IHOG_DROSI
ID IHOG_DROSI Reviewed; 880 AA.
AC B4Q599; Q2XY54; Q2XY55;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE Flags: Precursor;
GN Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GD22528;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX04032.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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:ABA86414.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-874, AND VARIANTS VAL-308; ASP-368
RP AND THR-713.
RC STRAIN=Ky-a {ECO:0000312|EMBL:ABA86413.1}, and
RC Ky-b {ECO:0000312|EMBL:ABA86414.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDX04032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000361; EDX04032.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ138807; ABA86413.1; -; Genomic_DNA.
DR EMBL; DQ138808; ABA86414.1; -; Genomic_DNA.
DR AlphaFoldDB; B4Q599; -.
DR SMR; B4Q599; -.
DR STRING; 7240.B4Q599; -.
DR PRIDE; B4Q599; -.
DR Proteomes; UP000000304; 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; 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_0000383620"
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 155..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 429..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..692
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 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 308
FT /note="A -> V (in strain: Ky-b)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT VARIANT 368
FT /note="E -> D (in strain: Ky-b)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT VARIANT 713
FT /note="I -> T (in strain: Ky-a)"
FT /evidence="ECO:0000269|PubMed:16120803"
FT CONFLICT 37
FT /note="T -> S (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="A -> S (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..157
FT /note="PES -> SEA (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="N -> K (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="H -> Q (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> S (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="T -> S (in Ref. 2; ABA86413/ABA86414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 97188 MW; DD7ECF3940AA2A5B CRC64;
MTLLTSSLLL FSLLTSRLEA IPVLEKSPAH PAHSAHTAHP AHPSPGVRIL RAPESLVAPL
GDEVVLECET SLQPERFEWS HRSSRSPGAG FKYLRTGTAK ANVSQEAAIS RLRVLVRPDT
LGEYRCVGWF GPLVVTSTTA RLELASTSLV DAQEPESPLQ WRVSAGNSVL WSCGQQVQSN
PSASWSYFRN GVEIKPEFIG TNGNLFLSNV SSESSGSYSC QATNPASGER IQLPGSLQLQ
VTPEQRSQSK SPHLLKGQPS SQEITIREGS SLLLLCPGVG SPPPTVVWSS PDVVGAVKNK
RSKVFGHALE ISNTRVHDAG TYICFQDNGV RPALEHYIKV HVEQPPQIVR PPWADLTNEG
DRLKLECEAT GVPTPEIYWL LNGHSSIDDT EAELSNNFLI LHSVLKRHAG YVQCFARNRL
GEHSAGTLLQ VNPKQIQEPR ESGGTHRPNP NQGSKHKQMY PPTPPNVTRL TDESVMLRWM
VPRNDGLPIV IFKVQYRMVG KRKNWQTTND NIPYGKPKWN SELGKSFTAS VTDLKPEHTY
RFRILAVYSN NDNKESNTSA KFYLQPGAAL DPMPVPELLE IEEYSETAVV LHWSLASDAD
EHLITGYYAY YRPSSSAGEY FKATIEGAHA RSFKIAPLET ATMYEFKLQS FSAVSASEFS
ALKQGRTQRP KTSTTEEPTL QMGDRDTTTP SHNETFNMSP MLTGTIGGGA VLILLLISTC
LCVCRRRNSR SRGNNPNKPR MAELRDDFVP LGNCSPTKQR QRTRHIHITL NPLAQQQQQA
LEEKNDTDQD APYYQRPSSY DYDPALRRMS SSSLRRSQRT LERAGGSNGS NNGNNNNLNQ
TAEAGAVENP GKPGRVLMKR PRLSSRSENL SSGSLNSVGV
