IHOG_DROVI
ID IHOG_DROVI Reviewed; 907 AA.
AC B4LRN7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-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=GJ17563;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW64639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW64639.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH940649; EDW64639.1; -; Genomic_DNA.
DR RefSeq; XP_002052484.1; XM_002052448.2.
DR RefSeq; XP_015028451.1; XM_015172965.1.
DR RefSeq; XP_015028452.1; XM_015172966.1.
DR AlphaFoldDB; B4LRN7; -.
DR SMR; B4LRN7; -.
DR STRING; 7244.FBpp0231980; -.
DR PRIDE; B4LRN7; -.
DR EnsemblMetazoa; FBtr0233488; FBpp0231980; FBgn0204733.
DR EnsemblMetazoa; FBtr0435080; FBpp0392081; FBgn0204733.
DR EnsemblMetazoa; FBtr0443244; FBpp0399656; FBgn0204733.
DR GeneID; 6627462; -.
DR KEGG; dvi:6627462; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; B4LRN7; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; B4LRN7; -.
DR Proteomes; UP000008792; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..907
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383621"
FT TOPO_DOM 24..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..149
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 152..233
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..433
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 468..578
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 586..681
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 427..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 511
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 513
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 552
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
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 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 173..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 367..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 907 AA; 99013 MW; A1B88E870BDC4D54 CRC64;
MSLTRRFSLT LLLLLPLLTS LLAAIPVLQA NLSPAPSSSP GPGVRILRAP ESTVAPPGDE
VVFVCETSLP PEYFEWSYAS SRSHPPRFKY LKSSSAKANH NITITHNNDI SKLRVIVRPE
TLGEYRCVAW FGPLAVTSTT ARLEMASISG DGADTDQRAH WRVAAGNTVL WHCGQVASNP
APSWSFYYND NEMPPASTLS DSNGTLLLPH VSAASSGSYS CVATNTASGV RLALPSRLEL
QVPAAALAST APALLNGQRV RTQVFAKAGE TVLLLCPGVG YPPPTAVWSS PNVPGAVYNN
RTRVLPYGLQ ISALQPLDAG TYICYLDNGI RPALEHFIEL VVQKSPRILR PPTANLTNEG
ERMQLECEAT GMPKPEIYWL LNGESSVYDV EAEQVPNGHL ILHSVQKRHA GYVQCFARNS
LGEHSAGTLL QVNPKQLPDG EGTGMDSGRS SARPTHSRKQ KQQTQMVPPS APNVTRLSDE
SVMLRWHVVR NDGLPIQFFK VQYRMLTESG KRKSWQTTNE NIPYGRQRHE SGAGVRNFTS
SVTGLKPNSS YRFRIMAVYS NNDNKESNTS GKFFLQRGAA LAPLAVPELV DIEEYSQTAV
VLHWRLSSDA DEQLISGYYA YYRPSASAGE YLKATIDGAK SRSFQISALE PGTIYEFKLQ
SFSAVAASEF SALKQGRTQR PRASSTPQPV LHAVDTTTPS HNETFNMNPM LTGTIGGGAL
LVLLVISACL CLCRRRSSRG NNPQHKPRLA ELREDFVPLN TCSPNKPRTR HIHITLNPLA
QQQQQQQQQQ LQQQQHDEKE AQDNDMGYFQ RQPVVYDAET LGFNGLARMS SSSLRRSQRT
LERAAAGGGS GGNNNNLNQP GDGSLANSAD SPRLQASNKP GRVILKRARL SSRSENLSSG
SLNSVGV
