LPHN_DROGR
ID LPHN_DROGR Reviewed; 1777 AA.
AC B4J780;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GH20083;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDW02098.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDW02098.1};
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; CH916367; EDW02098.1; -; Genomic_DNA.
DR RefSeq; XP_001987231.1; XM_001987195.1.
DR AlphaFoldDB; B4J780; -.
DR SMR; B4J780; -.
DR STRING; 7222.FBpp0153989; -.
DR MEROPS; P02.A01; -.
DR EnsemblMetazoa; FBtr0470157; FBpp0420233; FBgn0127547.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR InParanoid; B4J780; -.
DR OMA; SMRGAYR; -.
DR OrthoDB; 77744at2759; -.
DR PhylomeDB; B4J780; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000001070; 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..1777
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393374"
FT TOPO_DOM 1..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..940
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 941..961
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1009
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1016
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..134
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 725..772
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 189..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1562
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1777 AA; 194170 MW; C82E7FDE4C4B8918 CRC64;
MYLKNHTLGL RTKASQGAPL AKAAQSLLQL KKLDCVPPKY QTAYACEGKK LTIECEPGDL
INLIRANYGR FSITICNDHG NVEWSVNCMF PKSLTVLNSK CSHKQSCSVL AATSMFGDPC
PGTHKYLEAH YQCISAAQTS TTTNRPSPPP WVLSNGPPIF GNGSGLIQPT PQPPPRLPTL
PGVVGIHGIN GVPPTHATPS SSTAMLPGGR LKGVTSATTK HPGGRHDGLR PPPQLHHHHH
HTDDTAPTKS SSGSAGNVTA PSNTRILTGV GGGGSDDGTL LTTKSSPNRT PGTAASAANN
NSLGIGGTAP GSGGGVVRTI NNINLNAAGM GAEDESKLFC GPTHARNLFW NMTRVGDVNV
QPCPGGAAGI AKWRCVLMKR VPDAGYDEYD DEMPVASSTT PMPPPSSAGG DCLHNSSSCE
PPVSMAHKVN QNQRLRNFEP TWHPLTPDLT QCRSLWLNSL EMRVNQQDSS LISIANDLSE
VTSSKTLYGG DMLVTTKIIQ RMSEKMLHDK GTFPDQRQRE AIIMELLHGV VKTGSNLLDE
SQLSSWLDLN QEDQMRVATS LLTGLEYNAF LLADTIIRER NVVQKVKNIL LSVRVLETKT
IQGNVVFPDS DQWPLSSDRI ELPRTALKEN SEGGLVRIVF AAFDRLESIL KPSYDHFDLK
SARSYVRNTA ILSNDSDTNA GEMQQRVRIL NSKVISASLG KGRHIQLSQP IKLVLKHLKT
ENVSNPTCVF WNYIDHAWSA NGCSLESTNR THSVCSCNHL TNFAILMDVV DEHQHSLFTM
FDGNMRIFIY ISVAICVVFI IIALLTLKLF NGVFVKSART SIYSSIYICL LAIELLFLLG
IEQTETSIFC GFITVFLHCA ILSGTAWFCY EAFHSYSTLT SDELLLEVDQ TPKVNCYYLL
SYGLSLSVVA ISLGINPSTY TLRNDYCVLM EANALFYVTF VAPILIFFVA AISYTFLSWI
IMRRKSRTAL KTKEHTRLAN VRFDIRCSFV FLLLLSADWC CAYFYLRGAK LDEDVAAIYG
YCFVCFNTLM GLYIFVFHCI QNEKIRREYR KYVRQHAWLP KCLRCSKTSI SSGIVSGNGG
PGGVSGGVAT NSAGTLSKSK SKLPLGSSDD GHDEEQPHQQ QHQHDQPANE DAIIMGAGSD
CELSEAQQRR TLKSGLLAGS LQPVTPVGAV VLERGTLRST GMASVGHASP TSSAGSTHLI
FAHKHQQQLQ QQPGESYYHQ PDYYSWKHPQ AGGQREYYNN TGVPGGGGGV GVGGASPQQS
HEVFYWTQKH NNQHGKKKRG GGAGAVPASP SGSLHSRVTP ASQVLFYPSY KKTSGMKQPP
PSAQQAYPHY AEALDPPNNA AYYQQQLQQQ QQLRQQRQQQ QQQQLSSDEE QAHLLHLQHQ
QRRAGGQQQL PAPPPHMAQY QQELLAQQQR QQYRNKHSNC DLSQGIGLGM NMGMGQGLGG
DAYYNQGGGG SSNGGGVGGD GPVYEEILSN RNSDAQHYEV GDFDVDEVYN NSVGTGVFNS
MRAAVAAGGS RYGGGSLSGG SVTSRNQQQQ LQAKQKQPPR RCAADDDDDD DDDDDEYDDE
VTAAEQLHDS VCDDEDNESD MDDDDTHGLP PQSDERMRRL MALQDEDFKR RFQRQQRKNG
LPLDYGAPPQ TSAGATIAHP IEHNGAVFGV SGGVGEGSMR GAYRQQQQQL NAKSPSARLA
VNELFGHGNA GPPLPPANQT PAQKRQQLQK LSPQSTTSSS SHTSHSNLQQ HSAPTHHHLQ
HQQPQLHHHQ QQQQARNLSA MLDENNTVRC YLEPLAK
