SHH_DANRE
ID SHH_DANRE Reviewed; 418 AA.
AC Q92008; O13170; O13171; O13208; O13209; O13245; O13246;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Sonic hedgehog protein {ECO:0000305};
DE Short=SHHA;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q62226};
DE AltName: Full=Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains {ECO:0000250|UniProtKB:Q62226};
DE Short=ShhNC {ECO:0000250|UniProtKB:Q62226};
DE AltName: Full=VHH-1;
DE Contains:
DE RecName: Full=Sonic hedgehog protein A N-product;
DE AltName: Full=Shh N-terminal processed signaling domains {ECO:0000250|UniProtKB:Q62226};
DE Short=ShhNp {ECO:0000250|UniProtKB:Q62226};
DE AltName: Full=Sonic hedgehog protein N-product;
DE Short=ShhN;
DE Flags: Precursor;
GN Name=shha; Synonyms=shh, vhh1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8124714; DOI=10.1016/0092-8674(94)90514-2;
RA Roelink H., Augsburger A., Heemskerk J., Korzh V., Norlin S.,
RA Ruiz i Altaba A., Tanabe Y., Placzek M., Edlund T., Jessell T.M., Dodd J.;
RT "Floor plate and motor neuron induction by vhh-1, a vertebrate homolog of
RT hedgehog expressed by the notochord.";
RL Cell 76:761-775(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC PROCESSING, AND AUTOCATALYTIC
RP CLEAVAGE.
RX PubMed=7583153; DOI=10.1016/s0960-9822(95)00185-0;
RA Ekker S.C., Ungar A.R., Greenstein P., von Kessler D.P., Porter J.A.,
RA Moon R.T., Beachy P.A.;
RT "Patterning activities of vertebrate hedgehog proteins in the developing
RT eye and brain.";
RL Curr. Biol. 5:944-955(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7579523;
RA Fietz M.J., Concordet J.-P., Barbosa R., Johnson R., Krauss S.,
RA McMahon A.P., Tabin C., Ingham P.W.;
RT "The hedgehog gene family in Drosophila and vertebrate development.";
RL Development Suppl. 120:43-51(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10207136; DOI=10.1242/dev.126.10.2103;
RA Muller F., Chang B., Albert S., Fischer N., Tora L., Strahle U.;
RT "Intronic enhancers control expression of zebrafish sonic hedgehog in floor
RT plate and notochord.";
RL Development 126:2103-2116(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-92 AND 113-170.
RC TISSUE=Muscle;
RX PubMed=8917540; DOI=10.1073/pnas.93.23.13036;
RA Zardoya R., Abouheif E., Meyer A.;
RT "Evolutionary analyses of hedgehog and Hoxd-10 genes in fish species
RT closely related to the zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13036-13041(1996).
CC -!- FUNCTION: [Sonic hedgehog protein]: The C-terminal part of the sonic
CC hedgehog protein precursor displays an autoproteolysis and a
CC cholesterol transferase activity (By similarity). Both activities
CC result in the cleavage of the full-length protein into two parts (ShhN
CC and ShhC) followed by the covalent attachment of a cholesterol moiety
CC to the C-terminal of the newly generated ShhN (By similarity). Both
CC activities occur in the reticulum endoplasmic (By similarity). Once
CC cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226,
CC ECO:0000269|PubMed:7583153}.
CC -!- FUNCTION: [Sonic hedgehog protein A N-product]: The dually lipidated
CC sonic hedgehog protein N-product (ShhNp) is a morphogen which is
CC essential for a variety of patterning events during development (By
CC similarity). Involved in dorso-ventral patterning of the brain and in
CC early patterning of the developing eyes (PubMed:7583153). Binds to the
CC patched (PTCH1) receptor, which functions in association with
CC smoothened (SMO), to activate the transcription of target genes (By
CC similarity). In the absence of SHH, PTCH1 represses the constitutive
CC signaling activity of SMO (By similarity).
CC {ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226,
CC ECO:0000269|PubMed:7583153}.
CC -!- CATALYTIC ACTIVITY: [Sonic hedgehog protein]:
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:0000250|UniProtKB:Q62226};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC Evidence={ECO:0000250|UniProtKB:Q62226};
CC -!- SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates HHAT-
CC mediated palmitoylation of the SHH N-terminus (By similarity).
CC Interacts with BOC and CDON (By similarity). Interacts with HHIP (By
CC similarity). Interacts with DISP1 via its cholesterol anchor (By
CC similarity). Interacts with SCUBE2 (By similarity).
CC {ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.
CC -!- SUBUNIT: [Sonic hedgehog protein A N-product]: Multimer.
CC {ECO:0000250|UniProtKB:Q15465}.
CC -!- SUBCELLULAR LOCATION: [Sonic hedgehog protein]: Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q15465}. Note=Co-localizes with HHAT in the ER
CC and Golgi membrane. {ECO:0000250|UniProtKB:Q15465}.
CC -!- SUBCELLULAR LOCATION: [Sonic hedgehog protein A N-product]: Cell
CC membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic hedgehog
CC protein N-product (ShhNp) is firmly tethered to the cell membrane where
CC it forms multimers (By similarity). Further solubilization and release
CC from the cell surface seem to be achieved through different mechanisms,
CC including the interaction with DISP1 and SCUBE2, movement by
CC lipoprotein particles, transport by cellular extensions called
CC cytonemes or by the proteolytic removal of both terminal lipidated
CC peptides. {ECO:0000250|UniProtKB:Q62226}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral midline of the neural tube
CC and brain. Also found in the notochord and in developing fin bud. In
CC the developing brain, expression occurs in domains that include a
CC discrete region in the floor of the diencephalon.
CC -!- DEVELOPMENTAL STAGE: First detectable in the inner cell layer of the
CC embryonic shield during gastrulation. By 9.5 hours of development,
CC expressed in a continuous band that extends from the tail to the head,
CC the anterior boundary of expression being positioned in the center of
CC the animal pole anterior to the presumptive midbrain.
CC -!- DOMAIN: [Sonic hedgehog protein A N-product]: Binds calcium and zinc
CC ions; this stabilizes the protein fold and is essential for protein-
CC protein interactions mediated by this domain.
CC {ECO:0000250|UniProtKB:Q62226}.
CC -!- DOMAIN: [Sonic hedgehog protein A N-product]: The Cardin-Weintraub (CW)
CC motif is required for heparan sulfate binding of the solubilized ShhNp
CC (By similarity). The N-terminal palmitoylated peptide is cleaved at the
CC Heparan sulfate-binding Cardin-Weintraub (CW) motif site (By
CC similarity). The cleavage reduced the interactions with heparan
CC sulfate. The cleavage is enhanced by SCUBE2 (By similarity).
CC {ECO:0000250|UniProtKB:Q62226}.
CC -!- PTM: [Sonic hedgehog protein]: The C-terminal domain displays an
CC autoproteolysis activity and a cholesterol transferase activity (By
CC similarity). Both activities result in the cleavage of the full-length
CC protein and covalent attachment of a cholesterol moiety to the C-
CC terminal of the newly generated N-terminal fragment (ShhN) (By
CC similarity). Cholesterylation is required for the sonic hedgehog
CC protein N-product targeting to lipid rafts and multimerization (By
CC similarity). ShhN is the active species in both local and long-range
CC signaling, whereas the C-product (ShhC) is degraded in the reticulum
CC endoplasmic (By similarity). {ECO:0000250|UniProtKB:Q62226,
CC ECO:0000269|PubMed:7583153}.
CC -!- PTM: [Sonic hedgehog protein A N-product]: N-palmitoylation by HHAT of
CC ShhN is required for sonic hedgehog protein N-product multimerization
CC and full activity (By similarity). It is a prerequisite for the
CC membrane-proximal positioning and the subsequent shedding of this N-
CC terminal peptide (By similarity). {ECO:0000250|UniProtKB:Q62226}.
CC -!- PTM: [Sonic hedgehog protein A N-product]: The lipidated N- and C-
CC terminal peptides of ShhNp can be cleaved (shedding) (By similarity).
CC The N-terminal palmitoylated peptide is cleaved at the Cardin-Weintraub
CC (CW) motif site (By similarity). The cleavage reduced the interactions
CC with heparan sulfate (By similarity). The cleavage is enhanced by
CC SCUBE2 (By similarity). {ECO:0000250|UniProtKB:Q62226}.
CC -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
CC -!- CAUTION: The several steps and mechanisms that permit controlled Shh
CC dispersion and gradient formation remain controversial. The Shh C-
CC terminal domain displays an autoproteolysis activity and a cholesterol
CC transferase activity resulting in the cleavage and covalent attachment
CC of a cholesterol moiety to the C-terminal of the newly generated N-
CC terminal fragment (ShhN). The protein is further modified by covalent
CC addition of palmitate at the N-terminal of ShhN, resulting to the dual-
CC lipidated Shh (ShhNp). ShhNp is firmly tethered to the cell membrane
CC where it forms multimers. Further solubilization and release from the
CC cell surface seem to be achieved through different mechanisms,
CC including the interaction with DISP1 and SCUBE2, movement by
CC lipoprotein particles, transport by cellular extensions called
CC cytonemes or by proteolytic removal of both terminal lipidated
CC peptides. Once released, the fully processed Shh can signal within
CC embryonic tissues both at short and long-range.
CC {ECO:0000250|UniProtKB:Q62226}.
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DR EMBL; L27585; AAA20998.1; -; mRNA.
DR EMBL; U30711; AAC59742.1; -; mRNA.
DR EMBL; Z35669; CAA84738.1; -; mRNA.
DR EMBL; AF124382; AAD47913.1; -; Genomic_DNA.
DR EMBL; U51339; AAB38570.1; -; Genomic_DNA.
DR EMBL; U51351; AAB38575.1; -; Genomic_DNA.
DR EMBL; U51357; AAB38588.1; -; Genomic_DNA.
DR EMBL; U51370; AAB38593.1; -; Genomic_DNA.
DR PIR; A53193; A53193.
DR RefSeq; NP_571138.1; NM_131063.3.
DR AlphaFoldDB; Q92008; -.
DR SMR; Q92008; -.
DR STRING; 7955.ENSDARP00000125090; -.
DR MEROPS; C46.005; -.
DR PaxDb; Q92008; -.
DR Ensembl; ENSDART00000149395; ENSDARP00000125090; ENSDARG00000068567.
DR Ensembl; ENSDART00000189635; ENSDARP00000145101; ENSDARG00000111447.
DR GeneID; 30269; -.
DR KEGG; dre:30269; -.
DR CTD; 30269; -.
DR ZFIN; ZDB-GENE-980526-166; shha.
DR eggNOG; KOG3638; Eukaryota.
DR GeneTree; ENSGT00940000159119; -.
DR HOGENOM; CLU_034686_0_0_1; -.
DR InParanoid; Q92008; -.
DR OMA; LDSHSIH; -.
DR OrthoDB; 1169356at2759; -.
DR PhylomeDB; Q92008; -.
DR TreeFam; TF106458; -.
DR Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-DRE-5362798; Release of Hh-Np from the secreting cell.
DR Reactome; R-DRE-5632681; Ligand-receptor interactions.
DR Reactome; R-DRE-5635838; Activation of SMO.
DR SignaLink; Q92008; -.
DR PRO; PR:Q92008; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000068567; Expressed in tail bud paraxial mesoderm and 13 other tissues.
DR ExpressionAtlas; Q92008; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005113; F:patched binding; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0021984; P:adenohypophysis development; IDA:ZFIN.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0008015; P:blood circulation; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0043010; P:camera-type eye development; IDA:ZFIN.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:ZFIN.
DR GO; GO:0035143; P:caudal fin morphogenesis; IMP:ZFIN.
DR GO; GO:0001708; P:cell fate specification; IMP:ZFIN.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IDA:ZFIN.
DR GO; GO:0021536; P:diencephalon development; IGI:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:ZFIN.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:ZFIN.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0060956; P:endocardial cell differentiation; IGI:ZFIN.
DR GO; GO:0031018; P:endocrine pancreas development; IDA:ZFIN.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:ZFIN.
DR GO; GO:0033504; P:floor plate development; IMP:ZFIN.
DR GO; GO:0021508; P:floor plate formation; IMP:ZFIN.
DR GO; GO:0030900; P:forebrain development; IMP:ZFIN.
DR GO; GO:0010001; P:glial cell differentiation; IMP:ZFIN.
DR GO; GO:0042063; P:gliogenesis; IMP:ZFIN.
DR GO; GO:0032835; P:glomerulus development; IMP:ZFIN.
DR GO; GO:0021986; P:habenula development; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IDA:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
DR GO; GO:0048839; P:inner ear development; IGI:ZFIN.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:ZFIN.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:ZFIN.
DR GO; GO:0007517; P:muscle organ development; IMP:ZFIN.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ZFIN.
DR GO; GO:0007399; P:nervous system development; IMP:ZFIN.
DR GO; GO:0001839; P:neural plate morphogenesis; IMP:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IMP:ZFIN.
DR GO; GO:0048663; P:neuron fate commitment; IGI:ZFIN.
DR GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:ZFIN.
DR GO; GO:0070444; P:oligodendrocyte progenitor proliferation; IMP:ZFIN.
DR GO; GO:0031016; P:pancreas development; IDA:ZFIN.
DR GO; GO:0033339; P:pectoral fin development; IMP:ZFIN.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:ZFIN.
DR GO; GO:0048618; P:post-embryonic foregut morphogenesis; IMP:ZFIN.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IDA:ZFIN.
DR GO; GO:1905178; P:regulation of cardiac muscle tissue regeneration; IMP:ZFIN.
DR GO; GO:0061035; P:regulation of cartilage development; IGI:ZFIN.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IMP:ZFIN.
DR GO; GO:0048741; P:skeletal muscle fiber development; IDA:ZFIN.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IMP:ZFIN.
DR GO; GO:0055002; P:striated muscle cell development; IMP:ZFIN.
DR GO; GO:0048795; P:swim bladder morphogenesis; IMP:ZFIN.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Cell membrane; Developmental protein;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT CHAIN 24..418
FT /note="Sonic hedgehog protein"
FT /id="PRO_0000013226"
FT CHAIN 24..197
FT /note="Sonic hedgehog protein A N-product"
FT /id="PRO_0000013227"
FT MOTIF 32..38
FT /note="Cardin-Weintraub"
FT /evidence="ECO:0000250|UniProtKB:Q62226"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15465"
FT SITE 197..198
FT /note="Cleavage; by autolysis"
FT SITE 243
FT /note="Involved in cholesterol transfer"
FT /evidence="ECO:0000250"
FT SITE 267
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000250"
FT SITE 270
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 197
FT /note="Cholesterol glycine ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 418 AA; 46403 MW; CF000AFFFD2F5795 CRC64;
MRLLTRVLLV SLLTLSLVVS GLACGPGRGY GRRRHPKKLT PLAYKQFIPN VAEKTLGASG
RYEGKITRNS ERFKELTPNY NPDIIFKDEE NTGADRLMTQ RCKDKLNSLA ISVMNHWPGV
KLRVTEGWDE DGHHFEESLH YEGRAVDITT SDRDKSKYGT LSRLAVEAGF DWVYYESKAH
IHCSVKAENS VAAKSGGCFP GSALVSLQDG GQKAVKDLNP GDKVLAADSA GNLVFSDFIM
FTDRDSTTRR VFYVIETQEP VEKITLTAAH LLFVLDNSTE DLHTMTAAYA SSVRAGQKVM
VVDDSGQLKS VIVQRIYTEE QRGSFAPVTA HGTIVVDRIL ASCYAVIEDQ GLAHLAFAPA
RLYYYVSSFL FPQNSSSRSN ATLQQEGVHW YSRLLYQMGT WLLDSNMLHP LGMSVNSS
