ID A0A267GU65_9PLAT Unreviewed; 441 AA.
AC A0A267GU65;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
GN ORFNames=BOX15_Mlig003939g1 {ECO:0000313|EMBL:PAA88839.1},
GN BOX15_Mlig003939g2 {ECO:0000313|EMBL:PAA83033.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA88839.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA88839.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA88839.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA88839.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {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}.
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:PAA88839.1}.
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DR EMBL; NIVC01000436; PAA83033.1; -; Genomic_DNA.
DR EMBL; NIVC01000173; PAA88839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GU65; -.
DR STRING; 282301.A0A267GU65; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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:0016540; P:protein autoprocessing; IEA:InterPro.
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 PANTHER; PTHR11889; HEDGEHOG; 1.
DR PANTHER; PTHR11889:SF31; PROTEIN HEDGEHOG; 1.
DR Pfam; PF01085; HH_signal; 1.
DR Pfam; PF01079; Hint; 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.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU280812}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU280812};
KW Developmental protein {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 Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..441
FT /note="Hedgehog protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011916216"
FT DOMAIN 220..335
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 336..380
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
SQ SEQUENCE 441 AA; 49718 MW; 609D7060F5758FF8 CRC64;
MPNQQSVFKP LHPHLLLLLI LTLLLSGQPQ PVNACFSQSH LYQPRESSNR QRSSHSFAFG
EYQPKTSELA VQASGPEGAP VRQSRHLLRS RSDLLEFNGR RRSRYMTRRC KEKLEQLALL
VRNQWNGHVR IRVHHAWMPK HDAYWDSQVG HRGLESLHFS GRAVDMSLLK LKPNLNYRDV
TLGRLAQLAY YQAYFDYCKV LKDTVHCSVK SDDPMDSDWL ACFPSKATVV KRHHGNSGNH
NNSNNAVVAI DTLTPGDEIL TLDELTGKQV FTRVLGYHHK LGDSEATYLK IQLANGHQLE
VSPNHLVFST SATSLKIRPT YAADLSIGDR LMTPQSSDGG WTGVVKISVR HRRGRYAPMT
SAGHLLVNGV WVSSYAHTRH QAAAHVLFAP LRWLDFLCSS GGRFCNSMTS DAYDRDGVHW
YSGWLHRAAQ LMAPGSVLFP N
//
