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Database: UniProt
Entry: A0A182PRH7_9DIPT
LinkDB: A0A182PRH7_9DIPT
Original site: A0A182PRH7_9DIPT 
ID   A0A182PRH7_9DIPT        Unreviewed;      1097 AA.
AC   A0A182PRH7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Interference hedgehog {ECO:0000256|ARBA:ARBA00041099};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI009561-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI009561-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI009561-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}.
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DR   AlphaFoldDB; A0A182PRH7; -.
DR   STRING; 199890.A0A182PRH7; -.
DR   EnsemblMetazoa; AEPI009561-RA; AEPI009561-PA; AEPI009561.
DR   VEuPathDB; VectorBase:AEPI009561; -.
DR   OrthoDB; 3138076at2759; -.
DR   Proteomes; UP000075885; 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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR44170:SF53; BROTHER OF IHOG, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 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; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
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        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        807..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          244..336
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          345..417
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          434..518
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          572..674
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          686..780
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  120599 MW;  CC0C02C73137E763 CRC64;
     MYGEADKRPR TQPPFVSDRR SLLSRTQQHL PHCCGGSSRT ERRIPYGGLL LLCLVLTMCI
     FPPVSSSPQS SYSHHSHHSH GHHHQAAPHG VLSGTGSHHS GSGSATASQQ YGSSSGRSSS
     SGSGLGVYII RAPESTIAPA DDEVLFECEL NLVPEQLDWR FRAQGTSGQR KDYVLIQSNH
     HGYNASVVDG RYKLRVSVSE STIGEYQCVA WFGASAIASI PARLTLATIG LEAESIPGRH
     DRVPTTMRRI QPLQHFKVFP GNSIIIDCGD IVSNPPPIWS YYRDGMTIYP NVTQLQTGRR
     LILASLTQRD SGTYWCSAVN SITGSEVLLP QRTTVTVDYV PRSAPRAFTQ PQNVSVLPGD
     TALLECPGVG NPVPVPAWTR ANGIPLNARA RIQDYGLQLS NVHPEDEGQY LCRLQNGIDP
     PLLHSIWLTV LEPPRIVAPP RSTLTNESDS LELECIARGS PHPDIYWMIN GDYTKWDSLI
     RTNGTRLIIQ SVEKRHAGIV QCFARNSVGE ASEGNLLQVI PKQIPGGVGT TPLGSVPSSP
     KSGNDHSPKR KGGKKHKNRK YGMRIPNMVM IPPSRPNITR LSDESVMVRW SVPSSDGLPI
     QFFKVQYRML GDPSKNIART QWMTENDDIS PYTRSYEVNN LKPDHLYRFR IVAVYSNNDN
     KEGAASGKFH LQRGSQLGLT KNHLLAPTLT RIEPVSQHAV VLQWQFPQHL PHPIDGFYAY
     YRPATTAGEY SKATVDSSTA RHFKIDHLEP GTAYEFKLQS FTASAASDFS EILTGRTLKP
     PTPPPTVPTV IAAAEGPDGS QVVPVNYLLV IGCVLIVSVL IVLFLCCCFS RRKKRGHGAD
     EPDAKVHIPV DQNGFTGAVS NGGPRVAHHK TRTNGMNGRM NITPNPLAQD GDKVTASFHA
     SCGIPQPQKP HQQQQQQQQQ QEQLMLASMP HRRTLERTAV RPIPNGATIA YGVDPKLMLD
     SGQPAVSPPD CRQSSMRRTR RGSGSVPGSP RIGRGPSNEF LQQQQQQQQQ QGVTVARSPM
     PMRAAGMKRS AATRLGRAEN MSSGSLNSIE LMYLVRRRMR KPRAAAATPS ALPQQDSEHH
     CHKQAFYERA NGYRLIS
//
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