ID A0A5N3XNS8_MUNRE Unreviewed; 454 AA.
AC A0A5N3XNS8;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
GN ORFNames=FD755_012240 {ECO:0000313|EMBL:KAB0375597.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0375597.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0375597.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0375597.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0375597.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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=glycyl-L-cysteinyl-[protein] + cholesterol + 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:ARBA00048589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC Evidence={ECO:0000256|ARBA:ARBA00048589};
CC -!- SUBUNIT: Multimer. {ECO:0000256|ARBA:ARBA00034131}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB0375597.1}.
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DR EMBL; VCEB01000006; KAB0375597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N3XNS8; -.
DR Proteomes; UP000326062; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:TreeGrafter.
DR GO; GO:0005113; F:patched binding; IEA:TreeGrafter.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0048468; P:cell development; IEA:UniProtKB-ARBA.
DR GO; GO:0001708; P:cell fate specification; IEA:TreeGrafter.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:TreeGrafter.
DR GO; GO:0007389; P:pattern specification process; IEA:UniProtKB-ARBA.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:TreeGrafter.
DR GO; GO:0009888; P:tissue development; IEA:UniProtKB-ARBA.
DR GO; GO:0035295; P:tube development; IEA:UniProtKB-ARBA.
DR CDD; cd00081; Hint; 1.
DR FunFam; 2.170.16.10:FF:000001; Indian hedgehog; 1.
DR FunFam; 3.30.1380.10:FF:000001; Indian hedgehog; 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; IPR050387; Hedgehog_Signaling.
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|ARBA:ARBA00022824,
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000326062};
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..454
FT /note="Hedgehog protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024395248"
FT DOMAIN 196..318
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 323..368
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 454 AA; 48732 MW; 19655830E275163E CRC64;
MLLLARCLLV LLVSSLLMCS GLACGPGRGF GKRRNPKKLT PLAYKQFIPN VAEKTLGASG
RYEGKITRNS ERFKELTPNY NPDIIFKDEE NTGADRLMTQ RCKDKLNALA ISVMNQWPGV
KLRVTEGWDE DGHHSEESLH YEGRAVDITT SDRDRSKYGM LARLAVEAGF DWVYYESKAH
IHCSVKAENS VAAKSGGCFP GSATVHLEQG GTKLVKDLRP GDRVLAADDE GRLLYSDFLT
FLDRDRGAKK IFYAIETREP RERLLLTAAH LLFVAPHNGS AAGAPEGAAA AAAGGGAPGR
RALFASRVRP GQHVYVVAER GGARRLLPAA VHSVTLREET AGAYAPLTAH GTILINRVLA
SCYAVIEEHS WAHGAFAPYR LAHALLAALA PGRTDRGGAG DGGGGGRVPP PVPGAADAPG
AAGIHWYSEL LYQIGTWLLD SEALHPLGMA VKSS
//
