LPHN_DROPE
ID LPHN_DROPE Reviewed; 1684 AA.
AC B4GD14;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GL10904;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW31552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49 {ECO:0000312|EMBL:EDW31552.1};
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; CH479181; EDW31552.1; -; Genomic_DNA.
DR RefSeq; XP_002015662.1; XM_002015626.1.
DR AlphaFoldDB; B4GD14; -.
DR SMR; B4GD14; -.
DR STRING; 7234.FBpp0175011; -.
DR MEROPS; P02.A01; -.
DR EnsemblMetazoa; FBtr0176519; FBpp0175011; FBgn0148514.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR OMA; SMRGAYR; -.
DR PhylomeDB; B4GD14; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000008744; 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..1684
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393377"
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..918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..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..1684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..110
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 181..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1652
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 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
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 1684 AA; 184820 MW; DE6C7655A36AB35A CRC64;
MASNNYIQIM EKAPKYQTAY ACEGKKLTIE CEQGELINLI RANYGRFSIT ICNDHGNVEW
SVNCMFPKSL TVLNSRCAHK NSCSVLAATS MFGDPCPGTH KYLEAHYQCV SAAQTSTTTN
RPSPPPWVLN NGPPIFGNGS GLIHPTNIGG GSGGASAPPR LPTLPGVVGI NGNGGMFNIP
PPATHATPPG STATLPGGRL KGVATSTTTT KHPAGRRDGL PPPPQLHHHH NHHTDETTPT
KPSGKVPAAS NATAPSNTRI LTGVGGGGTD DGTLLTTKSS PNRTPGTAAS GPSVSSNGSA
VRTINNINLN AAGMAGADDE TKLFCGPTHA RNLFWNMTRV GDVNVQPCPG GAAGIAKWRC
VLMKRMPDSS FDEDDEEMAG TSTTTPMSTS SDCLYNSSSC EPPVTMAHKV NQRLRNFEPT
WHPLTPDLTQ CRSLWLNNLE MRVNQRDSSL ISIANDMSEV TSSKTLYGGD MLVTTKIIQT
VSEKMLHDKE TFPDQRQREA MIMELLHCVV KTGSNLLDES QLSSWLDLNP EDQMRVATSL
LTGLEYNAFL LADTIIRERS VVQKVKNILL SVRVLETKTI QSSVVFPDSD QWPISSDRIE
LPRAALIENS EGGLVRIVFA AFDRLESILK PSYDHFDLKS SRSYVRNTAI LTNDSDASAG
DLQQRLRILN SKVISASLGK GRHIQLSQPI TLTLKHLKTE NVTNPTCVFW NYIDHAWSAN
GCSLESTNRT HSVCSCNHLT NFAILMDVVD EHQHSLFTMF DGNMRIFIYI SIAICVVFIV
IALLTLKLFN GVFVKSARTS IYINIYICLL AIELLFLLGI EQTETSIFCG FITVFLHCAI
LSGTSWFCYE AFHSYSTLTS DELLLEVDQT PKVNCYYLLS YGLSLSVVAI SLVINPSTYT
QNDYCVLMEA NAVFYATFVA PVLIFFMAAI GYTFLSWIIM CRKSRTGLKT KEHTRLATVR
FDIRCSFVFF LLLSAVWCSA YFYLRGAKMD EDVTGIYGYN FICFNTLLGL YIFVFHCIQN
EKIRREYRKY VRQHAWLPKC LRCSKTSISS GIVAGGGTGL GGTNAGTLCS VSTAKKSKLP
LGTNDDAHDE QQQQQHMSAT EDAIMGASSD CELNEAQQRR TLKSGLITGT LQPSQSLGGH
VVLERGNTLR STGHASPTSS AGSTHLIFAH KPQQQQPPLG EAYYHQPDYY SWKQTAGGMK
AQREYYNNAG AATSSPQQAH EVFYWTQKPN SQHGKKKRGG VGAIPASPSG SLHSRATAAS
QVLFYPSYKK TKPGQQAHPH YAEALDPPQP PNTAAYYQQQ QQLRQQRQQQ QQQLSSDEEQ
AEQHAHLLHL QHQQQQQQQR RAGGQQQLPA PPPHMAQYQQ EFMQRQYRNK HSNCDLGDAY
YNQGSVGGAD GGPVYEEILS NRNSDAQHYE VGDFDVDEVY NNSVGTGVFN NMRAAVAAGG
SRYGGSLSGG SVSSRNQQQQ QHSLAQPISA RRCTADEDDD EDEDDEETTA AEQLHDGVCD
EEEEDEESDM EDDSHGLPPQ SAERMRRLMA LQDEDFKRRF QRQQRKHGAP VDYGTLPPGS
AQAVIGGAHP EHNGAVFGVS GGVGEGSMRG ALRQQHAKSP SARLAVNELF GHGNTGPPLP
PANQTPAQKR QQLQKLSPQS TTSSSSHTSH SNPHSHPPHH QQRHLSAMLD ENNTVRCYLE
PLAK
