IHOG_DROGR
ID IHOG_DROGR Reviewed; 888 AA.
AC B4JEF2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE Flags: Precursor;
GN Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GH11362;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDW03672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDW03672.1};
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; CH916368; EDW03672.1; -; Genomic_DNA.
DR RefSeq; XP_001988805.1; XM_001988769.1.
DR AlphaFoldDB; B4JEF2; -.
DR SMR; B4JEF2; -.
DR STRING; 7222.FBpp0145268; -.
DR EnsemblMetazoa; FBtr0146776; FBpp0145268; FBgn0118842.
DR EnsemblMetazoa; FBtr0458063; FBpp0408563; FBgn0118842.
DR GeneID; 6561666; -.
DR KEGG; dgr:6561666; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; B4JEF2; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; B4JEF2; -.
DR Proteomes; UP000001070; 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; -; 6.
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 SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..888
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383614"
FT TOPO_DOM 25..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..123
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 134..215
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 234..321
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 327..414
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 450..557
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 565..660
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..888
FT /note="Polar residues"
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 493
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 531
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
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 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 257..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 348..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 888 AA; 96811 MW; B14ED51EA218E331 CRC64;
MSLTRFSLCL LLTLLLAAIP VYLASPDPGV RILRSPESTV APPGDEVVFV CETSLPPEHF
EWSYASSRSR FRYLKSGNHN ISITHDNDIS KLRVVVSLET LGEYRCVAWF GPLAVTSTTA
RLELAALSGG GGDEGFKGNQ AHWRVTAGNT VQWHCGHIES NPAPSWSFYY NDIELPAAST
LSDSNGTLLL SNVSVASSGS YRCVATNTAS GVRLALPSRL ELQVSAEAMP ATAPHLLDGQ
RVRTKVARVG ESVLLLCPGV GCPSPTAIWS SPNVPGAIKN NRTRVLPYGL QINELQALDG
GTYICYLDNG IRPALKHSIQ LLVQQAPRIV LAPSANLTNE GEAMQLECVA TGIPEPEIYW
LLNGNNSAND SKANPGSNGI LILQSVQKRH AGYVQCFARN SLGEDSAGTI LQVNPTQIQT
GDGGGGSRAY VRPQQHMFGR KQKQQTQMVP PSAPNVTRLS DESVMLRWHV MPNEGLPIKF
FKVQYRMLTG TGKSWQTTNE NIPYGKERND YGAVKNFTSS VTGLRPDRRY RFRIMAVYSN
NDNKESNTSG KFFLQRGATL APLAVPSLVD IEEYSQTAVV LHWDLTSDAD EDLISGYYAY
YRPSASAGEY LKATIDGAKS RSFQISALEP GTIYEFKLQS FSAVAASEFS ALKQGRTQRP
RVSTTTEPAV HAMDTTTPSH NETFNLNPLL TGTIGGGALL VLLVVSACLC LCRRRSSRGT
NQQNKPRLAE LREDFVPLNT CSPNKPRTRH LHITLNPLAQ QQQQQQQQQQ QQQQQQHEEK
DTQDNDMSYF QRPPVVYDAE ALGFNGMARM SSSSLRRSQR TLERAAAAGG GAGSGTNNNN
LNQPTDGSTA DSPRLQASNK PGRVILKRAR LSSRSENLSS GSLNSVGV
