IHOG_DROYA
ID IHOG_DROYA Reviewed; 880 AA.
AC B4NZY8; Q2XY52; Q2XY53;
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=GE18390;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW87815.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW87815.1};
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).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABA86415.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-874, AND VARIANTS LEU-10; GLN-175;
RP MET-806 AND VAL-863.
RC STRAIN=T33 {ECO:0000312|EMBL:ABA86416.1}, and
RC Tai18 {ECO:0000312|EMBL:ABA86415.1};
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
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; CM000157; EDW87815.1; -; Genomic_DNA.
DR EMBL; DQ138809; ABA86415.1; -; Genomic_DNA.
DR EMBL; DQ138810; ABA86416.1; -; Genomic_DNA.
DR RefSeq; XP_002088103.1; XM_002088067.2.
DR AlphaFoldDB; B4NZY8; -.
DR SMR; B4NZY8; -.
DR STRING; 7245.FBpp0263400; -.
DR EnsemblMetazoa; FBtr0264908; FBpp0263400; FBgn0084224.
DR GeneID; 6527007; -.
DR KEGG; dya:Dyak_GE18390; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; B4NZY8; -.
DR Proteomes; UP000002282; Chromosome 2L.
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; Repeat; Signal; Transmembrane; 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_0000383623"
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..234
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 810..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"
FT VARIANT 10
FT /note="F -> L (in strain: Tai18)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT VARIANT 175
FT /note="K -> Q (in strain: Tai18)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT VARIANT 806
FT /note="L -> M (in strain: Tai18)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT VARIANT 863
FT /note="L -> V (in strain: Tai18)"
FT /evidence="ECO:0000269|PubMed:16120803"
SQ SEQUENCE 880 AA; 97160 MW; 4440BBC832D2C50F CRC64;
MTLLTSSLLF FSLLTSRLEA IPVLEKSPAH PAHSAHPAHP SHPSPGVRIL RAPESLVAPL
GDEVVLECET SLQPERFEWS HRSSRSSGAG FKYLRTGTAK ANVSQEAAIS RLKVLVRQDT
LGEYRCVGWF GPLVVTSTIA RLELASTSLL GGQESESPLQ WRVSAGNSVL WPCGKQVKSN
PSASWSYYRN GVEIKPEFIG TNGNIFLSNV SSESSGSYSC QATNPASGER IQLTGSLQLQ
VTPEQRSQSK SPHLLNGQPN SQEITIREGS SLLLLCPGVG SPPPTVVWSS PDVVGAVKNK
RSKVIGHALE ISNTRVQDAG TYICFQDNGV RPVLEHYIKV HVEQPPQIVR PPWADLTNEG
DRLKLECEAT GVPTPEIYWL LNGHSSLDDT EAELSNNFLI LHSVLKRHAG YVQCFARNRL
GEHSAGTLLQ VNPKQIQEPR ESGGTHRPKP NQGSKQKQMY PPTPPNVTRL SDESVMLRWM
VPRNDGLPIV IFKVQYRMVG KRKNWQTTND NIPYGKPKWN SELGKSFTAS VTDLKPQHTY
RFRILAVYSN NDNKESNTSA KFYLQPGAAL DPMPVPELLE IEEYSETAVV LHWSLASDAD
EHLITGYYAY YRPSSSAGEY FKATIEGAHA RSFKIAPLET ATMYEFKLQS FSAVSASEFS
ALKQGRTQRP KTSTTEEPTL QMGDRDTTTP SHNETFNMSP MLTGTIGGGA VLILLLISTC
LCVCRRRSSR SRGNNPNKPR MAELRDDFVP LGNCSPTKQR QRTRHIHITL NPLAQQQQQA
LEEKNDTDQD APYYQRPSSY DYDPGLRRMS SSSLRRSQRT LERAGGSNGS NNGNNNNLNQ
SAEAGPVENP GKPGRVLMKR PRLSSRSENL SSGSLNSVGV
