IHOG_DROAN
ID IHOG_DROAN Reviewed; 880 AA.
AC B3MKS0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE Flags: Precursor;
GN Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GF14467;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV31601.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV31601.1};
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; CH902620; EDV31601.1; -; Genomic_DNA.
DR RefSeq; XP_001962380.1; XM_001962344.2.
DR AlphaFoldDB; B3MKS0; -.
DR SMR; B3MKS0; -.
DR STRING; 7217.FBpp0117659; -.
DR EnsemblMetazoa; FBtr0119167; FBpp0117659; FBgn0091494.
DR GeneID; 6497291; -.
DR KEGG; dan:6497291; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; B3MKS0; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; B3MKS0; -.
DR Proteomes; UP000007801; 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 InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00047; ig; 1.
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_0000383612"
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 37..142
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 154..235
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 251..339
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 345..432
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 462..570
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 578..673
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 435..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..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 498
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 504
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 506
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 544
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 275..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 366..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 880 AA; 96924 MW; 99D948EFC5D48A3D CRC64;
MPSIVSSLLL VVLLTSPLGA IPVLYPSPPP LPAYPSPGVR ILRPPESLVA PLGDEVVLEC
ETSLPPERFE WSYRRWTPNG TAVNGSPGAG FKYLKTSSMK ANVTQEAAIS RLKVLVRQDT
LGEYRCNGWF GPLLVTSTTA RLELATTSVK SQEPVTSLQW QITNGNSVLW PCGQPVRSNP
AASWTFYRNG VELGPEYSGT GGNLFLRNVS VDSSGSYSCQ ATNPASGERI KSTSSMELQV
VPSRGSQVKA PYLLPGQPGS QTVTAIEGGT LLLLCPGVGS PPPTAVWSSP DIVGAVNNKR
TRVLAHALEI SNVQIGDSGT YICYLDNGVR PPLEHFIQVK VEQPPQIVRP PWIDMVNEGE
RVQLECEATG VPTPEIYWLL NGKSSIYDTE AEQLPNGHLV LHSVLKRHAG YVQCFARNSL
GEHSAGMSLQ VTPKPIHSES TQQSDHNHSK ANRGRRPAQM IPPSAPNVTR LSDESVMLRW
MVPRNDGLAI LFFKVQYRTV GEGKRKNWQT TNENIPYGRP EWNSEMGKSF TASVTDLKPQ
RTYRFRIMAV YTNNDNKESN MSAKFFLQPG AALDPMPVPE MLEIDEYSET AVVLHWRLDS
DADEQLITGY YAYYRPSSSA GEYFKATIEG ASSRSFTIGN LEAGTVYEFK LQSFSAESAS
EFSALKQGRT QRPMVSTTEE ATLQTGVRDT TTPSHNETFS MSPIVTGTIG GGAVLILFVV
TTCLCMWRRR NSRAHRGGGQ NKPRMAELRE DFVPLDSCSP TKQRQRSRHI HITLNPLAQQ
QQQALDEKND AEHDMTYFQR QPTYDYDPGL RRMSSSSLRR SQRTLERAGS SNGNNNNLNQ
SADMGPVDNP GKPGRVLMKR PRLSSRSENL SSGSLNSVGV
