Q02936 (HH_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Secreted › extracellular 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 component	Cell membrane Cytoplasm Membrane Nucleus Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Developmental protein Hydrolase Morphogen Protease Segmentation polarity protein
PTM	Autocatalytic cleavage Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Bolwig'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 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 epidermis development Traceable author statement PubMed 10837029. Source: FlyBase epithelial cell migration, open tracheal system Inferred from mutant phenotype PubMed 11290298. 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 germ cell attraction Traceable author statement PubMed 12814944. 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 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-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 morphogenesis of larval imaginal disc epithelium Inferred from mutant phenotype PubMed 16236766. 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 genetic interaction PubMed 8252628. Source: FlyBase protein autoprocessing Inferred from direct assay Ref.7. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW 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 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 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_component	endocytic vesicle Inferred from direct assay PubMed 18198278. Source: FlyBase endosome Inferred from direct assay PubMed 17484784. Source: FlyBase 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_function	cell surface binding Inferred from direct assay PubMed 16630821PubMed 17077139. Source: FlyBase morphogen 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 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – ?

Potential

Propeptide

? – 84

Potential

PRO_0000383048

Chain

85 – 471

387

Protein hedgehog

PRO_0000013202

Chain

85 – 257

173

Protein hedgehog N-product

PRO_0000013203

Chain

258 – 471

214

Protein hedgehog C-product

PRO_0000013204

Regions

Compositional bias

5 – 41

37

Ser-rich

Sites

Site

257 – 258

2

Cleavage; by autolysis

Site

303

1

Involved in cholesterol transfer

Site

326

1

Involved in auto-cleavage

Site

329

1

Essential for auto-cleavage

Amino acid modifications

Lipidation

85

1

N-palmitoyl cysteine Ref.9

Lipidation

257

1

Cholesterol glycine ester

Natural variations

Alternative sequence

161 – 192

32

RCKEK…WDEDY → VRKTLKHRKLVTKFVIHHWE SFAYRNHCDKVT in isoform Short.

VSP_002065

Alternative sequence

193 – 471

279

Missing in isoform Short.

VSP_002066

Experimental info

Mutagenesis

85

1

C → S: N-product is made but fails to undergo palmitoylation. Ref.8 Ref.9

Mutagenesis

303

1

D → A: No cholesterol transfer.

Mutagenesis

326

1

T → A: Greatly reduced autoprocessing activity.

Mutagenesis

329

1

H → A: No autoprocessing activity.

Sequence conflict

156

1

R → G in AAA28604. Ref.1

Sequence conflict

347

1

D → H in AAA28604. Ref.1

Sequence conflict

373

1

V → L in AAA28604. Ref.1

Sequence conflict

407

1

Q → P in Z11840. Ref.3

Secondary structure

1

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471

Helix Strand Turn

Details...

Beta strand

107 – 111

5

Turn

116 – 119

4

Helix

131 – 135

5

Beta strand

144 – 146

3

Helix

160 – 176

17

Beta strand

182 – 188

7

Helix

199 – 202

4

Beta strand

205 – 210

6

Helix

215 – 217

3

Helix

218 – 228

11

Beta strand

231 – 234

4

Beta strand

241 – 244

4

Beta strand

264 – 267

4

Beta strand

272 – 274

3

Helix

275 – 277

3

Beta strand

283 – 287

5

Beta strand

293 – 317

25

Beta strand

322 – 325

4

Beta strand

330 – 335

6

Turn

336 – 339

4

Beta strand

340 – 345

6

Helix

346 – 348

3

Beta strand

354 – 358

5

Turn

360 – 362

3

Beta strand

365 – 393

29

Beta strand

396 – 400

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (A) (B) [UniParc]. Last modified September 1, 2009. Version 4. Checksum: 8ECD796A92FE7043	FASTA	471	52,150
	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
	Isoform Short [UniParc]. Checksum: C19D4D9EF4367D47	FASTA	192	21,323
	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 VRKTLKHRKL VTKFVIHHWE 190 SFAYRNHCDK VT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

PIR

A46400.

RefSeq

NP_001034065.1. NM_001038976.1.
NP_524459.2. NM_079735.3.

UniGene

Dm.2371.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q02936.

SMR

Q02936. Positions 100-248, 258-402.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-51313N.

IntAct

Q02936. 2 interactions.

STRING

7227.FBpp0099945.

Protein family/group databases

MEROPS

C46.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0100506; FBpp0099945; FBgn0004644.

GeneID

42737.

KEGG

dme:Dmel_CG4637.

UCSC

CG4637-RA. d. melanogaster.

Organism-specific databases

CTD

42737.

FlyBase

FBgn0004644. hh.

Phylogenomic databases

eggNOG

NOG250647.

GeneTree

ENSGT00390000001117.

InParanoid

Q02936.

KO

K06224.

OMA

HSCGPGR.

OrthoDB

EOG46Q58K.

PhylomeDB

Q02936.

Gene expression databases

Bgee

Q02936.

GermOnline

CG4637. Drosophila melanogaster.

Family and domain databases

Gene3D

3.30.1380.10. 1 hit.

InterPro

IPR001657. Hedgehog.
IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR000320. Hedgehog_signaling_dom.
IPR001767. Hint_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR006141. Intein_splice_site.
[Graphical view]

Pfam

PF01085. HH_signal. 1 hit.
PF01079. Hint. 1 hit.
[Graphical view]

PIRSF

PIRSF009400. Peptidase_C46. 1 hit.

PRINTS

PR00632. SONICHHOG.

SMART

SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]

SUPFAM

SSF55166. Hedgehog_sig_N. 1 hit.

PROSITE

PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q02936.

GenomeRNAi

42737.

NextBio

830301.

PMAP-CutDB

Q02936.

Entry information

Entry name

HH_DROME

Accession

Primary (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:	April 3, 2013
This is version 151 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project