IHOG_DROSE
ID IHOG_DROSE Reviewed; 880 AA.
AC B4HY03;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE Flags: Precursor;
GN Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GM13730;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW51933.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW51933.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Mediates response to the active Hedgehog (Hh) protein signal
CC in embryos, functioning upstream or at the level of patched (ptc).
CC {ECO:0000250|UniProtKB:Q9VM64}.
CC -!- SUBUNIT: Homodimer. Heterotetramer; 2 iHog chains bind 2 hh chains when
CC facilitated by heparin, heparin is required to promote high-affinity
CC interactions between hh and iHog (By similarity).
CC {ECO:0000250|UniProtKB:Q9VM64}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:Q9VM64, ECO:0000255}.
CC -!- DOMAIN: The first fibronectin type-III domain mediates a specific
CC interaction with Hh protein, in vitro. The second fibronectin type-III
CC domain is additionally required for in vivo signaling activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9VM64}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IHOG family.
CC {ECO:0000255, ECO:0000305}.
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DR EMBL; CH480818; EDW51933.1; -; Genomic_DNA.
DR RefSeq; XP_002036010.1; XM_002035974.1.
DR AlphaFoldDB; B4HY03; -.
DR SMR; B4HY03; -.
DR STRING; 7238.B4HY03; -.
DR EnsemblMetazoa; FBtr0196715; FBpp0195207; FBgn0168661.
DR GeneID; 6611469; -.
DR KEGG; dse:6611469; -.
DR HOGENOM; CLU_004633_1_0_1; -.
DR OMA; CGLMEGK; -.
DR PhylomeDB; B4HY03; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:EnsemblMetazoa.
DR GO; GO:0035230; C:cytoneme; IEA:EnsemblMetazoa.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0015026; F:coreceptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0097108; F:hedgehog family protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005113; F:patched binding; IEA:EnsemblMetazoa.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0048749; P:compound eye development; IEA:EnsemblMetazoa.
DR GO; GO:0035017; P:cuticle pattern formation; IEA:EnsemblMetazoa.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:EnsemblMetazoa.
DR GO; GO:0071694; P:maintenance of protein location in extracellular region; IEA:EnsemblMetazoa.
DR GO; GO:0007379; P:segment specification; IEA:EnsemblMetazoa.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IEA:EnsemblMetazoa.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Heparin-binding; Immunoglobulin domain;
KW Membrane; Proteoglycan; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..880
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383619"
FT TOPO_DOM 21..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..142
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 132..232
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 252..340
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 346..432
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 461..567
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 575..670
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 426..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 501
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 503
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 541
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 173..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 367..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 880 AA; 97143 MW; 25C7F358D71D0E60 CRC64;
MTLLTSSLLL FSLLTSRLEA IPVLEKSPAH PAHSAHTAHP AHPSPGVRIL RAPESLVAPL
GDEVVLECET SLQPERFEWS HRSSRSPGAG FKYLRTGTAK ANVSQEAAIS RLRVLVRPDT
LGEYRCVGWF GPLVVTSTTA RLELASTSLV DAQESEAPLQ WRVSAGNSVL WSCGQQVQSN
PSASWSYFRN GVEIKPEFIG TNGNLFLSNV SSESSGIYSC QATNPASGER IQLPGSMQLQ
VTPEQRSQSK SPHLLKGQPS SQEITIREGS SLLLQCPGVG SPPPTVVWSS PDVVGAVKNK
RSKVFGHALE ISNTRVHDAG TYICFQDNGV RPALEHYIKV HVEQPPQIVR PPWADLTNEG
DRLKLECEAT GVPTPEIYWL LNGHSSVDDT EAELSNNFLI LHSVLKRHAG YVQCFARNRL
GEHSAGTLLQ VNPKQIQEPR ESGGTHRPKP NQGSKQKQMY PPTPPNVTRL SDESVMLRWM
VPRNGGLPIV IFKVQYRMVG KRKNWQTTND NIPYGKPKWN SELGKSFTAS VTDLKPEHTY
RFRILAVYSN NDNKESNTSA KFYLQPGAAL DPMPVPELLE IEEYSETAVV LHWSLASDAD
EHLITGYYAY YRPSSSAGEY FKATIEGAHA RSFKIAPLET ATMYEFKLQS FSAVSASEFS
ALKQGRTQRP KTSTTEEPTL QMGDRDTTTP SHNETFNMSP MLTGTIGGGA VLILLLISTC
LCVCRRRTSR SRGNNPNKPR MAELRDDFVP LGNCSPTKQR QRTRHIHITL NPLAQQQQQA
LEEKNDTDQD APYYQRPSSY DYDPTLRRMS SSSLRRSQRT LERAGGSNGS NNGNNNNLNQ
SAEAGAVENP GKPGRVLMKR PRLSSRSENL SSGSLNSVGV
