IHOG_DROMO
ID IHOG_DROMO Reviewed; 897 AA.
AC B4KJW1;
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=GI17739;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW12564.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW12564.1};
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; CH933807; EDW12564.1; -; Genomic_DNA.
DR RefSeq; XP_002003122.1; XM_002003086.2.
DR RefSeq; XP_015021007.1; XM_015165521.1.
DR AlphaFoldDB; B4KJW1; -.
DR SMR; B4KJW1; -.
DR STRING; 7230.FBpp0166956; -.
DR EnsemblMetazoa; FBtr0168464; FBpp0166956; FBgn0140480.
DR EnsemblMetazoa; FBtr0431863; FBpp0389118; FBgn0140480.
DR GeneID; 6577153; -.
DR KEGG; dmo:Dmoj_GI17739; -.
DR eggNOG; ENOG502QSGM; Eukaryota.
DR HOGENOM; CLU_004633_1_0_1; -.
DR InParanoid; B4KJW1; -.
DR OMA; CGLMEGK; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; B4KJW1; -.
DR Proteomes; UP000009192; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..897
FT /note="Interference hedgehog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000383616"
FT TOPO_DOM 27..702
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..897
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..147
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 148..235
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 244..336
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 342..429
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 462..571
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 579..674
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 434..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 504
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 506
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT BINDING 545
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:Q9VM64"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 363..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 897 AA; 97903 MW; 24BD0C6B7AC9C84E CRC64;
MSVTRGHKST PSLLLLFLSV LTSLLAAIPV LQANAPSAGP GVRILRPPES TVAPSGDEVV
FVCETSLPPE HFEWSYASTR SHAPRFKYLK SSSAKNNSNI TITNDNDISK LRVIVRPETL
GEYRCVAWFG PLAVTSTTAR LELATISGDK IAQRSNWRVA AGNTVLWQCG QVVSNPAPTW
SFYYNDIEMP AASTLSDSSG TLLLPHVSTA SSGTYTCVAT NTASGQRLAM PRRLELQVPS
AALPSAAPAL LPGQSVRTEV LARIGETVLL LCPGVGYPPP TAVWSSPDVT GAVYNNRTRV
LPYGLQIGGL QPKDTGTYIC YLDNGIRPAL EHYIQLVVQQ APRIVRPPSA NLTNEGEFMV
LECAATGTPT PKIYWLLNGE NSVYDTESEL PANGSLILRR VQKRHAGCVQ CFARNVLGED
SAGTLLQVNP TQIQAGDGMG TGGMGRSSNR NAHNRKQKQM VPPSAPNVTR LSDESVMLRW
HVVKNDGLHI QFFKVQYRMT DSGKRKSWQT TNENIPYGKQ RHDSDEAVRN FTSSVTGLRP
DHSYRFRIMA VYSNNDNKES NTSGKFFLQR GAALAPLPVP ELLDIKEYSQ TAVMLHWHLP
SDADEQLISG YYAYYRPSAS AGEYLKATID GAKARSALIS ALEPGTIYEF KLQSFSAMAA
SEFSSLKQGR TQRPRSSTTA QPTMHTVDTT TPTHNETFNM NPLLTGTISG GALLILLVIS
ACLCLCKRRH SRGDNSQNKP RLAELREDFV PLNTCSPNKP RTRHIHITLN PLAQQQQQQL
QQQHQQDEKD SQDNELGYFQ RQPVVYDAET LGFNGLARMS SSSLRRSQRT LERAAAGGGS
GGNNNNLNQA TDASLAASLD SPRLQASNKP GRVILKRSRL SSRSENLSSG SLNSVGV
