LPHN_DROAN
ID LPHN_DROAN Reviewed; 1714 AA.
AC B3MFV7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GF12369;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV35639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV35639.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH902619; EDV35639.1; -; Genomic_DNA.
DR RefSeq; XP_001958817.2; XM_001958781.2.
DR RefSeq; XP_014763191.1; XM_014907705.1.
DR AlphaFoldDB; B3MFV7; -.
DR SMR; B3MFV7; -.
DR STRING; 7217.FBpp0115561; -.
DR MEROPS; P02.A01; -.
DR EnsemblMetazoa; FBtr0392654; FBpp0352014; FBgn0089406.
DR GeneID; 6495220; -.
DR KEGG; dan:6495220; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR InParanoid; B3MFV7; -.
DR OMA; SMRGAYR; -.
DR PhylomeDB; B3MFV7; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000007801; Unassembled WGS sequence.
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..1714
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393372"
FT TOPO_DOM 1..765
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..786
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 787..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 895..911
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 967..987
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 988..994
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1015
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..115
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 704..751
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 183..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1501
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1714 AA; 188749 MW; 9E624FC2A9E8831E CRC64;
MSSIDISGRY ALNDLEMVSK YQTAYACEGK KLTIECDPGD VINLIRANYG RFSITICNDH
GNVEWSVNCM FPKSLTVLNS RCAHKQSCSV LAATSMFGDP CPGTHKYLEA HYQCISAAQT
STTTNRPSPP PWVLNNGPPI FGNGSGLIHP PGSPGAAPPP PRLPTLPGVV GISGNGGLFN
VPPPHTVTHS TPSSSTVPGR MKGVATSTTT TKNPAGRHDG LPPPPQLHHH HTHHGEEAAP
PTKPSSKLPS AGNATAPSNT RILTGVGGSG TDDGTLLTTK SSPNRPPVTA SNGSPASGNN
SVVRTINNIN MNAAGMSGAD DESKLFCGPT HARNLFWNMT RVGDVNVQPC PGGAAGIAKW
RCVLMKRLPD SGYDEYDDDP SSTTPAPSGG DCLHNSSSCD PPVSMAHKVN QRLRNFEPTW
HPMTPDLTQC RSLWLNNLEL RVNQRDSSLI SIANDMSEVT SSKTLYGGDM LVTTKIIQTV
SEKMLHDKET FPDQRQREAM IMELLHCVVK TGSNLLDESQ LSSWLDLNPE DQMRVATSLL
TGLEYNAFLL ADTIIRERSV VQKVKNILLS VRVLETKTIP PSVIFPDSDQ WPLSSDRIEL
PRAALLDNSE GGLVRIVFAA FDRLESILKP SYDHFDLKSS RSYVRNTAIL ANDSSDSNTG
EIQQRIRILN SKVISASLGK GRHIQLSQPI TLTLKHLKTE NVTNPTCVFW NYIDHAWSAN
GCSLESTNRT HSVCSCNHLT NFAILMDVVD EHQHSLFTMF DGNMRVFIYI SIAICVVFIV
IALLTLKLFN GVFVKSARTT IYTSIYVCLL AIELLFLLGI EQTETSIFCG FITVFLHCAI
LSGAAWFCYE AFHSYYTLTS DELLVEVDQT PKVNWYYLLS YGLSVSVVAI SVAINPSTYT
QNDYCVLMEA NILFYATFVA PVLIFFVAAI GYTFLSWIIM CRKSCTGLKT KEHTRLASVR
FDIRCSFVFL LLLSAVWCSA YFYLRGAKTD EDTTTIYGYC FICFNTLLGL YIFVFHCIQN
EKIRREYRKY VRQHAWLPKC LRCSKTSISS GIVAGGGPAA GTLCSVNTSK KPKLPLGVSE
EVHGEQQQHQ QAMGVPAPED AIMGATSDCE LNEAQQRRTL KSGLMTGTLQ TPQQPLAGHV
VLERGSTLRS TGHASPTSSA GSTHLIFAHK QQQQQQALGE SYYHQPDYYS WKQPPQGGLK
SQREYYNNAG VAASSPQQAH EVFYWTQKPN SQHGKKKRGG AVPASPSGSL HSRTAAASQV
LFYPSYKKTK QGQPSGYPHY AEALDPPHSA GAAFYQQQQQ MRRQQQQQQQ QQQQQLSSDE
EQAEQHAHLL HLQHQQQHQR RVGGQQQLPA PPPHMAHFQQ EFMQRQFRNK TSNCDLAMGG
DTYHNQGSEG GADVCPVYEE ILSNRNSDVQ HYEVGDFDVD EVYNNSVGTG VFNSMRAAIT
AGGSRYGGGS LSGGSVSSRS QQQQLQKQQK QQQQQQQRSA RRCTADDDDD DDEEEDDEAT
AAEQLHDSVC DDDDEEEDSD LDDDAHKLPP QSDERMRRLM AMQDEDFKRR FQRQQRKNGA
SIDYGALPPG VAPGAGSAGP HPDHNRAVFG VSGGVGEGSM RGAYRQQQQQ QQQQLNAKSP
SARLAVNELF GHGNAGPPLP PANQTPAQKR QQLQKLSPQS TTSSSSHTSH SNLQPHPHPL
THQHPHPPQH QQRHLSAMLD ENNTVRCYLE PLAK
