ID   A0A158R5G2_9BILA        Unreviewed;       866 AA.
AC   A0A158R5G2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Receptor protein-tyrosine kinase {ECO:0000313|WBParaSite:SMUV_0000667701-mRNA-1};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000667701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000667701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
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DR   AlphaFoldDB; A0A158R5G2; -.
DR   STRING; 451379.A0A158R5G2; -.
DR   WBParaSite; SMUV_0000667701-mRNA-1; SMUV_0000667701-mRNA-1; SMUV_0000667701.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00096; Ig; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
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   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR12231:SF262; DPR-INTERACTING PROTEIN KAPPA, ISOFORM A; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SMART; SM00406; IGv; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        793..814
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          125..214
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          219..308
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          313..453
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          458..549
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          558..661
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          663..767
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          353..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..399
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   866 AA;  97320 MW;  CF9EEF23DD0A122C CRC64;
     MFLYQIPLYQ SIKRKTYYLH IEKIPNGLEL KFSTTDQHQL ITFAKFQTSL RCHAEGSNIP
     ENVYVEWHLE EDQKKAIVYP TGQIRSNIYF SSPTVSDSGQ YRCVARQDNS VIESKTINIT
     FIKAPEFMDN ETEQHPEEGT DAKLSCKIEN IGDSIIFWRF GAKTIKEGGP RVYKFEDDGQ
     TLLIPQFMAD KDDGLYQCYV NGLNKFFVKN ITVTAYEKPK IVDLETSENI IAYEGQSVDL
     TCLASGRPSP TYQWTRQKDD SEALQNSERY TIADGNLRIK SVLPLDKGTY RCSASNSLAT
     ASTDRILDVF EKPKIEAMED ITKDIGERVE MTCKYSGNGT ISVKWVHMGS EYKTSADTSS
     ADNVLEQSGN EMRRKRRQES RNASEADEDG DEEDADGDSQ KSADSDNDSH ITVTKTDNSL
     TLTIDQAKQE HSGGYQCVTE NDAGITQQEI KLSIRHQPII TSSSGLTKAV RGREVALYCE
     VSAVPDPDWT WYNELNQVIK PDGDNIKIQT GPHNLHSQLI FSQISTQQFG SYRCVANNSV
     GTPADKEIKV VETVIPNIPT NINCTANMYP NYAICKIPYS DVPIGRLPDT LTFKYVKNDE
     AFDDSNLVRS FTTSYDSNNE KEEYIISGLE PETRYKLRIS AENEAGTSEY SDDVLMETSE
     PKVPEMPAKI DVDCNEKCLA EWTPSNDMGA PIQKYRVYLE KLQDEKTEDI GDSVQMKEFD
     SMMTPLNVDL SQFRLAPLTD YRLRVSAVNE KGEGEAGETT FKTLEAPVTS INTRVSETTA
     SSLQAAPWGS TNLILTIAFI LLFLLLVADL ICFAANRCGI IACFCSKCFG RNVRNKREKD
     LEQANKSETN RLLSETKTNS RSASNR
//