ID   A0A7K9X6B4_9GRUI        Unreviewed;       425 AA.
AC   A0A7K9X6B4;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 5.
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: Intercellular signal essential for a variety of patterning
CC       events during development. {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:NXI92852.1}.
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DR   EMBL; VWZZ01002220; NXI92852.1; -; Genomic_DNA.
DR   Proteomes; UP000587472; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF55166; SSF55166; 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   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   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   METAL           92
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           93
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           93
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           98
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           128
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           129
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           129
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           132
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           134
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           143
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           150
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT   METAL           185
FT                   /note="Zinc"
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
//