DHH_DANRE
ID DHH_DANRE Reviewed; 88 AA.
AC P79729; Q9YGU3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Desert hedgehog protein;
DE Short=DHH;
DE Flags: Fragment;
GN Name=dhh;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9831563; DOI=10.1126/science.282.5394.1711;
RA Amores A., Force A., Yan Y.-L., Joly L., Amemiya C., Fritz A., Ho R.K.,
RA Langeland J., Prince V.E., Wang Y.-L., Westerfield M., Ekker M.,
RA Postlethwait J.H.;
RT "Zebrafish hox clusters and vertebrate genome evolution.";
RL Science 282:1711-1714(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-71.
RC TISSUE=Muscle;
RX PubMed=8917540; DOI=10.1073/pnas.93.23.13036;
RA Zardoya R., Abouheif E., Meyer A.;
RT "Evolutionary analyses of hedgehog and Hoxd-10 genes in fish species
RT closely related to the zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13036-13041(1996).
CC -!- FUNCTION: Intercellular signal essential for a variety of patterning
CC events during development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}. Note=Desert hedgehog protein N-
CC product: Cell membrane; Lipid-anchor; Extracellular side. The N-
CC terminal peptide remains associated with the cell surface. Desert
CC hedgehog protein C-product: Secreted, extracellular space. The C-
CC terminal peptide diffuses from the cell. {ECO:0000250}.
CC -!- DOMAIN: The desert hedgehog protein N-product binds calcium and zinc
CC ions; this stabilizes the protein fold and is essential for protein-
CC protein interactions mediated by this domain. {ECO:0000250}.
CC -!- PTM: The C-terminal domain displays an autoproteolysis activity and a
CC cholesterol transferase activity. Both activities result in the
CC cleavage of the full-length protein and covalent attachment of a
CC cholesterol moiety to the C-terminal of the newly generated N-terminal
CC fragment (N-product). This covalent modification appears to play an
CC essential role in restricting the spatial distribution of the protein
CC activity to the cell surface. The N-product is the active species in
CC both local and long-range signaling, whereas the C-product has no
CC signaling activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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DR EMBL; AF071236; AAD15931.1; -; Genomic_DNA.
DR EMBL; U51388; AAB38613.1; -; Genomic_DNA.
DR AlphaFoldDB; P79729; -.
DR SMR; P79729; -.
DR STRING; 7955.ENSDARP00000053870; -.
DR PaxDb; P79729; -.
DR ZFIN; ZDB-GENE-990714-5; dhh.
DR eggNOG; KOG3638; Eukaryota.
DR InParanoid; P79729; -.
DR SignaLink; P79729; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005113; F:patched binding; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR001657; Hedgehog.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR000320; Hedgehog_signalling_dom.
DR Pfam; PF01085; HH_signal; 1.
DR PRINTS; PR00632; SONICHHOG.
DR SUPFAM; SSF55166; SSF55166; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Calcium; Cell membrane; Developmental protein;
KW Hydrolase; Membrane; Metal-binding; Protease; Reference proteome; Secreted;
KW Zinc.
FT CHAIN <1..>88
FT /note="Desert hedgehog protein"
FT /id="PRO_0000058750"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43323"
FT CONFLICT 17
FT /note="Q -> M (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="R -> K (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="A -> G (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..38
FT /note="HHPPG -> NHLED (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="TK -> RN (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="L -> M (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Q -> R (in Ref. 2; AAB38613)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 88
SQ SEQUENCE 88 AA; 10069 MW; E3D34A0C36677FA6 CRC64;
QRCKDCLYKL AIAVMNQWPG VRLRVTEAWD EDGHHPPGSL HYEGRAVDIT TSDRDTKKYG
LLAQLAVEAG FDWVHYESKY HVHCSVKA
