LPHN_DROVI
ID LPHN_DROVI Reviewed; 1724 AA.
AC B4LNA8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-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=GJ21826;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW61060.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW61060.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH940648; EDW61060.1; -; Genomic_DNA.
DR RefSeq; XP_002049867.2; XM_002049831.2.
DR AlphaFoldDB; B4LNA8; -.
DR SMR; B4LNA8; -.
DR STRING; 7244.FBpp0236243; -.
DR PRIDE; B4LNA8; -.
DR EnsemblMetazoa; FBtr0436972; FBpp0393832; FBgn0208944.
DR GeneID; 6625650; -.
DR KEGG; dvi:6625650; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR InParanoid; B4LNA8; -.
DR OMA; SMRGAYR; -.
DR OrthoDB; 77744at2759; -.
DR PhylomeDB; B4LNA8; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000008792; 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; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1724
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393380"
FT TOPO_DOM 1..771
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..792
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..826
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 827..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..924
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 925..945
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 946..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..1000
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1001..1021
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..124
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 710..757
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 152..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
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 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1724 AA; 189389 MW; 7D5253739D4F4D66 CRC64;
MGLHFYECNL SVQRKRVCSL EKRQMKAPKY QTAYACEGKK LTIECEPGDL INLIRANYGR
FSITICNDHG NVEWSVNCMF PKSLTVLNSK CSHKQSCSVL AATSMFGDPC PGTHKYLEAH
YQCISAAQTS TTTNRPSPPP WVLSNGPPIF GNGSGLIQAP PPPPPRLPSL PGVVGIHGIN
AVPPTHSTPS SSTATLPGGR LKGVTSATTK HPGGRHDGLP PPPQLHHHHH HTDETVPTKS
SSSGSTGNVT SPSNTRILTG VGGAGSDDGT LLTTKSSPNR TPGTVASTTN SSLSIGGTGA
GGVVRTINNI NLNAAGMGTD DESKLFCGPT HARNLFWNMT RVGDVNVQPC PGGAAGIAKW
RCVLMKRLPD AGYDEYDDDL PVASSTTPIP PSSAGDCLHN SSSCEPPVSM AHKVNQNQRL
RNFEPTWHPL TPDLTQCRSL WLNSLEMRVN QRDSSLISIA NDLSEVTSSK TLYGGDMLVT
TKIIQTMSEK MLHDKETFPD QRQREAIIME LLHGVVKTGS NLLDESQLSS WLDLNPEDQM
RVATSLLTGL EYNAFLLADT IIRERNVVQK VKNILLSVRV LETKTIHGSV VFPDSDQWPL
SSDRIELPRS ALIENSEGGL VRIVFAAFDR LESILKPSYD HFDLKSARSY VRNTAILSND
SDAATGDMQQ RIRILNSKVI SASLGKGRHI QLSHPITLVL KHLKTENVSN PTCVFWNYID
HAWSVNGCSL ESTNRTHSVC SCNHLTNFAI LMDVVDEHQH SLFTMFDGNM RIFIYISVAI
CVVFIIIALL TLKLFNGVFV KSARTSIYSS IYICLLAIEL LFLLGIEQTE TSIFCGFITI
FLHCAILSGT AWFCYEAFHS YSTLTSDELL LEVDQTPKVN CYYLWSYGLS LTVVAISLAI
NPSTYTQNDY CVLMEANALF YATFVAPILI FFVAAIGYTF LSWIIMRRKS RTTLKTKEHT
RLANVRFDIR CSFVFLLLLS AVWCCAYFYL RGAKLDEEVA TVYGYCFICF NTMLGLYIFV
FHCIQNEKIR REYRKYVRQH AWLPKCLRCS KTSISSGVVA GNGGPGVGNV ANNSAGTLSK
SKSKLPLSAT DEARAVEQQQ QQKDVPAADD AIIMGAGSDS ELNEAQQRRT LKSGLLTGSL
QPTPVGAVVL ERGTLRSTGM ASVGHASPTS SAGSTHLIFA HKQQQQLQQP GEAYYHQPDY
YSWKHPQAGQ REYYNNTGVT ANAGIGGASP SQAHEVFYWT QKHNNQHGKK KRGGNAGAVP
ASPSGSLHSR VTAASQVLFY PSYKKTSGLK QPPATQAYPH YAEALDPPNA AYYQQQLQQQ
QLRQQRQQQQ QQLSSDEEQA EQHAHLLHLQ HQQRRAGGPQ LPAPPPHMAQ YQQELLAQQQ
RQQYRNKHSN CDLSQGMGLG KGMGMVLGDA YYNQGGSSNG GGDGGPVYEE ILSNRNSDGQ
HYEVGDFDVD EVYNNSVGTG VFNSMRAAVA AGGNRYCGGS LSGGSVTSRN QQQQQKQKQP
PRRCVADDDD DDDDDEYDDE VTAAEQLHDS VCDDEDNDSD IDDDTHGLPP QSDERMRRLM
ALQDEDFKRR FQRQQRKNGL PLDYGASAQT ASINHPEHNG AVFGVSGGVG EGSMRGAYRQ
QQQQNAKSPS ARLAVNELFG HGNAGPPLPP ANQTPAQKRQ QLQKLSPQST TSSSSHTSHS
NPQHAPAHHI QHQQHHQQQQ QARHLSAMLD ENNTVRCYLE PLAK
