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Database: UniProt
Entry: A0A060XSJ4_ONCMY
LinkDB: A0A060XSJ4_ONCMY
Original site: A0A060XSJ4_ONCMY 
ID   A0A060XSJ4_ONCMY        Unreviewed;       421 AA.
AC   A0A060XSJ4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
GN   ORFNames=GSONMT00023889001 {ECO:0000313|EMBL:CDQ82237.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ82237.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ82237.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ82237.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSOMYP00000107778.1}
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   EMBL; FR905933; CDQ82237.1; -; Genomic_DNA.
DR   STRING; 8022.A0A060XSJ4; -.
DR   PaxDb; 8022-A0A060XSJ4; -.
DR   Ensembl; ENSOMYT00000117172.1; ENSOMYP00000107778.1; ENSOMYG00000053529.1.
DR   GeneTree; ENSGT00940000164444; -.
DR   OrthoDB; 197397at2759; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   Proteomes; UP000694395; Chromosome 7.
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: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   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:SF85; 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|RuleBase:RU280812};
KW   Golgi apparatus {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:UP000193380};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..421
FT                   /note="Hedgehog protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040664800"
FT   DOMAIN          196..310
FT                   /note="Hint"
FT                   /evidence="ECO:0000259|SMART:SM00306"
FT   DOMAIN          317..361
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="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         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            246
FT                   /note="Involved in cholesterol transfer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT   SITE            269
FT                   /note="Involved in auto-cleavage"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT   SITE            272
FT                   /note="Essential for auto-cleavage"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
SQ   SEQUENCE   421 AA;  45971 MW;  157DC0856232839F CRC64;
     MLLPRLVVCL AGCAVILSQV SEGCGPGRGY GKRRSPRKLA PLAYKQFSPN VAEKTLGASG
     RYEGKITRTS ERFKELTPNY NPDIIFKDEE NTGADRMMTQ RCKDKLNSLA ISVMNLWPGV
     RLRVTEGWDE DGHHSEESLH YEGRAVDITT SDRDRNKYAM LARLAVEAGF DWVYYESKAH
     VHCSVKSEHS VAAKSGGCFP GGAWVTLEDG GQRLIQDLQP GERVLASSGS DGSGELVYSE
     VLTFLDRDPA TRKEFYTIGT EGGVSLSLTA AHLLFVSKGN CSEGAEPTPG SMRTVYASDA
     RPGQCVLTTV SGEEGRKGVG HLSRISRVSV QEDKGVFAPL TRHGTLSVNG MVASCYAVVD
     RHDLAHWAFA PLRLLHRWTG SAGGHFGDTG VHWYSQLLYW IGSLLLDSGH FHPWGLADPG
     R
//
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