ID A0A182PFJ1_9DIPT Unreviewed; 1103 AA.
AC A0A182PFJ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
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:AEPI005698-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:AEPI005698-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI005698-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR AlphaFoldDB; A0A182PFJ1; -.
DR STRING; 199890.A0A182PFJ1; -.
DR EnsemblMetazoa; AEPI005698-RA; AEPI005698-PA; AEPI005698.
DR VEuPathDB; VectorBase:AEPI005698; -.
DR OrthoDB; 5405965at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0040011; P:locomotion; IEA:UniProt.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45842:SF12; KEKKON 5, ISOFORM A; 1.
DR PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF13855; LRR_8; 4.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00365; LRR_SD22; 9.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 722..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 400..496
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 501..590
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 598..676
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 848..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 121787 MW; CD19732AE93AE868 CRC64;
DLASNRLSHE TISTQLSDLR KLKELNLNNN RLHRLPVLRG VSNLTKLVAS NNQIKTIDAE
ALAGLPALKF LDLSRNAIQE LQYSSFPETL QYNLQYLNLN FNKLVVLTKG TFNRLQSLKR
LEISSNGLKE VQSLTFQNLN QLKSLKLNNN RIPALLDGVF HGLIAIASLE LNNNSISTIH
KGGFFNLTSL THLWLAHNRI VEIEQSGWEF TPKLKSLDLS YNQLESLDRS TFEELSDLQT
LNLQGNRISE IGEGTFNQTT SLKTLYLNEN RISETIEDMS GPFTGLGKLE RLYLNANQIK
SVSRNAFLGL KSLMLLELSQ NNISSIQNNS FRDTTQLKNL IMNSTNLICD CNLRWFYRWI
RDPSHEFQID AECIYPIWLR NRLIRELHSS NFMCYDSPKP HLIEEPESQL GIRGTNVSLV
CAATSTAADP MTFKWKQDNV ELSADQYTTH QINNENGTIG SSELFIPNIQ QSGAGKYQCI
ITNNYGVVYS QKVKVTVGTY PKFRKTPSDV SVEPGKVARL DCAAVGDPKP QIYWEKDGGN
DFPAAKERRM HVIPNEDAFL ILNVQLVDMG VYSCTAENQA GVIRANASVI VLESQTAPRP
VSSLETAIGK ASVIECKVGV SPKPVIFWLK DGEPIELTER HFITGEGQLL VIVDTEMADA
GLYECRFENE ISSEIGSTRL IVVDGPEDMH GSVLGEVGTA HDGATGVLEE VHTLNARMFD
SWPVLVIALI VCIVLTSLVW MCCMYRLQKR IRGGGSSCPG ETELDLATGM EINQPNLIVR
SGVGTSTTPA GYFEYLIPMV RGGEMTSNVD DDGESADGGT IGRNHDGFYT AVSKANVRST
ELDLDDLDDD LSSKDSGTGG DCASATGSTN AAHRGSHEDL KCLLHSLNRK HTSEQELNHH
KPYQLARRSD AIILPAVQND PDDDPRLEPP PVIPPVNATS AVLIVGPATE IAAPVSETVQ
RDDRIPAHAA HIATRMPNSQ TFPVLTQPAS AVTGSALRTS SLEASADPVL PLKKPAPQQQ
IQVNQLYQLL LENPRLMEKP AKYRTKSMDQ CHEVELRPAS ASSGIGTGSS NGSTMNGEFP
SEQRQQQQLS SRMVTDARRK VKR
//