ID A0A026VTY3_OOCBI Unreviewed; 802 AA.
AC A0A026VTY3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Interference hedgehog {ECO:0000256|ARBA:ARBA00041099};
GN ORFNames=X777_16426 {ECO:0000313|EMBL:EZA47263.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA47263.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA47263.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107906; EZA47263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026VTY3; -.
DR STRING; 2015173.A0A026VTY3; -.
DR OMA; CGLMEGK; -.
DR Proteomes; UP000053097; 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; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 669..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..204
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 215..295
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 303..389
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 435..537
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 544..639
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 394..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 88618 MW; 857ABDA10E9112EC CRC64;
MQCLAFAGER QELGMSFTRH PQPLAAPLND DVNFECSLNL AAEYFAWHHR PLGSNKWTPL
SHPNGTTKDS YTNGGKTSRL LINFGDESKA GDYRCIAFFG TSGLASDPAR LTLATIQRFS
DKSDVFIQVT EGNTVPITCP VPYSEPEAIA QFYKNDILIE DADLVNSKTM VIKSARLTDS
GAYHCSASNY ITLQMFTSNR KTILTVHANT TFQAPYFTKQ PQTEYTVTRG KNVTLECFAA
GYPVPRVTWS RLGSSLPLKS IRSSTGLTIV HVQLSDRGEY DCVWSNEVQQ IKSVIILRVV
EPPRVIKQPK ASTFAEGGEL ELSCSVTGEP EPTVEWLING QSLMPSKNQE IKGSTLLISE
VEKKHAGIVQ CVASNEYGSH SGYNLLQVNP KQHVLGGTTE SKPEYETISR HKHTRGGGRR
RGKEGKKKGA AILIPPTQPN VTRLSDVSVM VRWTVPENKG LPIQFFKVQY REIGPKVNGK
QAKWMTANTE IPNHVRSFEV TDLQPDHTYR FRIAAVYSNN DNKLSPNSVR FHLTRKKGFE
SNKMPIPLLT NTEAIGPHQV LLIWQNPDRK TKIDGFYIYH RATTTAGDYL KTTVEGKDAF
NMTISHLQAD TAYEFKLQSF CVDGASEFSQ ILRQKTKKLV EHPVEQVVAE NKLKPIENNK
PVSIHVTHIV GGVLGAAVLL VTLTLSARYL YKKVRCKQSQ ESQGDGKPIA NGRVMVNGGV
TDSKINITSN PLAGLDASED IMQPKSGQQS SMEMTSFLNG QNNNGSNNSH NNGDAAGSDV
NVTSHNEPSS LLQGPLPIEQ RL
//
