ID   IHOG_DROWI              Reviewed;         881 AA.
AC   B4N072;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE   Flags: Precursor;
GN   Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GK24246;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1] {ECO:0000312|EMBL:EDW78007.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW78007.1};
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; CH963920; EDW78007.1; -; Genomic_DNA.
DR   RefSeq; XP_002067021.2; XM_002066985.2.
DR   AlphaFoldDB; B4N072; -.
DR   SMR; B4N072; -.
DR   STRING; 7260.FBpp0253389; -.
DR   PRIDE; B4N072; -.
DR   EnsemblMetazoa; FBtr0254897; FBpp0253389; FBgn0226207.
DR   GeneID; 6644407; -.
DR   KEGG; dwi:6644407; -.
DR   eggNOG; ENOG502QSGM; Eukaryota.
DR   HOGENOM; CLU_004633_1_0_1; -.
DR   InParanoid; B4N072; -.
DR   OMA; CGLMEGK; -.
DR   OrthoDB; 102649at2759; -.
DR   PhylomeDB; B4N072; -.
DR   Proteomes; UP000007798; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..881
FT                   /note="Interference hedgehog"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000383622"
FT   TOPO_DOM        27..693
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        694..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        715..881
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..138
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          128..228
FT                   /note="Ig-like C2-type 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          242..330
FT                   /note="Ig-like C2-type 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          336..425
FT                   /note="Ig-like C2-type 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          450..558
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          566..661
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          655..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         486
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT   BINDING         492
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT   BINDING         494
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT   BINDING         532
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        167..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        266..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        358..407
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   881 AA;  97977 MW;  B619FC05789BBD9C CRC64;
     MSSSSSSLLL MMLLLLLLLL TSKLEAIPVL SSTSPSPGVR ILRSSESIVA PLDDEVVFEC
     ETSLPPERFE WSYSNTSSSS SAISSSFIYL SSVAGKVNIS HEYAISRLAI VVRPESLGEY
     RCVGWFGPLV VTSTIARLDL ASISLATKKE SHLNWRTAPG NSIIWPCGQQ VQANPLASWS
     FYKNGKEIQP LNHNGTLILN NISSESNGVY SCMATNTASG VRLPIPSSME LHVTKQEGSK
     SPYLLFGQPT RQSVTTREGQ RLLLVCPGVG SPPPIPVWSS PNVTAAVPNK RSKLLSYGLE
     INPVQVEDAG IYICYLDNGI RPPLELYINV RVEQAPVIVQ APWAGSLTNE SDRLQLECQA
     KGEPKPTIYW LLNGKRSHEV NQSQLLSNGR YLVLKKVLKE HAGYVQCFAR NHLGEHSAGT
     LLQVNPKLVN ETDLVVSRPQ RPKKLQIMVP PSAPNVTRLS DESVMLRWHV QRNEGLPIQF
     FKVQYRLINE GKRKMWQTTN ENIPYGKPKW NSALGKNFTA SVTNLKPQRT YRFRIMAVYS
     NNDNKESNTS AKFFLQRGSS LEPMPVPELV KIDEYSETAV VLHWRLSDDA DEQSITGYYA
     YYRPSSFAGE YSKATIEGAK ARSFHIGSLE VGTIYEFKLQ SFSADSASEF SALKQGRTQR
     SKLTTTEQPI QQKGGDRNVN TTPNHNETYS LNPLLTGTIG GGALLLLLLI AFSFCLCRRK
     NRNGGDGRNS QNKPRLAELR EDFLPLAGGG VPGSKQRQRS RHIHITLNPL DQQQQQPLDE
     KNTNTNLNSP HLEADPELVY FQRQQQNHPT TYDYDHGQRR LSSSSLRRSQ RTLERTPGSN
     NNLQQIGSET TTTGQRVILK RPRLSSRSEN LSSGSLNSVG V