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HH_DROER
ID   HH_DROER                Reviewed;         465 AA.
AC   B3P7F8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Protein hedgehog {ECO:0000250|UniProtKB:Q02936};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q62226};
DE   Contains:
DE     RecName: Full=Protein hedgehog N-product {ECO:0000250|UniProtKB:Q02936};
DE   Flags: Precursor;
GN   Name=hh {ECO:0000250|UniProtKB:Q02936}; ORFNames=GG12458;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000312|EMBL:EDV54047.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV54047.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog
CC       protein precursor displays an autoproteolysis activity that results in
CC       the cleavage of the full-length protein into two parts (N-product and
CC       C-product) (By similarity). In addition, the C-terminal part displays a
CC       cholesterol transferase activity that results by the covalent
CC       attachment of a cholesterol moiety to the C-terminal of the newly
CC       generated N-product (By similarity). Once cleaved, the C-product has no
CC       signaling activity and diffuses from the cell (By similarity).
CC       {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.
CC   -!- FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog
CC       protein N-product is a morphogen which is essential for a variety of
CC       patterning events during development. Establishes the anterior-
CC       posterior axis of the embryonic segments and patterns the larval
CC       imaginal disks. Binds to the patched (ptc) receptor, which functions in
CC       association with smoothened (smo), to activate the transcription of
CC       target genes wingless (wg), decapentaplegic (dpp) and ptc. In the
CC       absence of hh, ptc represses the constitutive signaling activity of smo
CC       through fused (fu). Essential component of a signaling pathway which
CC       regulates the Duox-dependent gut immune response to bacterial uracil;
CC       required to activate Cad99C-dependent endosome formation, norpA-
CC       dependent Ca2+ mobilization and p38 MAPK, which are essential steps in
CC       the Duox-dependent production of reactive oxygen species (ROS) in
CC       response to intestinal bacterial infection. During photoreceptor
CC       differentiation, it up-regulates transcription of Ubr3, which in turn
CC       promotes the hh-signaling pathway by mediating the ubiquitination and
CC       degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- CATALYTIC ACTIVITY: [Protein hedgehog]:
CC       Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-
CC         C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-
CC         [protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-
CC         COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135,
CC         ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC         Evidence={ECO:0000250|UniProtKB:Q62226};
CC   -!- SUBUNIT: Interacts with shf. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10
CC       and then at stage 11 shifts to the cytoplasm. Also secreted in either
CC       cleaved or uncleaved form to mediate signaling to other cells.
CC       {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane
CC       {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains
CC       associated with the cell surface. Heparan sulfate proteoglycans of the
CC       extracellular matrix play an essential role in diffusion. Lipophorin is
CC       required for diffusion, probably by acting as vehicle for its movement,
CC       explaining how it can spread over long distances despite its
CC       lipidation. {ECO:0000250|UniProtKB:Q02936}.
CC   -!- PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein
CC       precursor displays an autoproteolysis activity that results in the
CC       cleavage of the full-length protein into two parts (N-product and C-
CC       product) (By similarity). In addition, the C-terminal part displays a
CC       cholesterol transferase activity that results by the covalent
CC       attachment of a cholesterol moiety to the C-terminal of the newly
CC       generated N-product (By similarity). The N-product is the active
CC       species in both local and long-range signaling, whereas the C-product
CC       has no signaling activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465,
CC       ECO:0000250|UniProtKB:Q62226}.
CC   -!- PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-
CC       product targeting to lipid rafts and multimerization.
CC       {ECO:0000250|UniProtKB:Q62226}.
CC   -!- PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the
CC       hedgehog N-product, within the secretory pathway, is required for the
CC       embryonic and larval patterning activities of the hedgehog signal.
CC       {ECO:0000250|UniProtKB:Q02936}.
CC   -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000255}.
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DR   EMBL; CH954182; EDV54047.1; -; Genomic_DNA.
DR   RefSeq; XP_001982177.1; XM_001982141.2.
DR   AlphaFoldDB; B3P7F8; -.
DR   BMRB; B3P7F8; -.
DR   SMR; B3P7F8; -.
DR   STRING; 7220.FBpp0131004; -.
DR   MEROPS; C46.001; -.
DR   PRIDE; B3P7F8; -.
DR   EnsemblMetazoa; FBtr0132512; FBpp0131004; FBgn0104746.
DR   GeneID; 6554619; -.
DR   KEGG; der:6554619; -.
DR   eggNOG; KOG3638; Eukaryota.
DR   HOGENOM; CLU_034686_0_0_1; -.
DR   OMA; APAVRGC; -.
DR   OrthoDB; 1169356at2759; -.
DR   PhylomeDB; B3P7F8; -.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:EnsemblMetazoa.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblMetazoa.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016015; F:morphogen activity; IEA:UniProtKB-KW.
DR   GO; GO:0005113; F:patched binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0001746; P:Bolwig's organ morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0035231; P:cytoneme assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0007427; P:epithelial cell migration, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0035224; P:genital disc anterior/posterior pattern formation; IEA:EnsemblMetazoa.
DR   GO; GO:0008347; P:glial cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007506; P:gonadal mesoderm development; IEA:EnsemblMetazoa.
DR   GO; GO:0060914; P:heart formation; IEA:EnsemblMetazoa.
DR   GO; GO:0007442; P:hindgut morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0035217; P:labial disc development; IEA:EnsemblMetazoa.
DR   GO; GO:0016335; P:morphogenesis of larval imaginal disc epithelium; IEA:EnsemblMetazoa.
DR   GO; GO:0002385; P:mucosal immune response; IEA:EnsemblMetazoa.
DR   GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; IEA:EnsemblMetazoa.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:EnsemblMetazoa.
DR   GO; GO:0007280; P:pole cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:EnsemblMetazoa.
DR   GO; GO:0007458; P:progression of morphogenetic furrow involved in compound eye morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:EnsemblMetazoa.
DR   GO; GO:2000495; P:regulation of cell proliferation involved in compound eye morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:2000274; P:regulation of epithelial cell migration, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:0007367; P:segment polarity determination; ISS:UniProtKB.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0035154; P:terminal cell fate specification, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0007418; P:ventral midline development; IEA:EnsemblMetazoa.
DR   GO; GO:0035222; P:wing disc pattern formation; IEA:EnsemblMetazoa.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR001657; Hedgehog.
DR   InterPro; IPR001767; Hedgehog_Hint.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR000320; Hedgehog_signalling_dom.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR006141; Intein_N.
DR   Pfam; PF01085; HH_signal; 1.
DR   Pfam; PF01079; Hint; 1.
DR   PIRSF; PIRSF009400; Peptidase_C46; 1.
DR   PRINTS; PR00632; SONICHHOG.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Calcium; Cell membrane; Cytoplasm;
KW   Developmental protein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Morphogen; Nucleus; Palmitate; Protease; Segmentation polarity protein;
KW   Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..78
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000383054"
FT   CHAIN           79..465
FT                   /note="Protein hedgehog"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT                   /id="PRO_0000383055"
FT   CHAIN           79..251
FT                   /note="Protein hedgehog N-product"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT                   /id="PRO_0000383056"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         144
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         144
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   BINDING         185
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15465"
FT   SITE            251..252
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            297
FT                   /note="Involved in cholesterol transfer"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            320
FT                   /note="Involved in auto-cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   SITE            323
FT                   /note="Essential for auto-cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   LIPID           79
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
FT   LIPID           251
FT                   /note="Cholesterol glycine ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q02936"
SQ   SEQUENCE   465 AA;  51569 MW;  DE0AEEFA4E52362D CRC64;
     MDNTSSVPWA SAASVTCLSL DAKCHSSSAK SAASSISASP ETQAMRHIAH TQRCLSRLTS
     LVALLLIVLP MTFSPAHSCG PGRGLGRHRA RNLYPLVLKQ TIPNLSEYTN SASGPLEGVI
     RRDSPKFKDL VPNYNRDILF RDEEGTGADR LMSKRCREKL NLLAYSVMNE WPGIRLLVTE
     SWDEDYHHGQ ESLHYEGRAV TIATSDRDQS KYGMLARLAV EAGFDWVSYV SRRHIYCSVK
     SDSSISSHVH GCFTPESTAL LENGVRKPLG ELSIGDRVLS MTANGQAVYS EVILFMDRNL
     EQMQNFVQLH TDGEAVLTVT PAHLVSVWQA ESQKLTFVFA DRVEEKNQVL VRDVETGELR
     PQRVVKVGSV RSKGVVAPLT REGTIVVNSV AASCYAVINS QSLAHWGLAP MRLLSTLEAW
     LPAKEQLHSS PKVVTTAEQQ NGIHWYANAL YKVKDYVLPQ SWRHD
 
 
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