LPHN_DROYA
ID LPHN_DROYA Reviewed; 1707 AA.
AC B4P3A0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GE19213;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW89373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW89373.1};
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; CM000157; EDW89373.1; -; Genomic_DNA.
DR RefSeq; XP_002089661.2; XM_002089625.2.
DR AlphaFoldDB; B4P3A0; -.
DR SMR; B4P3A0; -.
DR STRING; 7245.FBpp0264223; -.
DR MEROPS; P02.A01; -.
DR GeneID; 6528618; -.
DR KEGG; dya:Dyak_GE19213; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR OMA; SMRGAYR; -.
DR PhylomeDB; B4P3A0; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000002282; Chromosome 2L.
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..1707
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393381"
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..1707
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 176..301
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 1169..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..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..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1668
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 1255
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 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1328
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 1707 AA; 187305 MW; D4B6B8CF22AB431C CRC64;
MLPTILSISY EHTYAYLSKY QTAYACEGKK LTIECEPGDV INLIRANYGR FSITICNDHG
NVEWSVNCMF PKSLSVLNSR CAHKQSCGVL AATSMFGDPC PGTHKYLEAH YQCISAAQTS
TTTNRPSPPP WVLSNGPPIF GNGSGLIHPP GVGAGAPPPP RLPTLPGVVG ISGNPGLFNV
PPQHTAVTHS TPSSSTTAVG GGRLKGVPTS TTTTKHPAGR HDGLPPPPQL HHHHNHHGDD
TATPTKPSSK LPAGGNATSP SNTRILTGVG GSGTDDGTLL TTKSSPNRPP GTAASGAVVP
GNGSVVRTIN NINLNAAGIS GGDDESKLFC GPTHARNLYW NMTRVGDVNV QPCPGGAAGI
AKWRCVLMKR MPDSGYDEYD DDPSSTTPAP NGGDCLHNSS SCEPPVSMAH KVNQRLRNFE
PTWHPATPDL 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 VIPVLVFFVA AIGYTFLSWI ILCRKSRTGL KTKEHTRLAS
VRFDIRCSFV FLLLLSAVWC SSYFYLRGAK MDDDTADVYG YCFICFNTLL GLYIFVFHCI
QNEKIRREYR KYVRQHAWLP KCLRCSKTSI SSGIVTGNGP TAGTLCSVST SKKPKLPLGV
SEEAHDDPQQ QQHTPVPITE DAIMGASSDC ELNEAQQRRT LKSGLMTGTL QAPPQTLGGH
VVLERGSTLR STGHASPTSS AGSTHLIFAH KQQQQQQQQQ QGPLGEGYYH QPDYYSWKQP
PTGTGGLKTP REYYNNTGAS ASSPQQAHEV FYWTQKPNSG QHGKKKRGAG GVPASPSGSL
HSRTAAASQV LFYPSYKKTK AGQPTGYPQY AEALDPPLAT GNAAAYYQQQ QQLRRQQLHQ
QQQQQLSSDE EQVEQHAHLL HLQRRAGSQQ QLPAPPPHMA QYQHEFMQRQ YRNKHSNCDL
GMGDAYYNQG SVGGADGGPV YEEILSNRNS DVQHYEVGDF DVDEVYNNSV GTGVFNNMRA
AVAAGGSRYG GGSLSGGSVS SRSQQQQLKK QQQQQSLAQQ RSARRCTADD DDDEEEEEDE
EATAAEQLHD SVCDEDEEED ESDLEDDAHG LPPQSDERMR RLMAMQDEDF KRRFQRQLRK
HGAPLDYGAL PPGSGPQPEH NGAVFGVSGG VGEGSMRGAF RQQQALNAKS PGGRLAVNDL
FGHGNSGPPL PPANQTPAQK RQQLQKLSPQ STTSSSSHTS HSNPNPHPLQ LTHPHPHQHP
PHHQQRHLSA MLDENNTVRC YLEPLAK
