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Q02936

- HH_DROME

UniProt

Q02936 - HH_DROME

Protein

Protein hedgehog

Gene

hh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Intercellular signal essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu).
    The hedgehog protein N-product constitutes the active species in both local and long-range signaling, whereas the C-terminal product has no signaling activity. It acts as a morphogen, and diffuses long distances despite its lipidation. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation.
    The hedgehog protein C-product, which mediates the autocatalytic activity, has no signaling activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei257 – 2582Cleavage; by autolysis
    Sitei303 – 3031Involved in cholesterol transfer
    Sitei326 – 3261Involved in auto-cleavage
    Sitei329 – 3291Essential for auto-cleavage

    GO - Molecular functioni

    1. morphogen activity Source: FlyBase
    2. patched binding Source: UniProtKB
    3. peptidase activity Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. smoothened binding Source: UniProtKB

    GO - Biological processi

    1. analia development Source: FlyBase
    2. anterior/posterior axis specification, embryo Source: FlyBase
    3. anterior/posterior lineage restriction, imaginal disc Source: FlyBase
    4. anterior commissure morphogenesis Source: FlyBase
    5. anterior head segmentation Source: FlyBase
    6. Bolwig's organ morphogenesis Source: FlyBase
    7. cell-cell signaling involved in cell fate commitment Source: UniProtKB
    8. compartment pattern specification Source: FlyBase
    9. compound eye morphogenesis Source: FlyBase
    10. compound eye photoreceptor cell differentiation Source: FlyBase
    11. cytoneme assembly Source: FlyBase
    12. developmental pigmentation Source: FlyBase
    13. ectoderm development Source: FlyBase
    14. embryonic pattern specification Source: UniProtKB
    15. epidermis development Source: FlyBase
    16. epithelial cell migration, open tracheal system Source: FlyBase
    17. eye morphogenesis Source: FlyBase
    18. foregut morphogenesis Source: FlyBase
    19. genital disc anterior/posterior pattern formation Source: FlyBase
    20. genital disc development Source: FlyBase
    21. germ cell attraction Source: FlyBase
    22. germ cell migration Source: FlyBase
    23. germ-line stem cell division Source: FlyBase
    24. glial cell migration Source: FlyBase
    25. gonadal mesoderm development Source: FlyBase
    26. growth Source: FlyBase
    27. heart development Source: FlyBase
    28. heart formation Source: FlyBase
    29. hindgut morphogenesis Source: FlyBase
    30. imaginal disc-derived wing vein specification Source: FlyBase
    31. imaginal disc growth Source: FlyBase
    32. imaginal disc pattern formation Source: FlyBase
    33. intein-mediated protein splicing Source: InterPro
    34. labial disc development Source: FlyBase
    35. leg disc morphogenesis Source: FlyBase
    36. mesoderm development Source: FlyBase
    37. morphogenesis of larval imaginal disc epithelium Source: FlyBase
    38. negative regulation of protein ubiquitination Source: FlyBase
    39. negative regulation of proteolysis Source: FlyBase
    40. open tracheal system development Source: FlyBase
    41. ovarian follicle cell development Source: FlyBase
    42. ovarian follicle cell stalk formation Source: FlyBase
    43. pole cell migration Source: FlyBase
    44. positive regulation of hh target transcription factor activity Source: FlyBase
    45. positive regulation of smoothened signaling pathway Source: FlyBase
    46. positive regulation of transcription factor import into nucleus Source: FlyBase
    47. posterior head segmentation Source: FlyBase
    48. progression of morphogenetic furrow involved in compound eye morphogenesis Source: FlyBase
    49. protein autoprocessing Source: UniProtKB
    50. R8 cell fate specification Source: FlyBase
    51. regulation of cell proliferation Source: FlyBase
    52. regulation of mitotic cell cycle Source: FlyBase
    53. regulation of organ growth Source: FlyBase
    54. regulation of protein import into nucleus Source: FlyBase
    55. regulation of transcription from RNA polymerase II promoter Source: FlyBase
    56. segment polarity determination Source: UniProtKB
    57. smoothened signaling pathway Source: FlyBase
    58. somatic stem cell division Source: FlyBase
    59. spiracle morphogenesis, open tracheal system Source: FlyBase
    60. trunk segmentation Source: FlyBase
    61. ventral midline development Source: FlyBase
    62. wing disc anterior/posterior pattern formation Source: FlyBase
    63. wing disc proximal/distal pattern formation Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Morphogen, Protease, Segmentation polarity protein

    Enzyme and pathway databases

    SignaLinkiQ02936.

    Protein family/group databases

    MEROPSiC46.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein hedgehog
    Cleaved into the following 2 chains:
    Protein hedgehog N-product
    Short name:
    Hh-Np
    Short name:
    N-Hh
    Alternative name(s):
    C-Hh
    Gene namesi
    Name:hh
    ORF Names:CG4637
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0004644. hh.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells.
    Chain Protein hedgehog N-product : Cell membrane; Lipid-anchor; Extracellular side
    Note: The N-terminal peptide remains associated with the cell surface.
    Chain Protein hedgehog C-product : Secretedextracellular space
    Note: The C-terminal peptide diffuses from the cell.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: FlyBase
    3. endocytic vesicle Source: FlyBase
    4. endosome Source: FlyBase
    5. extracellular region Source: UniProtKB
    6. extracellular space Source: FlyBase
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851C → S: N-product is made but fails to undergo palmitoylation. 3 Publications
    Mutagenesisi303 – 3031D → A: No cholesterol transfer. 1 Publication
    Mutagenesisi326 – 3261T → A: Greatly reduced autoprocessing activity. 1 Publication
    Mutagenesisi329 – 3291H → A: No autoprocessing activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 84Sequence AnalysisPRO_0000383048
    Signal peptidei1 – ?Sequence Analysis
    Chaini85 – 471387Protein hedgehogPRO_0000013202Add
    BLAST
    Chaini85 – 257173Protein hedgehog N-productPRO_0000013203Add
    BLAST
    Chaini258 – 471214Protein hedgehog C-productPRO_0000013204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi85 – 851N-palmitoyl cysteine1 Publication
    Lipidationi257 – 2571Cholesterol glycine ester

    Post-translational modificationi

    The C-terminal domain displays autoproteolytic activity. Cleavage of the full-length hedgehog protein is followed by the covalent attachment of a cholesterol moiety to the C-terminus of the newly generated N-terminal fragment (N-product).
    Cholesterol attachment plays an essential role in restricting the spatial distribution of hedgehog activity to the cell surface.
    N-terminal palmitoylation of the hedgehog N-product is required for the embryonic and larval patterning activities of the hedgehog signal. Rasp acts within the secretory pathway to catalyze the N-terminal palmitoylation of Hh.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Lipoprotein, Palmitate

    Miscellaneous databases

    PMAP-CutDBQ02936.

    Expressioni

    Tissue specificityi

    In embryos, expression starts at stage 5 as a few stripes at the anterior and posterior ends, this expands to 17 stripes during stages 8-11. Expression is also seen in CNS and some PNS cells until stage 13-14, and in foregut, hindgut and salivary glands. In larvae, expression is seen in the posterior compartment of the wing imaginal disk.4 Publications

    Developmental stagei

    Expressed in embryos, larvae and pupae at high levels with maximum expression in 6-12 hours embryos and 0-24 hours pupae. Low levels of expression are seen in adults.4 Publications

    Gene expression databases

    BgeeiQ02936.

    Interactioni

    Subunit structurei

    Interacts with shf.1 Publication

    Protein-protein interaction databases

    BioGridi67682. 37 interactions.
    DIPiDIP-51313N.
    IntActiQ02936. 2 interactions.
    STRINGi7227.FBpp0099945.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi107 – 1115
    Turni116 – 1194
    Helixi131 – 1355
    Beta strandi144 – 1463
    Helixi160 – 17617
    Beta strandi182 – 1887
    Helixi199 – 2024
    Beta strandi205 – 2106
    Helixi215 – 2173
    Helixi218 – 22811
    Beta strandi231 – 2344
    Beta strandi241 – 2444
    Beta strandi264 – 2674
    Beta strandi272 – 2743
    Helixi275 – 2773
    Beta strandi283 – 2875
    Beta strandi293 – 31725
    Beta strandi322 – 3254
    Beta strandi330 – 3356
    Turni336 – 3394
    Beta strandi340 – 3456
    Helixi346 – 3483
    Beta strandi354 – 3585
    Turni360 – 3623
    Beta strandi365 – 39329
    Beta strandi396 – 4005

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AT0X-ray1.90A258-402[»]
    2IBGX-ray2.20E/F/G/H99-248[»]
    ProteinModelPortaliQ02936.
    SMRiQ02936. Positions 100-248, 258-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02936.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 4137Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the hedgehog family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250647.
    GeneTreeiENSGT00390000001117.
    InParanoidiQ02936.
    KOiK06224.
    OMAiHSCGPGR.
    OrthoDBiEOG779NZ5.
    PhylomeDBiQ02936.

    Family and domain databases

    Gene3Di2.170.16.10. 1 hit.
    3.30.1380.10. 1 hit.
    InterProiIPR001657. Hedgehog.
    IPR028992. Hedgehog/Intein_dom.
    IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
    IPR000320. Hedgehog_signalling_dom.
    IPR001767. Hint_dom.
    IPR003586. Hint_dom_C.
    IPR003587. Hint_dom_N.
    IPR006141. Intein_splice_site.
    [Graphical view]
    PfamiPF01085. HH_signal. 1 hit.
    PF01079. Hint. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009400. Peptidase_C46. 1 hit.
    PRINTSiPR00632. SONICHHOG.
    SMARTiSM00305. HintC. 1 hit.
    SM00306. HintN. 1 hit.
    [Graphical view]
    SUPFAMiSSF51294. SSF51294. 1 hit.
    SSF55166. SSF55166. 1 hit.
    PROSITEiPS50817. INTEIN_N_TER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q02936-1) [UniParc]FASTAAdd to Basket

    Also known as: A, B

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDNHSSVPWA SAASVTCLSL DAKCHSSSSS SSSKSAASSI SAIPQEETQT    50
    MRHIAHTQRC LSRLTSLVAL LLIVLPMVFS PAHSCGPGRG LGRHRARNLY 100
    PLVLKQTIPN LSEYTNSASG PLEGVIRRDS PKFKDLVPNY NRDILFRDEE 150
    GTGADRLMSK RCKEKLNVLA YSVMNEWPGI RLLVTESWDE DYHHGQESLH 200
    YEGRAVTIAT SDRDQSKYGM LARLAVEAGF DWVSYVSRRH IYCSVKSDSS 250
    ISSHVHGCFT PESTALLESG VRKPLGELSI GDRVLSMTAN GQAVYSEVIL 300
    FMDRNLEQMQ NFVQLHTDGG AVLTVTPAHL VSVWQPESQK LTFVFADRIE 350
    EKNQVLVRDV ETGELRPQRV VKVGSVRSKG VVAPLTREGT IVVNSVAASC 400
    YAVINSQSLA HWGLAPMRLL STLEAWLPAK EQLHSSPKVV SSAQQQNGIH 450
    WYANALYKVK DYVLPQSWRH D 471
    Length:471
    Mass (Da):52,150
    Last modified:September 1, 2009 - v4
    Checksum:i8ECD796A92FE7043
    GO
    Isoform Short (identifier: Q02936-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         161-192: RCKEKLNVLAYSVMNEWPGIRLLVTESWDEDY → VRKTLKHRKLVTKFVIHHWESFAYRNHCDKVT
         193-471: Missing.

    Show »
    Length:192
    Mass (Da):21,323
    Checksum:iC19D4D9EF4367D47
    GO

    Sequence cautioni

    The sequence AAA28604.1 differs from that shown. Reason: Frameshift at positions 21 and 48.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561R → G in AAA28604. (PubMed:8166882)Curated
    Sequence conflicti347 – 3471D → H in AAA28604. (PubMed:8166882)Curated
    Sequence conflicti373 – 3731V → L in AAA28604. (PubMed:8166882)Curated
    Sequence conflicti407 – 4071Q → P in Z11840. (PubMed:1280560)Curated

    Mass spectrometryi

    Molecular mass is 20238.44 Da from positions 85 - 257. Determined by MALDI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei161 – 19232RCKEK…WDEDY → VRKTLKHRKLVTKFVIHHWE SFAYRNHCDKVT in isoform Short. CuratedVSP_002065Add
    BLAST
    Alternative sequencei193 – 471279Missing in isoform Short. CuratedVSP_002066Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05404 mRNA. Translation: AAA28604.1. Frameshift.
    L05405 Genomic DNA. No translation available.
    L02793 Unassigned DNA. Translation: AAA16458.1.
    Z11840 Genomic DNA. No translation available.
    S66384 mRNA. Translation: AAB28646.1.
    AE014297 Genomic DNA. Translation: AAF56102.1.
    AE014297 Genomic DNA. Translation: ABC66186.1.
    PIRiA46400.
    RefSeqiNP_001034065.1. NM_001038976.1. [Q02936-1]
    UniGeneiDm.2371.

    Genome annotation databases

    EnsemblMetazoaiFBtr0100506; FBpp0099945; FBgn0004644. [Q02936-1]
    GeneIDi42737.
    KEGGidme:Dmel_CG4637.
    UCSCiCG4637-RA. d. melanogaster. [Q02936-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05404 mRNA. Translation: AAA28604.1 . Frameshift.
    L05405 Genomic DNA. No translation available.
    L02793 Unassigned DNA. Translation: AAA16458.1 .
    Z11840 Genomic DNA. No translation available.
    S66384 mRNA. Translation: AAB28646.1 .
    AE014297 Genomic DNA. Translation: AAF56102.1 .
    AE014297 Genomic DNA. Translation: ABC66186.1 .
    PIRi A46400.
    RefSeqi NP_001034065.1. NM_001038976.1. [Q02936-1 ]
    UniGenei Dm.2371.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AT0 X-ray 1.90 A 258-402 [» ]
    2IBG X-ray 2.20 E/F/G/H 99-248 [» ]
    ProteinModelPortali Q02936.
    SMRi Q02936. Positions 100-248, 258-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67682. 37 interactions.
    DIPi DIP-51313N.
    IntActi Q02936. 2 interactions.
    STRINGi 7227.FBpp0099945.

    Protein family/group databases

    MEROPSi C46.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0100506 ; FBpp0099945 ; FBgn0004644 . [Q02936-1 ]
    GeneIDi 42737.
    KEGGi dme:Dmel_CG4637.
    UCSCi CG4637-RA. d. melanogaster. [Q02936-1 ]

    Organism-specific databases

    CTDi 42737.
    FlyBasei FBgn0004644. hh.

    Phylogenomic databases

    eggNOGi NOG250647.
    GeneTreei ENSGT00390000001117.
    InParanoidi Q02936.
    KOi K06224.
    OMAi HSCGPGR.
    OrthoDBi EOG779NZ5.
    PhylomeDBi Q02936.

    Enzyme and pathway databases

    SignaLinki Q02936.

    Miscellaneous databases

    EvolutionaryTracei Q02936.
    GenomeRNAii 42737.
    NextBioi 830301.
    PMAP-CutDB Q02936.
    PROi Q02936.

    Gene expression databases

    Bgeei Q02936.

    Family and domain databases

    Gene3Di 2.170.16.10. 1 hit.
    3.30.1380.10. 1 hit.
    InterProi IPR001657. Hedgehog.
    IPR028992. Hedgehog/Intein_dom.
    IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
    IPR000320. Hedgehog_signalling_dom.
    IPR001767. Hint_dom.
    IPR003586. Hint_dom_C.
    IPR003587. Hint_dom_N.
    IPR006141. Intein_splice_site.
    [Graphical view ]
    Pfami PF01085. HH_signal. 1 hit.
    PF01079. Hint. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009400. Peptidase_C46. 1 hit.
    PRINTSi PR00632. SONICHHOG.
    SMARTi SM00305. HintC. 1 hit.
    SM00306. HintN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51294. SSF51294. 1 hit.
    SSF55166. SSF55166. 1 hit.
    PROSITEi PS50817. INTEIN_N_TER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of hedgehog, a Drosophila segment-polarity gene required for cell-cell communication."
      Tashiro S., Michiue T., Higashijima S., Zenno S., Ishimaru S., Takahashi F., Orihara M., Kojima T., Saigo K.
      Gene 124:183-189(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Strain: Canton-S.
      Tissue: Embryo.
    2. "Secretion and localized transcription suggest a role in positional signaling for products of the segmentation gene hedgehog."
      Lee J.J., von Kessler D.P., Parks S., Beachy P.A.
      Cell 71:33-50(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    3. "Molecular organization and embryonic expression of the hedgehog gene involved in cell-cell communication in segmental patterning of Drosophila."
      Mohler J., Vani K.
      Development 115:957-971(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Strain: Oregon-R.
      Tissue: Embryo.
    4. "The Drosophila hedgehog gene is expressed specifically in posterior compartment cells and is a target of engrailed regulation."
      Tabata T., Eaton S., Kornberg T.B.
      Genes Dev. 6:2635-2645(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Strain: Oregon-R.
      Tissue: Embryo.
    5. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    6. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    7. "The product of hedgehog autoproteolytic cleavage active in local and long-range signalling."
      Porter J.A., von Kessler D.P., Ekker S.C., Young K.E., Lee J.J., Moses K., Beachy P.A.
      Nature 374:363-366(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOCATALYTIC CLEAVAGE, PROTEOLYTIC PROCESSING.
    8. "An acylatable residue of Hedgehog is differentially required in Drosophila and mouse limb development."
      Lee J.D., Kraus P., Gaiano N., Nery S., Kohtz J., Fishell G., Loomis C.A., Treisman J.E.
      Dev. Biol. 233:122-136(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
    9. "Skinny hedgehog, an acyltransferase required for palmitoylation and activity of the hedgehog signal."
      Chamoun Z., Mann R.K., Nellen D., von Kessler D.P., Bellotto M., Beachy P.A., Basler K.
      Science 293:2080-2084(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-85, MUTAGENESIS OF CYS-85, MASS SPECTROMETRY.
    10. "Cholesterol modification of hedgehog is required for trafficking and movement, revealing an asymmetric cellular response to hedgehog."
      Gallet A., Rodriguez R., Ruel L., Therond P.P.
      Dev. Cell 4:191-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF CHOLESTEROL.
    11. "The Drosophila ortholog of the human wnt inhibitor factor shifted controls the diffusion of lipid-modified hedgehog."
      Gorfinkiel N., Sierra J., Callejo A., Ibanez C., Guerrero I.
      Dev. Cell 8:241-253(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHF.
    12. "Lipoprotein particles are required for Hedgehog and Wingless signalling."
      Panakova D., Sprong H., Marois E., Thiele C., Eaton S.
      Nature 435:58-65(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF LIPOPHORIN IN MOVEMENT.
    13. "Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins."
      Hall T.M.T., Porter J.A., Young K.E., Koonin E.V., Beachy P.A., Leahy D.J.
      Cell 91:85-97(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 258-402, MUTAGENESIS.

    Entry informationi

    Entry nameiHH_DROME
    AccessioniPrimary (citable) accession number: Q02936
    Secondary accession number(s): A4V396, Q9VCQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 164 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3