ID A0A9D3XCQ6_9SAUR Unreviewed; 428 AA.
AC A0A9D3XCQ6;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 02-APR-2025, entry version 11.
DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
GN ORFNames=KIL84_010908 {ECO:0000313|EMBL:KAH1177206.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1177206.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1177206.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1177206.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1177206.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) 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:KAH1177206.1}.
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DR EMBL; JAHDVG010000474; KAH1177206.1; -; Genomic_DNA.
DR OrthoDB; 5212at2759; -.
DR Proteomes; UP000827986; Unassembled WGS sequence.
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.
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:UP000827986};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..428
FT /note="Hedgehog protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039522554"
FT DOMAIN 199..313
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 316..361
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 128
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 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT SITE 200..201
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 246
FT /note="Involved in cholesterol transfer"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 270
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 273
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
SQ SEQUENCE 428 AA; 47251 MW; 5556540A452F1302 CRC64;
MDEMLLLTRI LLVGFICVLL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG
ASGRYEGKIS RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW
PGVKLRVTEG WDEDGHHSEE SLHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES
KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EQGGTKRVRD LSPGDRVLAA DAQGRLLYSD
FLAFLDREQG APKLFYVIET RQPRARLLLT AAHLLFVAPP RNHSQPEPEP EPARRRALFA
SRVRPGQRVY VLGEGGRRLL PAAVHSVSLR EEASGAYAPL TAQGTILINR VLASCYAVIE
EHSWAHWAFA PLRLAHALLA VLSPGAGLPE AEPAPPGLHW YSRLLYRLGS WVLDSDSLHP
LGMAVQAS
//
