ID G0P8A1_CAEBE Unreviewed; 1186 AA.
AC G0P8A1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Interference hedgehog {ECO:0000256|ARBA:ARBA00041099};
GN ORFNames=CAEBREN_11960 {ECO:0000313|EMBL:EGT47676.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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 EMBL; GL380130; EGT47676.1; -; Genomic_DNA.
DR AlphaFoldDB; G0P8A1; -.
DR STRING; 135651.G0P8A1; -.
DR EnsemblMetazoa; CBN11960.1; CBN11960.1; WBGene00150685.
DR eggNOG; KOG3513; Eukaryota.
DR HOGENOM; CLU_005756_1_1_1; -.
DR InParanoid; G0P8A1; -.
DR OMA; RAHAPFF; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00063; FN3; 5.
DR CDD; cd00096; Ig; 1.
DR CDD; cd04978; Ig4_L1-NrCAM_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
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; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 6.
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 Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1186
FT /note="Interference hedgehog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003405978"
FT TRANSMEM 1124..1146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..120
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 128..227
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 235..323
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 328..407
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 425..513
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 517..601
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 610..715
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 717..817
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 822..918
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 919..1012
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1014..1110
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 1186 AA; 135708 MW; EBD50DCB77425BFD CRC64;
MRLVTVQFLL VAQILAAQRS SIGPPKLLEQ SEEEVWYHLD DDDLKNRLTL RCEADENTDR
YTWLKDGEPF DIDSEDVLWE KETQSGTIVF AKPHASHQGY YQCFASNIFG TALSNKMHLR
LGSLEHFPKR DIQILRVKEG ESLTLNCTPP RGTPPPRIIW LYRSLDDSSV IETIKSRHIT
VDINGKLHFS SVELSDGKAT LVYECAATSP VLRGEYRSGD RIQLDIEPTQ EKSHPVKKLS
VSPSEVTVRA GSQLKLQCIF GGRPLPTIFW SKVDGELPKS RLKDLTSSES DFGRSLIVEN
VHPDDAGVYE CRGRHLVHTV NVRVMAAPFW EFDPPRDISL PEENTGELEC LAGGQPTPII
TWSMNGKFLH ELAEDSRRVL LDHGRILRVR SLNHDLDTGV YQCNASNPLG YVFANAFVHV
RAHAPFFRMP AARHWKVVLH STVILDCDVD AAPEAVVRWV DADDRPLQVV EGKNKLFPNH
TFMIYDVNSA DEGLYYCNVS NKYGINRATN RLQVFKPTYF VRIPTPKRLV LEAGETAEVF
CEAVADPRLP IKYQWTINGK VLTESQYYEI LPDRLRFRSV RGRHSGIIDC AAITDVDVKL
ASMQLIVKDV PAHPVVEAAH CSERKANIKW VAASDHGDSI KKYIVEMFTD FKKNEWEVIN
EEVNVNKENF EVDITLTPWV NYTFRVVAVN SHGRSDMKID GQPKEDWLTC QTRPSFPYTN
PTGVKGEGTE PDNLVISWKP LDRYYWNAPN MQYLVRYKLD EPIHGWTEFL VEDSLANYTI
IRDQPTFRKY LIQVQSVNSV GPSIVEPEIH HGWSGEDVPD EAPRDFRIDT QINFTTINFT
WNPVDANTVN GHFVGYEIEY WKAENTVRKY SIKIPANSTY KIINSFHAVT NYSAHIRTRN
KRLRSAPSHP VSFAMPEGPP GKVHNLRVYS VGSTAILLQW DAPLQPNGRI RGYFISFQND
KNETEETYVI HRQKYYLHEK SEPDTGYKVS VWAETRAGEG PTTLRPVRTW PSRIPDAPVF
RVKNITLDSF VVEWLPNNHS VWKMPGAAFF VNYTAESSNT WHQTEIIYLP NTEILLRNLK
EDQKYFIQGI AKDGPRQSES VFLPIKTLNR DYANRLKEDS LRSAAWFIAV LGVLGIGLFT
ICLTFCCGNK NRQEKFAVRR KEIEIGHQQD NEEEKQFLEY QYGFKN
//
