LPHN_DROPS
ID LPHN_DROPS Reviewed; 1693 AA.
AC Q292N4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GA21229;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL24828.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region non-covalently linked to a seven-transmembrane moiety.
CC {ECO:0000250|UniProtKB:O88923}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:O88923, ECO:0000255}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88923}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000255}.
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DR EMBL; CM000071; EAL24828.2; -; Genomic_DNA.
DR AlphaFoldDB; Q292N4; -.
DR SMR; Q292N4; -.
DR STRING; 7237.FBpp0277076; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR InParanoid; Q292N4; -.
DR OMA; SMRGAYR; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1693
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393378"
FT TOPO_DOM 1..774
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..808
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 809..829
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 830..835
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..882
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..903
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..927
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..948
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 949..975
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 997..1003
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1024
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1025..1693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..119
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 713..760
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 190..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1499
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1693 AA; 185677 MW; 1A059ECAD209313A CRC64;
MVLQGAKQRL CSSKNLDTCV LTPKYQTAYA CEGKKLTIEC EQGELINLIR ANYGRFSITI
CNDHGNVEWS VNCMFPKSLT VLNSRCAHKN SCSVLAATSM FGDPCPGTHK YLEAHYQCVS
AAQTSTTTNR PSPPPWVLNN GPPIFGNGSG LIHPTNIGGG SGGASAPPRL PTLPGVVGIN
GNGGMFNVPP PATHATPPGS TATLPGGRLK GVATSTTTTK HPAGRRDGLP PPPQLHHHHN
HHTDETTPTK PSGKVPAASN ATAPSNTRIL TGVGGGGTDD GTLLTTKSSP NRTPGTAASG
PSVSSNGSAV RTINNINLNA AGMAGADDET KLFCGPTHAR NLFWNMTRVG DVNVQPCPGG
AAGIAKWRCV LMKRMPDSSF DEDDEEMAGT STTTPMSTSG DCLHNSSSCE PPVTMAHKVN
QRLRNFEPTW HPLTPDLTQC RSLWLNNLEM RVNQRDSSLI SIANDMSEVT SSKTLYGGDM
LVTTKIIQTV SEKMLHDKET FPDQRQREAM IMELLHCVVK TGSNLLDESQ LSSWLDLNPE
DQMRVATSLL TGLEYNAFLL ADTIIRERSV VQKVKNILLS VRVLETKTIQ SSVVFPDSDQ
WPISSDRIEL PRAALIENSE GGLVRIVFAA FDRLESILKP SYDHFDLKSS RSYVRNTAIL
TNDSDASAGD LQQRLRILNS KVISASLGKG RHIQLSQPIT LTLKHLKTEN VTNPTCVFWN
YIDHAWSANG CSLESTNRTH SVCSCNHLTN FAILMDVVDE HQHSLFTMFD GNMRIFIYIS
IAICVVFIVI ALLTLKLFNG VFVKSARTSI YINIYICLLA IELLFLLGIE QTETSIFCGF
ITVFLHCAIL SGTSWFCYEA FHSYSTLTSD ELLLEVDQTP KVNCYYLLSY GLSLSVVAIS
LVINPSTYTQ NDYCVLMEAN AVFYATFVAP VLIFFMAAIG YTFLSWIIMC RKSRTGLKTK
EHTRLATVRF DIRCSFVFFL LLSAVWCSAY FYLRGAKMDE DVTGIYGYNF ICFNTLLGLY
IFVFHCIQNE KIRREYRKYV RQHAWLPKCL RCSKTSISSG IVAGGGTGLG GTNAGTLCSV
STAKKSKLPL GTNDDAHDEQ QQQQHMSATE DAIMGASSDC ELNEAQQRRT LKSGLITGTL
QPSQSLGGHV VLERGNTLRS TGHASPTSSA GSTHLIFAHK QQQQQPPLGE AYYHQPDYYS
WKQTAGGMKA QREYYNNAGA ATSSPQQAHE VFYWTQKPNS QHGKKKRGGV GAIPASPSGS
LHSRATAASQ VLFYPSYKKT KPGQQAHPHY AEALDPPQPP NTAAYYQQQQ QLRQQRQQQQ
QQLSSDEEQA EQHAHLLHLQ HQQQQQQQRR AGGQQQLPAP PPHMAQYQQE FMQRQYRNKH
SNCDLGDAYY NQGSVGGADG GPVYEEILSN RNSDAQHYEV GDFDVDEVYN NSVGTGVFNN
MRAAVAAGGS RYGGSLSGGS VSSRNQQQQQ HSLAQPISAR RCTADEDDDE DEDDEETTAA
EQLHDGVCDE EEEDEESDME DDSHGLPPQS AERMRRLMAL QDEDFKRRFQ RQQRKHGAPV
DYGTLPPGSA QAVIGGAHPE HNGAVFGVSG GVGEGSMRGA LRQQHAKSPS ARLAVNELFG
HGNTGPPLPP ANQTPAQKRQ QLQKLSPQST TSSSSHTSHS NPHSHPPHHQ QRHLSAMLDE
NNTVRCYLEP LAK
