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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.
25-OCT-2017, entry version 186.
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;
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;
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]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
{ECO:0000250|UniProtKB:Q15465, ECO:0000269|PubMed:15075292,
ECO:0000269|PubMed:18081866, 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:
Q4KMG0:CDON (xeno); NbExp=6; IntAct=EBI-15610166, EBI-7016840;
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.
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; -.
IntAct; Q62226; 6.
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: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; 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; 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;
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_0000013211.
CHAIN 25 198 Sonic hedgehog protein N-product.
/FTId=PRO_0000013212.
MOTIF 33 39 Cardin-Weintraub.
{ECO:0000269|PubMed:23118222}.
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,
ECO:0000269|PubMed:23118222}.
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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52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur