ID A0A3B4CS27_PYGNA Unreviewed; 433 AA.
AC A0A3B4CS27;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000013314.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000013314.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU280812}.
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). In addition, the C-terminal part displays a cholesterol
CC transferase activity that results by the covalent attachment of a
CC cholesterol moiety to the C-terminal of the newly generated N-product.
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00034065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC Evidence={ECO:0000256|ARBA:ARBA00034065};
CC -!- SUBUNIT: Multimer. {ECO:0000256|ARBA:ARBA00034131}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SUBCELLULAR LOCATION: [Sonic hedgehog protein]: Endoplasmic reticulum
CC membrane {ECO:0000256|RuleBase:RU280812}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane
CC {ECO:0000256|RuleBase:RU280812}; Lipid-anchor
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- SIMILARITY: Belongs to the hedgehog family.
CC {ECO:0000256|ARBA:ARBA00010649, ECO:0000256|RuleBase:RU280812}.
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DR RefSeq; XP_017567205.1; XM_017711716.1.
DR AlphaFoldDB; A0A3B4CS27; -.
DR STRING; 42514.ENSPNAP00000013314; -.
DR Ensembl; ENSPNAT00000036873.1; ENSPNAP00000013314.1; ENSPNAG00000019147.1.
DR GeneID; 108435708; -.
DR CTD; 30444; -.
DR GeneTree; ENSGT00940000159119; -.
DR OMA; PRARRQF; -.
DR OrthoDB; 197397at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0060956; P:endocardial cell differentiation; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0042063; P:gliogenesis; IEA:Ensembl.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0048663; P:neuron fate commitment; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:UniProt.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProt.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0055002; P:striated muscle cell development; IEA:Ensembl.
DR GO; GO:0035295; P:tube development; IEA:UniProt.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 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 PANTHER; PTHR11889; HEDGEHOG; 1.
DR PANTHER; PTHR11889:SF36; SONIC HEDGEHOG PROTEIN; 1.
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; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU280812};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR009400-2};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU280812};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU280812};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU280812};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU280812};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU280812};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280812};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009400-2};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR009400-2}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..433
FT /note="Hedgehog protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017205485"
FT DOMAIN 196..304
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 310..356
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT SITE 197..198
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 243
FT /note="Involved in cholesterol transfer"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 267
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 270
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
SQ SEQUENCE 433 AA; 48555 MW; 291F1CE76C9BA685 CRC64;
MLLLRRIALA SLLCLFLTSC GLACGPGRGY GKRRHPKKLT PLAYKQFIPN VAEKTLGASG
KYEGKITRDS ERFKELTPNY NPDIIFKDEE NTNADRLMTQ RCKDKLNSLA ISVMNQWPGV
KLRVTEGWDE DGNHLEESLH YEGRAVDITT SDRDKSKYGM LSRLAVEAGF DWVYYESKAH
IHCSVKAENS VAVKSGGCFP GSATVQLEDG RTKLVRDLRE GDRVLAADEQ GRAAFSDFIM
FMDREPRARR QFIVIETAAP ARRLTLTAAH LVLVRNGNSS GSSPLMSARF ASSVRPGHEV
FVSEEKEQED GRLRGARVTR VRTVELEREG AYAPVTAHGT VVVDRVLASC YAAVEQHRWA
HWALAPARLS HALAAWMRPY WQRAAKNTTV TEEEGRERGM HWYARALLRV GTWLLHRDSF
HPLGLADTET SAS
//
