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UniProtKB/Swiss-Prot entry Q91035


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SHH_CHICK
Primary accession number Q91035
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 74)
Name and origin of the protein
Protein name Sonic hedgehog protein [Precursor]
Synonym SHH
Contains Sonic hedgehog protein N-product
Sonic hedgehog protein C-product
Gene name
Name: SHH
From
Gallus gallus (Chicken) [TaxID: 9031] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Limb bud;
DOI=10.1016/0092-8674(93)90626-2; PubMed=8269518 [NCBI, ExPASy, EBI, Israel, Japan]
Riddle R.D., Johnson R.L., Laufer E., Tabin C.;
"Sonic hedgehog mediates the polarizing activity of the ZPA.";
Cell 75:1401-1416(1993).
[2]
FUNCTION, AND AUTOPROTEOLYTIC CLEAVAGE.
DOI=10.1016/0092-8674(95)90397-6; PubMed=7736596 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • FUNCTION: Binds to the patched (PTC) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTC represses the constitutive signaling activity of SMO. Also regulates another target, the gli oncogene. 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.
  • SUBUNIT: N-product is active as a multimer (By similarity).
  • SUBCELLULAR LOCATION: Sonic hedgehog protein C-product: Secreted, extracellular space (By similarity). Note=The C-terminal peptide diffuses from the cell (By similarity).
  • SUBCELLULAR LOCATION: Sonic hedgehog protein N-product: Cell membrane; Lipid-anchor (By similarity). 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 (By similarity).
  • TISSUE SPECIFICITY: Expressed in the posterior limb bud mesenchyme, the Hensen node, the notochord, and the floor plate of the neural tube.
  • DEVELOPMENTAL STAGE: First detectable at stage 17 during the initiation of limb bud formation. From that point onwards, the expression pattern exactly matches the location of the zone of polarizing activity (ZPA).
  • INDUCTION: By retinoic acid.
  • 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.
  • PTM: Cholesterylation is required for N-product targeting to lipid rafts and multimerization (By similarity).
  • PTM: N-palmitoylation of Cys-27 by HHAT is required for N-product multimerization and full activity (By similarity).
  • SIMILARITY: Belongs to the hedgehog family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L28099; AAA72428.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00604018; -.
PIR A49424; A49424.
RefSeq NP_990152.1; -.
UniGene Gga.345
3D structure databases
HSSP Q62226; 1VHH. [HSSP ENTRY / PDB]
SMR Q91035; 41-197.
ModBase Q91035.
Protein family/group databases
MEROPS C46.002; -.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016015; Molecular function: morphogen activity (non-traceable author statement from Roslin).
GO:0008233; Molecular function: peptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0042733; Biological process: embryonic digit morphogenesis (inferred from mutant phenotype from Roslin).
GO:0008624; Biological process: induction of apoptosis by extracellular signals (inferred from direct assay from Roslin).
GO:0016539; Biological process: intein-mediated protein splicing (inferred from electronic annotation from InterPro).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from direct assay from Roslin).
GO:0009949; Biological process: polarity specification of anterior/posterior axis (inferred from mutant phenotype from Roslin).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0032526; Biological process: response to retinoic acid (inferred from direct assay from Roslin).
QuickGo view.
Family and domain databases
InterPro IPR003586; Hedgehog_hint_C.
IPR003587; Hedgehog_hint_N.
IPR000320; HH_signal.
IPR006141; Intein_splicing_site.
IPR001657; Peptidase_C46.
IPR001767; Peptidase_C46_hint.
Graphical view of domain structure.
Pfam PF01085; HH_signal; 1.
PF01079; Hint; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF009400; Peptidase_C46; 1.
PRINTS PR00632; SONICHHOG.
SMART SM00305; HintC; 1.
SM00306; HintN; 1.
SMART graphical view of domain structure.
PROSITE PS50817; INTEIN_N_TER; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q91035; -.
Genome annotation databases
Ensembl ENSGALG00000006379; Gallus gallus. [Contig view]
GeneID 395615; -.
KEGG gga:395615; -.
Phylogenomic databases
HOGENOM Q91035; -.
HOVERGEN Q91035; -.
Other
ProtoNet Q91035.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autocatalytic cleavage; Cell membrane; Developmental protein; Hydrolase; Lipoprotein; Membrane; Palmitate; Protease; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26     Potential. 
CHAIN   27   425  399     Sonic hedgehog protein. PRO_0000013217
CHAIN   27   200  174     Sonic hedgehog protein N-product. PRO_0000013218
CHAIN   201   425  225     Sonic hedgehog protein C-product. PRO_0000013219
COMPBIAS   390   393  4     Poly-Thr. 
SITE   200   201  2     Cleavage; by autolysis (Probable). 
SITE   246   246  1     Involved in cholesterol transfer (By similarity). 
SITE   270   270  1     Involved in auto-cleavage (By similarity). 
SITE   273   273  1     Essential for auto-cleavage (By similarity). 
LIPID   27    27        N-palmitoyl cysteine (By similarity). 
LIPID   200   200        Cholesterol glycine ester (By similarity). 
Sequence information
Length: 425 AA [This is the length of the unprocessed precursor] Molecular weight: 46474 Da [This is the MW of the unprocessed precursor] CRC64: DA9627443D4A0173 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVEMLLLTRI LLVGFICALL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG 

        70         80         90        100        110        120 
ASGRYEGKIT RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW 

       130        140        150        160        170        180 
PGVKLRVTEG WDEDGHHSEE SLHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES 

       190        200        210        220        230        240 
KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EHGGTKLVKD LSPGDRVLAA DADGRLLYSD 

       250        260        270        280        290        300 
FLTFLDRMDS SRKLFYVIET RQPRARLLLT AAHLLFVAPQ HNQSEATGST SGQALFASNV 

       310        320        330        340        350        360 
KPGQRVYVLG EGGQQLLPAS VHSVSLREEA SGAYAPLTAQ GTILINRVLA SCYAVIEEHS 

       370        380        390        400        410        420 
WAHWAFAPFR LAQGLLAALC PDGAIPTAAT TTTGIHWYSR LLYRIGSWVL DGDALHPLGM 


VAPAS 

Q91035 in FASTA format

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