ID A0A1I8PA29_STOCA Unreviewed; 1017 AA.
AC A0A1I8PA29;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Interference hedgehog {ECO:0000256|ARBA:ARBA00041099};
GN Name=106081410 {ECO:0000313|EnsemblMetazoa:SCAU006200-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU006200-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU006200-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU006200-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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:0000256|ARBA:ARBA00037573}.
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. {ECO:0000256|ARBA:ARBA00038530}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IHOG family.
CC {ECO:0000256|ARBA:ARBA00038144}.
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 RefSeq; XP_013098785.1; XM_013243331.1.
DR AlphaFoldDB; A0A1I8PA29; -.
DR STRING; 35570.A0A1I8PA29; -.
DR EnsemblMetazoa; SCAU006200-RA; SCAU006200-PA; SCAU006200.
DR KEGG; scac:106081410; -.
DR VEuPathDB; VectorBase:SCAU006200; -.
DR OrthoDB; 3138076at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR44170:SF53; BROTHER OF IHOG, ISOFORM G-RELATED; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 747..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..182
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 211..272
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 289..376
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 381..467
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 506..618
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 628..723
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 111343 MW; 31180C963AA0DBDE CRC64;
MLPTTGTATA TTAPAPPTAS TTTTLFHKNT CSSLLPPFVR TPLCSSSGGF FAFSPLSVIV
KSVIFFLAFA TSACLASQPP TLGVHFVRSP ESAVAPKGDE VVFECEMNLG PERLEWKFRH
SSNRTADGSR FIYLSKESGY NITNDEKNSK LRFVVQPETL GDYQCVAWYG SAAIASLSAR
LTLVSISIDN SNGYSRNAIR WNVAPKNHIL LRCGTVSSNP AAIWSFYRNG EKIPQSEVIP
ANGALVLNTV TAKDSGNYTC SAMNPITSQE VKLPQRIDLR VDYSDRTPPY FLTQPPTQVT
ARPGETVVLE CPGVGSPPPV AVWSSPNIIN MNNNNRTRLL PYGLQIVDVV PEDQAQYVCR
LDNGIAPALV HGIKLNVLEK PSILRGPALT LTNESDTLEL ECSAAGNPYP DIYWLINDVD
TTMDPEMQHD GRRLVIRHVQ KRHAGIVQCF AKNEVGEVSD ANLLKINPKQ IHGSSASAAT
PRPRYEDVGG GTKKGSRKKH KPTMVPPSRP NVTRLSDDSV MLRWYVPKND GLPIQFFKVQ
YRMLGDASRK IPRENWQTTN DDIAYGKRNT DISKNYTTSV TGLKPDRFYR FRIVAVYNND
DNKEGNTSSK FFLQRGDALD LSKSNLPIPE LARIEALSES AVMLQWSLPT AAATSHIDGF
YAYYRPAASA GEYQKATVDG MHTRKFKIDM LEAGTAYEFK LQSFNDMAAS EFSAIVQGKT
KKSVTTPAPT LPAVVPATKA NQEDNSIFPV VAGAAGGGIL LLIATIAACL CMKKRKNSQN
EDENKPQLDH IQADFVTPQV QVLGVNNHHK GNHRLNGVLP RMNITPNPLA QEADKAHLAS
QGIHHAQPYY QTPPTPTMMN KRDYQQPPPV PPHQNNNHAP MMNHHLPPTG HHAPLTPSME
QQRRTLDRGV RNMNYNQSNG NAMSPPSHDA ALNMDGMATR IPSLRRTRRT SGGSTNNALN
ALSNNPNGGL GIPIAVSGSP RVQRSPMPAR AAMMKQRSRL GSHNDNISSG SLNSIEV
//
