ID   A0A7K9X6B4_9GRUI        Unreviewed;       425 AA.
AC   A0A7K9X6B4;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   14-DEC-2022, entry version 8.
DE   RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
DE   Flags: Fragment;
GN   Name=Shh {ECO:0000313|EMBL:NXI92852.1};
GN   ORFNames=PSOCRE_R04203 {ECO:0000313|EMBL:NXI92852.1};
OS   Psophia crepitans (common trumpeter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Psophiidae; Psophia.
OX   NCBI_TaxID=54359 {ECO:0000313|EMBL:NXI92852.1, ECO:0000313|Proteomes:UP000587472};
RN   [1] {ECO:0000313|EMBL:NXI92852.1, ECO:0000313|Proteomes:UP000587472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-001-60 {ECO:0000313|EMBL:NXI92852.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXI92852.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-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=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: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Endoplasmic reticulum
CC       membrane {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004394}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
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:NXI92852.1}.
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DR   EMBL; VWZZ01002220; NXI92852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7K9X6B4; -.
DR   Proteomes; UP000587472; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
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:0007267; P:cell-cell signaling; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
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; 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   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000587472};
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..425
FT                   /note="Hedgehog protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029675991"
FT   DOMAIN          199..309
FT                   /note="HintN"
FT                   /evidence="ECO:0000259|SMART:SM00306"
FT   DOMAIN          312..357
FT                   /note="HintC"
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"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXI92852.1"
FT   NON_TER         425
FT                   /evidence="ECO:0000313|EMBL:NXI92852.1"
SQ   SEQUENCE   425 AA;  46572 MW;  AF755EAA68F51E94 CRC64;
     MDEMLLLTRI LLVGFICALL VSSGLTCGPG RGIGKRRHPK KLTPLAYKQF IPNVAEKTLG
     ASGRYEGKIT RNSERFKELT PNYNPDIIFK DEENTGADRL MTQRCKDKLN ALAISVMNQW
     PGVKLRVTEG WDEDGHHSEE ALHYEGRAVD ITTSDRDRSK YGMLARLAVE AGFDWVYYES
     KAHIHCSVKA ENSVAAKSGG CFPGSATVHL EQGGTKLVKD LSPGDRVLAA DAEGRLLYSD
     FLAFLDREDG SHKLFYVIET RQPRARLLLT AAHLVFVAPQ HNQSQEGTPS SRALFASHIR
     PGQRVYVLGE GGQQLLPAAV HSVSLREEAS GAYAPLTAQG TILINRVLAS CYAVIEEHSW
     AHWAFAPFRL LQGMLAALCP SAGGVPVGAP ADSGIHWYSR LLYRIGSWVL DSDSLHPLGM
     VVPSS
//