IHOG_DROPS
ID IHOG_DROPS Reviewed; 903 AA.
AC Q29JX6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Interference hedgehog {ECO:0000250|UniProtKB:Q9VM64};
DE Flags: Precursor;
GN Name=iHog {ECO:0000250|UniProtKB:Q9VM64}; ORFNames=GA21616;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL32835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(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; CH379062; EAL32835.1; -; Genomic_DNA.
DR RefSeq; XP_001355776.1; XM_001355740.3.
DR AlphaFoldDB; Q29JX6; -.
DR SMR; Q29JX6; -.
DR STRING; 7237.FBpp0285700; -.
DR EnsemblMetazoa; FBtr0287262; FBpp0285700; FBgn0081601.
DR GeneID; 4816196; -.
DR KEGG; dpo:Dpse_GA21616; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; Q29JX6; -.
DR OMA; CGLMEGK; -.
DR PhylomeDB; Q29JX6; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0081601; Expressed in female reproductive system and 2 other tissues.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..903
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383618"
FT TOPO_DOM 21..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..144
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 134..236
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 252..341
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 470..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..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 506
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 512
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 514
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 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
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 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
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 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..128
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..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 903 AA; 99205 MW; 1E2EAE3F49F394E6 CRC64;
MSPLTSSLLL FSLLTSSLEA IPVLQPSFPP SSPSPAPSPG VRILRAPESI VAPLGDEVVF
ECETSLQPEG FEWSYRRWPN AANSNGSVGA SRFKYLKSGN GKLNVTQETA ISRLRVLVRP
DTVGEYRCIG WFGPLVVTST TARLELANTS VKGRQETHLQ WRVAPGNSVL WSCGQQVHSN
PSASWSYYRN GVEIKPELAA TNGNLFLTNV STASAGKYTC LATNPASGAR IEISSSMVLE
VLSGRGSQNK APHLLSGQPT SQAVTIREGS TLLLLCPGVG SPTPTAVWSS PDVVEAIHNK
RTRVLNHGLE ISNVQGHDTG TYICYLDNGV RPTLEHFINV TVEVPPRITR PPWADLTNEG
ERMQLECEAT GVPAPELYWL LNGESSINDT EAEQLPNGYL VLHSVQKRHA GYVQCFARNR
LGEQSAGTLL QVNPKQIQSE PRETGSGGGF GSHRSMKPVN HGQKPTKMIP PSPPNVTRLS
DESVMLRWHV PRNDGLLILF FKVQYRMISE GKRKNWQTTN DNIPYGKPKW NSELGKSFTA
SVTDLKPQRT YRFRILAVYS NNDNKESNTS AKFYLQPGAA LEPMPVPELL EIEEYSETAV
VLHWRLDSDA DEHLITGYYA YYRPSSSAGE YYKATIEGAH ARSFQIATLE AATIYEFKLQ
SFSAVSASEF SALKQGRTQR PKASTTEEPT IQGIGDRDTT TPSHNETFSM SPMLTGTIGG
GALLLILLVS AFLCMCRRRS PRGRGQTQNK PRMAELREDF VPLGSCSPNK QRQRTRHIHI
TLNPLAQQQQ QQLDEKNPPG LETDNDMAYF QRQPTYEYDP GLRRMSSSSL RRSQRTLERA
GGANSGGNNG GNNNNLNQSS EAGTADGPCM QSSSKPGRVI MKRPRLSSRS ENLSSGSLNS
VGV
