgehog protein 27 kDa product)]

 SHH_MOUSE               Reviewed;         437 AA.
Q62226;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 2.
10-MAY-2017, entry version 184.
RecName: Full=Sonic hedgehog protein;
Short=SHH;
AltName: Full=HHG-1;
Contains:
RecName: Full=Sonic hedgehog protein N-product;
AltName: Full=Sonic hedgehog protein 19 kDa product;
Contains:
RecName: Full=Sonic hedgehog protein C-product;
AltName: Full=Sonic hedgehog protein 27 kDa product;
Flags: Precursor;
Name=Shh; 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.
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 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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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: 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.
Activates the transcription of target genes by interacting with
its receptor PTCH1 to prevent normal inhibition by PTCH1 on the
constitutive signaling activity of SMO.
{ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:7736596}.
-!- SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates
HHAT-mediated palmitoylation of the SHH N-terminus. N-product is
active as a multimer. Interacts with BOC and CDON. Interacts with
HHIP. {ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:18081866,
ECO:0000269|PubMed:18794898, ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495, ECO:0000269|PubMed:7477329}.
-!- SUBCELLULAR LOCATION: Sonic hedgehog protein C-product: Secreted,
extracellular space {ECO:0000269|PubMed:7891723}. Note=The C-
terminal peptide diffuses from the cell (PubMed:7891723).
-!- SUBCELLULAR LOCATION: Sonic hedgehog protein N-product: Cell
membrane {ECO:0000269|PubMed:7891723}; Lipid-anchor
{ECO:0000269|PubMed:7891723}. 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 (PubMed:7891723).
-!- 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: 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:0000269|PubMed:18794898, ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
-!- 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. {ECO:0000269|PubMed:7720571,
ECO:0000269|PubMed:7736596, ECO:0000269|PubMed:7891723}.
-!- PTM: Cholesterylation is required for N-product targeting to lipid
rafts and multimerization. {ECO:0000269|PubMed:8824192}.
-!- PTM: N-palmitoylation of Cys-25 by HHAT is required for N-product
multimerization and full activity. {ECO:0000269|PubMed:11486055,
ECO:0000269|PubMed:15075292}.
-!- MISCELLANEOUS: Mice overexpressing Shh display digit duplications
in both forelimbs and hindlimbs.
-!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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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.
UniGene; Mm.57202; -.
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; -.
ProteinModelPortal; Q62226; -.
SMR; Q62226; -.
BioGrid; 203220; 10.
DIP; DIP-48537N; -.
STRING; 10090.ENSMUSP00000002708; -.
BindingDB; Q62226; -.
ChEMBL; CHEMBL5387; -.
MEROPS; C46.002; -.
iPTMnet; Q62226; -.
PhosphoSitePlus; Q62226; -.
SwissPalm; Q62226; -.
MaxQB; Q62226; -.
PaxDb; Q62226; -.
PRIDE; Q62226; -.
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; ENSGT00390000001117; -.
HOGENOM; HOG000233428; -.
HOVERGEN; HBG005480; -.
InParanoid; Q62226; -.
KO; K11988; -.
OMA; EHSWAHR; -.
OrthoDB; EOG091G0N90; -.
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.
Bgee; ENSMUSG00000002633; -.
CleanEx; MM_SHH; -.
Genevisible; Q62226; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0001948; F:glycoprotein binding; IDA:MGI.
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 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: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: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: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: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: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: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:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription 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: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:0060021; P:palate development; IMP: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 proliferation; IDA:MGI.
GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IDA: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:0048714; P:positive regulation of oligodendrocyte differentiation; IDA: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: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 from RNA polymerase II promoter; 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 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:0060458; P:right lung 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: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: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.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR001657; Hedgehog.
InterPro; IPR028992; Hedgehog/Intein_dom.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom.
InterPro; IPR000320; Hedgehog_signalling_dom.
InterPro; IPR001767; Hint_dom.
InterPro; IPR003586; Hint_dom_C.
InterPro; IPR003587; Hint_dom_N.
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;
Complete proteome; Developmental protein; Glycoprotein; Hydrolase;
Lipoprotein; Membrane; Metal-binding; Palmitate; Protease;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 437 Sonic hedgehog protein.
/FTId=PRO_0000013211.
CHAIN 25 198 Sonic hedgehog protein N-product.
/FTId=PRO_0000013212.
CHAIN 199 437 Sonic hedgehog protein C-product.
/FTId=PRO_0000013213.
COMPBIAS 383 387 Poly-Gly.
METAL 90 90 Calcium 1. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 91 91 Calcium 1. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 91 91 Calcium 2. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 96 96 Calcium 1. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 126 126 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 127 127 Calcium 1. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 127 127 Calcium 2. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 130 130 Calcium 2. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 132 132 Calcium 2. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495}.
METAL 141 141 Zinc. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329}.
METAL 148 148 Zinc. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329}.
METAL 183 183 Zinc. {ECO:0000269|PubMed:18794898,
ECO:0000269|PubMed:19561611,
ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:7477329}.
SITE 198 199 Cleavage; by autolysis. {ECO:0000250}.
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:0000269|PubMed:11486055,
ECO:0000269|PubMed:15075292}.
LIPID 198 198 Cholesterol glycine ester.
{ECO:0000269|PubMed:8824192}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 25 25 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 E10.5, and
shortening of limbs at E13.5. They die
soon after birth.
{ECO:0000269|PubMed:11486055,
ECO:0000269|PubMed:15075292}.
MUTAGEN 32 32 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.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 89 89 D->V: Moderately reduces Ptch1 binding in
vitro and signaling potency in chicken
embryo neural plate explant assays
compared with wild-type sequence.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 101 101 Q->H: Does not affect signaling activity
in any of Shh signaling assays and causes
no apparent defects in cholesterol-
mediated autoprocessing reactions.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 116 116 N->K: Shows no change in activities at
different temperatures.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 118 118 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.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 118 118 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.
{ECO:0000269|PubMed:16282375}.
MUTAGEN 189 189 E->Q: Does not affect signaling activity
in any of Shh signaling assays and causes
no apparent defects in cholesterol-
mediated autoprocessing reactions.
{ECO:0000269|PubMed:16282375}.
STRAND 48 52 {ECO:0000244|PDB:1VHH}.
TURN 57 60 {ECO:0000244|PDB:1VHH}.
STRAND 69 71 {ECO:0000244|PDB:3N1R}.
HELIX 72 76 {ECO:0000244|PDB:1VHH}.
STRAND 85 87 {ECO:0000244|PDB:1VHH}.
STRAND 92 94 {ECO:0000244|PDB:1VHH}.
HELIX 95 97 {ECO:0000244|PDB:1VHH}.
HELIX 101 117 {ECO:0000244|PDB:1VHH}.
STRAND 123 127 {ECO:0000244|PDB:1VHH}.
STRAND 131 135 {ECO:0000244|PDB:2WG4}.
HELIX 140 143 {ECO:0000244|PDB:1VHH}.
STRAND 146 151 {ECO:0000244|PDB:1VHH}.
HELIX 156 158 {ECO:0000244|PDB:1VHH}.
HELIX 159 168 {ECO:0000244|PDB:1VHH}.
STRAND 172 178 {ECO:0000244|PDB:1VHH}.
STRAND 181 185 {ECO:0000244|PDB:1VHH}.
HELIX 189 192 {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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