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Q02936 (HH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein hedgehog

Cleaved into the following 2 chains:

  1. Protein hedgehog N-product
    Short name=Hh-Np
    Short name=N-Hh
  2. Protein hedgehog C-product
    Short name=Hh-Cp
    Alternative name(s):
    C-Hh
Gene names
Name:hh
ORF Names:CG4637
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.2 Ref.4 Ref.8

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. Ref.1 Ref.2 Ref.4 Ref.8

The hedgehog protein C-product, which mediates the autocatalytic activity, has no signaling activity. Ref.1 Ref.2 Ref.4 Ref.8

Subunit structure

Interacts with shf. Ref.11

Subcellular location

Nucleus. Cytoplasm. 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. Ref.3

Protein hedgehog N-product: Cell membrane; Lipid-anchor; Extracellular side. Note: The N-terminal peptide remains associated with the cell surface. Ref.3

Protein hedgehog C-product: Secretedextracellular space. Note: The C-terminal peptide diffuses from the cell. Ref.3

Tissue specificity

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. Ref.1 Ref.2 Ref.3 Ref.4

Developmental stage

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. Ref.1 Ref.2 Ref.3 Ref.4

Post-translational modification

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. Ref.9

Sequence similarities

Belongs to the hedgehog family.

Mass spectrometry

Molecular mass is 20238.44 Da from positions 85 - 257. Determined by MALDI. Ref.9

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionDevelopmental protein
Hydrolase
Morphogen
Protease
Segmentation polarity protein
   PTMAutocatalytic cleavage
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBolwig's organ morphogenesis

Inferred from mutant phenotype PubMed 10704398. Source: FlyBase

R8 cell fate specification

Non-traceable author statement PubMed 11880339. Source: FlyBase

analia development

Traceable author statement PubMed 11494318. Source: FlyBase

anterior commissure morphogenesis

Inferred from mutant phenotype PubMed 16467357. Source: FlyBase

anterior head segmentation

Traceable author statement PubMed 15382142. Source: FlyBase

anterior/posterior axis specification, embryo

Non-traceable author statement PubMed 11839291. Source: FlyBase

anterior/posterior lineage restriction, imaginal disc

Traceable author statement PubMed 10625531. Source: FlyBase

cell-cell signaling involved in cell fate commitment

Inferred from mutant phenotype Ref.3. Source: UniProtKB

compartment pattern specification

Traceable author statement PubMed 11253649. Source: FlyBase

compound eye morphogenesis

Traceable author statement PubMed 10704398. Source: FlyBase

compound eye photoreceptor cell differentiation

Traceable author statement PubMed 15273984. Source: FlyBase

cytoneme assembly

Inferred from mutant phenotype PubMed 10367889. Source: FlyBase

developmental pigmentation

Traceable author statement PubMed 12957543. Source: FlyBase

ectoderm development

Non-traceable author statement PubMed 10973066. Source: FlyBase

embryonic pattern specification

Inferred from expression pattern Ref.2. Source: UniProtKB

epidermis development

Traceable author statement PubMed 10837029. Source: FlyBase

epithelial cell migration, open tracheal system

Inferred from mutant phenotype PubMed 11290298. Source: FlyBase

eye morphogenesis

Inferred from mutant phenotype PubMed 16651542. Source: FlyBase

foregut morphogenesis

Traceable author statement PubMed 10512197. Source: FlyBase

genital disc anterior/posterior pattern formation

Inferred from expression pattern PubMed 8798147. Source: FlyBase

genital disc development

Inferred from mutant phenotype PubMed 15893978. Source: FlyBase

germ cell attraction

Traceable author statement PubMed 12814944. Source: FlyBase

germ cell migration

Inferred from mutant phenotype PubMed 9435287. Source: FlyBase

germ-line stem cell division

Traceable author statement PubMed 11131529PubMed 12459723. Source: FlyBase

glial cell migration

Inferred from mutant phenotype PubMed 11804568. Source: FlyBase

gonadal mesoderm development

Inferred from mutant phenotype PubMed 9435287. Source: FlyBase

growth

Non-traceable author statement PubMed 11128988. Source: FlyBase

heart development

Non-traceable author statement PubMed 12027431. Source: FlyBase

heart formation

Inferred from mutant phenotype PubMed 8660881. Source: FlyBase

hindgut morphogenesis

Inferred from mutant phenotype PubMed 11231061. Source: FlyBase

imaginal disc growth

Traceable author statement PubMed 14691557. Source: FlyBase

imaginal disc pattern formation

Non-traceable author statement PubMed 11377964. Source: FlyBase

imaginal disc-derived wing vein specification

Traceable author statement PubMed 10625531. Source: FlyBase

intein-mediated protein splicing

Inferred from electronic annotation. Source: InterPro

labial disc development

Inferred from mutant phenotype PubMed 15680366. Source: FlyBase

leg disc morphogenesis

Traceable author statement PubMed 11494318. Source: FlyBase

mesoderm development

Non-traceable author statement PubMed 10973066. Source: FlyBase

morphogenesis of larval imaginal disc epithelium

Inferred from mutant phenotype PubMed 16236766. Source: FlyBase

negative regulation of protein ubiquitination

Inferred from direct assay PubMed 24244405. Source: FlyBase

negative regulation of proteolysis

Inferred from mutant phenotype PubMed 20850429. Source: FlyBase

open tracheal system development

Traceable author statement PubMed 14570584. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

ovarian follicle cell stalk formation

Traceable author statement PubMed 10822261. Source: FlyBase

pole cell migration

Inferred from genetic interaction PubMed 16256738. Source: FlyBase

positive regulation of hh target transcription factor activity

Inferred from genetic interaction PubMed 9874371. Source: FlyBase

positive regulation of smoothened signaling pathway

Traceable author statement PubMed 10497093. Source: FlyBase

positive regulation of transcription factor import into nucleus

Inferred from mutant phenotype PubMed 11090136. Source: FlyBase

posterior head segmentation

Traceable author statement PubMed 15382142. Source: FlyBase

progression of morphogenetic furrow involved in compound eye morphogenesis

Inferred from mutant phenotype PubMed 8252628. Source: FlyBase

protein autoprocessing

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of cell proliferation

Non-traceable author statement PubMed 11494318. Source: FlyBase

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 11279500. Source: FlyBase

regulation of organ growth

Traceable author statement PubMed 11377964. Source: FlyBase

regulation of protein import into nucleus

Inferred from mutant phenotype PubMed 14597576. Source: FlyBase

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 11743020. Source: FlyBase

segment polarity determination

Inferred from expression pattern Ref.3Ref.1. Source: UniProtKB

smoothened signaling pathway

Inferred from genetic interaction PubMed 8700230. Source: FlyBase

somatic stem cell division

Traceable author statement PubMed 12459723. Source: FlyBase

spiracle morphogenesis, open tracheal system

Inferred from mutant phenotype PubMed 15930099. Source: FlyBase

trunk segmentation

Traceable author statement PubMed 15382142. Source: FlyBase

ventral midline development

Inferred from mutant phenotype PubMed 16467357. Source: FlyBase

wing disc anterior/posterior pattern formation

Traceable author statement PubMed 10625531PubMed 11253649PubMed 12717815PubMed 15104233. Source: FlyBase

wing disc proximal/distal pattern formation

Traceable author statement PubMed 12717815. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.10. Source: FlyBase

endocytic vesicle

Inferred from direct assay PubMed 18198278. Source: FlyBase

endosome

Inferred from direct assay PubMed 17484784. Source: FlyBase

extracellular region

Non-traceable author statement Ref.3. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17484784. Source: FlyBase

nucleus

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Non-traceable author statement Ref.3. Source: UniProtKB

   Molecular_functionmorphogen activity

Traceable author statement PubMed 11494318. Source: FlyBase

patched binding

Non-traceable author statement Ref.4. Source: UniProtKB

peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11PubMed 16630821. Source: UniProtKB

smoothened binding

Non-traceable author statement Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q02936-1)

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.
Isoform Short (identifier: Q02936-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Propeptide? – 84 PotentialPRO_0000383048
Chain85 – 471387Protein hedgehog
PRO_0000013202
Chain85 – 257173Protein hedgehog N-product
PRO_0000013203
Chain258 – 471214Protein hedgehog C-product
PRO_0000013204

Regions

Compositional bias5 – 4137Ser-rich

Sites

Site257 – 2582Cleavage; by autolysis
Site3031Involved in cholesterol transfer
Site3261Involved in auto-cleavage
Site3291Essential for auto-cleavage

Amino acid modifications

Lipidation851N-palmitoyl cysteine Ref.9
Lipidation2571Cholesterol glycine ester

Natural variations

Alternative sequence161 – 19232RCKEK…WDEDY → VRKTLKHRKLVTKFVIHHWE SFAYRNHCDKVT in isoform Short.
VSP_002065
Alternative sequence193 – 471279Missing in isoform Short.
VSP_002066

Experimental info

Mutagenesis851C → S: N-product is made but fails to undergo palmitoylation. Ref.8 Ref.9
Mutagenesis3031D → A: No cholesterol transfer.
Mutagenesis3261T → A: Greatly reduced autoprocessing activity.
Mutagenesis3291H → A: No autoprocessing activity.
Sequence conflict1561R → G in AAA28604. Ref.1
Sequence conflict3471D → H in AAA28604. Ref.1
Sequence conflict3731V → L in AAA28604. Ref.1
Sequence conflict4071Q → P in Z11840. Ref.3

Secondary structure

................................................ 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (A) (B) [UniParc].

Last modified September 1, 2009. Version 4.
Checksum: 8ECD796A92FE7043

FASTA47152,150
        10         20         30         40         50         60 
MDNHSSVPWA SAASVTCLSL DAKCHSSSSS SSSKSAASSI SAIPQEETQT MRHIAHTQRC 

        70         80         90        100        110        120 
LSRLTSLVAL LLIVLPMVFS PAHSCGPGRG LGRHRARNLY PLVLKQTIPN LSEYTNSASG 

       130        140        150        160        170        180 
PLEGVIRRDS PKFKDLVPNY NRDILFRDEE GTGADRLMSK RCKEKLNVLA YSVMNEWPGI 

       190        200        210        220        230        240 
RLLVTESWDE DYHHGQESLH YEGRAVTIAT SDRDQSKYGM LARLAVEAGF DWVSYVSRRH 

       250        260        270        280        290        300 
IYCSVKSDSS ISSHVHGCFT PESTALLESG VRKPLGELSI GDRVLSMTAN GQAVYSEVIL 

       310        320        330        340        350        360 
FMDRNLEQMQ NFVQLHTDGG AVLTVTPAHL VSVWQPESQK LTFVFADRIE EKNQVLVRDV 

       370        380        390        400        410        420 
ETGELRPQRV VKVGSVRSKG VVAPLTREGT IVVNSVAASC YAVINSQSLA HWGLAPMRLL 

       430        440        450        460        470 
STLEAWLPAK EQLHSSPKVV SSAQQQNGIH WYANALYKVK DYVLPQSWRH D 

« Hide

Isoform Short [UniParc].

Checksum: C19D4D9EF4367D47
Show »

FASTA19221,323

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA46400.
RefSeqNP_001034065.1. NM_001038976.1. [Q02936-1]
UniGeneDm.2371.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AT0X-ray1.90A258-402[»]
2IBGX-ray2.20E/F/G/H99-248[»]
ProteinModelPortalQ02936.
SMRQ02936. Positions 100-248, 258-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67682. 37 interactions.
DIPDIP-51313N.
IntActQ02936. 2 interactions.
STRING7227.FBpp0099945.

Protein family/group databases

MEROPSC46.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0100506; FBpp0099945; FBgn0004644. [Q02936-1]
GeneID42737.
KEGGdme:Dmel_CG4637.
UCSCCG4637-RA. d. melanogaster. [Q02936-1]

Organism-specific databases

CTD42737.
FlyBaseFBgn0004644. hh.

Phylogenomic databases

eggNOGNOG250647.
GeneTreeENSGT00390000001117.
InParanoidQ02936.
KOK06224.
OMAHSCGPGR.
OrthoDBEOG779NZ5.
PhylomeDBQ02936.

Enzyme and pathway databases

SignaLinkQ02936.

Gene expression databases

BgeeQ02936.

Family and domain databases

Gene3D2.170.16.10. 1 hit.
3.30.1380.10. 1 hit.
InterProIPR001657. 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]
PfamPF01085. HH_signal. 1 hit.
PF01079. Hint. 1 hit.
[Graphical view]
PIRSFPIRSF009400. Peptidase_C46. 1 hit.
PRINTSPR00632. SONICHHOG.
SMARTSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMSSF51294. SSF51294. 1 hit.
SSF55166. SSF55166. 1 hit.
PROSITEPS50817. INTEIN_N_TER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02936.
GenomeRNAi42737.
NextBio830301.
PMAP-CutDBQ02936.
PROQ02936.

Entry information

Entry nameHH_DROME
AccessionPrimary (citable) accession number: Q02936
Secondary accession number(s): A4V396, Q9VCQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase