LPHN_DROER
ID LPHN_DROER Reviewed; 1710 AA.
AC B3N8M1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GG23370;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV59498.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV59498.1};
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; CH954177; EDV59498.1; -; Genomic_DNA.
DR RefSeq; XP_001970439.2; XM_001970403.2.
DR AlphaFoldDB; B3N8M1; -.
DR SMR; B3N8M1; -.
DR STRING; 7220.FBpp0141916; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR OMA; SMRGAYR; -.
DR PhylomeDB; B3N8M1; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000008711; 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:0008344; P:adult locomotory behavior; IEA:EnsemblMetazoa.
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; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..1710
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393373"
FT TOPO_DOM 1..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 876..896
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 897..920
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..968
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 969..989
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 990..999
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1000..1020
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..114
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 706..753
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 183..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1710 AA; 187803 MW; 31A7270A455DC2F1 CRC64;
MLPTILSISY EHTYAYLSKY QTAYACEGKK LTIECEPGDV INLIRANYGR FSITICNDHG
NVEWSVNCMF PKSLSVLNSR CAHKQSCGVL AATSMFGDPC PGTHKYLEAH YQCISAAQTS
TTTNRPSPPP WVLSNGPPIF GNGSGLIHPP GIGAGAPPPP RLPTLPGVVG ISGNPGLFNV
PPQHTAVTHS TPSSSTTAMA GGRLKGVATS TTTTKHPAGR HDGLPPPPQL HHHHNHHGED
TASPTKPSSK LPAGGNATSP SNTRILTGVG GSGTDDGTLL TTKSSPNRTP GTAASGSVVP
GNGSVVRTIN NINLNSAGMS GGDDESKLFC GPTHARNLYW NMTRVGDVNV QPCPGGAAGI
AKWRCVLMKR MPDSGYDEYD DDPSSTTPAT SSADCLHNSS SCEPPVSMAH KVNQRLRNFE
PTWHPTTPDL TQCRSLWLNN LEMRVNQRDS SLISIANDMS EVTSSKTLYG GDMLVTTKII
QTVSEKMLHD KETFPDQRQR EAMIMELLHC VVKTGSNLLD ESQLSSWLDL NPEDQMRVAT
SLLTGLEYNA FLLADTIIRE RSVVQKVKNI LLSVRVLETK TIQSSVVFPD SDQWPLSSDR
IELPRAALID NSEGGLVRIV FAAFDRLESI LKPSYDHFDL KSSRSYVRNT AILSNDSDVN
AGEIQQRLRI LNSKVISASL GKGRHIQLSQ PITLTLKHLK TENVTNPTCV FWNYIDHAWS
ANGCSLESTN RTHSVCSCNH LTNFAILMDV VDEHQHSLFT MFDGNMRIFI YISIGICVVF
IVIALLTLKL FNGVFVKSAR TSIYTSIYLC LLAIELLFLL GIEQTETSIF CGFITIFLHC
AILSGTAWFC YEAFHSYSTL TSDELLLEVD QTPKVNCYYL LSYGLSLSVV AISLVIDPST
YTQNDYCVLM EANALFYATF VMPVLVFFVA AIGYTFLSWI IMCRKSRTGL KTKEHTRLAS
VRFDIRCSFV FLLLLSAVWC SAYFYLRGAK MDDDTADVYG YCFICFNTLL GLYIFVFHCI
QNEKIRREYR KYVRQHAWLP KCLRCSKTSI SSGIVTGNGP TAGTLCSVST SKKPKLPIGV
SEEAHDDPQQ QQQTPVPITE DAIMGASSDC ELNEAQQRRT LKSGLMTGTL QAPPQTLGGH
VVLERGSTLR STGHASPTSS AGSTHLIFAH KQQQQQQQQG PLGESYYHQP DYYSWKQPPT
GTGGLKTPRE YYNNTGAAAS SPQQAHEVFY WTQKPNSGQH GKKKRGAGGV PASPSGSLHS
RTAAASQVLF YPSYKKTKAG QPTGYPQYAE ALDPPLATGN AAAYYQQQQQ LRRQQLHLQQ
QQQQQQQLSS DEEQVEQHAH LLQLQRRAGS QQQLPAPPPH MAQYQQEFMQ RQYRNKQSNC
DLGMGDAYYN QGSVGGADGG PVYEEILSNR NSDVQHYEVG DFDVDEVYNN SVGTGVFNNM
RAAVAAGGSR YGGGSLSGGS VSSRSQQQQL KKQQQQQSLA QQRSARRCTA DDDDDEDEEE
DEEATAAEQL HDSVCDEDEE EDESDLEDDA HGLPPQSDER MRRLMAMQDE DFKRRFQRQL
RKHGAPLDYG ALPPGAGPQP EHNGAVFGVS GGVGEGSKRG AFRQQQQALN AKSPGGRLAV
NDLFGHGNSG PPLPPANQTP AQKRQQLQKL SPQSTTSSSS HTSHSNPNPH PHQLTHPHPH
QHPPHHQQRH LSAMLDENNT VRCYLEPLAK
