ID LPHN_DROSE Reviewed; 1693 AA.
AC B4HS00;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GM21049;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW46963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW46963.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDW46963.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH480816; EDW46963.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002032950.1; XM_002032914.1.
DR AlphaFoldDB; B4HS00; -.
DR SMR; B4HS00; -.
DR STRING; 7238.B4HS00; -.
DR GlyCosmos; B4HS00; 8 sites, No reported glycans.
DR EnsemblMetazoa; FBtr0204034; FBpp0202526; FBgn0175930.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000001292; Unassembled WGS sequence.
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 CDD; cd22830; Gal_Rha_Lectin_dCirl; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF347; LATROPHILIN CIRL; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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_0000393379"
FT TOPO_DOM 1..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..814
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 815..835
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 836..861
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 883..906
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 907..927
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 928..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..985
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1006
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1693
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 692..739
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 185..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1673
FT /note="Disordered"
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..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1311
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 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1693 AA; 185638 MW; 5E257AD1A98E7557 CRC64;
MLPTILSISY EHISLDLSKY QTAYACEGKK LTIECDPGDV INLIRANYGR FSITICNDHG
NVEWSVNCMF PKSLSVLNSR CAHKQSCGVL AATSMFGDPC PGTHKYLEAH YQCISAAQTS
TTTNRPSPPP WVLSNGPPIF GNGSGLIHPP GVGAGAPPPP RLPTLPGVVG ISGNPGLFNV
PPQHTAVTHS TPWSSTTAVG GGRLKGGATS TTTTKHPAGR HDGLPPPPQL HHHHNHHGED
TASPTKPSSK LPAGGNVTSP SNTRILTGVG GSGTDDGTLL TTKSSPNRPP GTAASGSVAG
NSSVVRTINN INLNAAGMSG GDDESKLFCG PTHARNLYWN MTRVGDVNVQ PCPGGAAGIA
KWRCVLMKRM PDSGYDEYDD DASSTTPAPS GGDCLHNSSS CEPPVSMAHK VNQRLRNFEP
TWHPATPDLT QCRSLWLNNL EMRVNQRDSS LISIANDMSE VTSSKTLYGG DMLVTTKIIQ
TVSEKMMHDK ETFPDQRQRE AMIMELLHCV VKTGSNLLDE SQLSSWLDLN PEDQMRVATS
LLTGLEYNAF LLADTISGSA VWCKKSKIYS SVVFPDTDQW PLSSDRIELP RAALIDNSEG
GLVRIVFAAF DRLESILKPS YDHFDLKSSR SYVRNTAILS NDSDVNAGEI QQRLRILNSK
VISASLGKGR HIQLSQPITL TLKHLKTENV TNPTCVFWNY IDHAWSANGC SLESTNRTHS
VCSCNHLTNF AILMDVVDEH QHSLFTMFDG NMRIFIYISI GICVVFIVIA LLTLKLFNGV
FVKSARTSIY TSIYLCLLAI ELLFLLGIEQ TETSIFCGFI TIFLHCAILS GTAWFCYEAF
HSYSTLTSDE LLLEVDQTPK VNCYYLLSYG LSLSVVAISL VIDPSTYTQN DYCVLMEANA
LFYATFVVPV LVFFVAAIGY TFLSWIIMCR KSRTGLKTKE HTRLASVRFD IRCSFVFLLL
LSAVWCSAYF YLRGAKMDDD TADVYGYCFI CFNTLLGLYI FVFHCIQNEK IRREYRKYVR
QHAWLPKCLR CSKTSISSGI VTGNGPTAGT LCSVSTSKKP KLPLGVSEEA HDDPQQQQQT
PVPITEDAIM GATSDCELNE AQQRRTLKSG LMTGTLQAPT QTLGGHVVLE RGSTLRSTGH
ASPTSSAGST HLIFAHKQQQ QQQQQGPLGE SYYHQPDYYS WKQPSTGTGG LKTPREYYNN
AGAAASSPQQ AHEVFYWTQK PNSGQHGKKK RGAGGVPASP SGSLHSRTAA ASQVLFYPSY
KKTKPGQPTG YPQYAEALDP PLATGNAAAY YQQQQQLRRQ QLHQQQQQLS SDEEQAEQHA
HLLHLQRRAG SQQQLPAPPP HMAQYQQEFM QRQYRNKHSN CDLGMGDAYY NQGSVGGADG
GPVYEEILSN RNSDVQHYEV GDFDVDEVYN NSVGTGVFNN MRAAVAAGGS RYGGGSLSGG
SVSSRSQQQQ LKKQQQQQSL AQQRSVRRCT ADDDDDEDEE EDEEATAAEQ LHDSVCDEDE
EEDESDLEHD AHGLPPQSDE RMRRLMAMQD EDFKRRFQRQ LRKHGAPLDY GALPPGAGPQ
PEHNGAVFGV SGGVGEGSMR GAFRQQQQQQ ALNAKSPGGR LAVNELFGHG NSGPPLPPAN
QTPAQKRQQL QKLSPQSTTS SSSHTSHSNP NLHPHQLTHP HPHQHPPHHQ QRHLSAMLDE
NNTVRCYLEP LAK
//
