ID LPHN_DROMO Reviewed; 1725 AA.
AC B4KMZ1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Latrophilin Cirl {ECO:0000250|UniProtKB:A1Z7G7};
GN Name=Cirl {ECO:0000250|UniProtKB:A1Z7G7}; ORFNames=GI18798;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW09913.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW09913.1};
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; CH933808; EDW09913.1; -; Genomic_DNA.
DR RefSeq; XP_002005978.2; XM_002005942.2.
DR RefSeq; XP_015019584.1; XM_015164098.1.
DR AlphaFoldDB; B4KMZ1; -.
DR SMR; B4KMZ1; -.
DR MEROPS; P02.A01; -.
DR GlyCosmos; B4KMZ1; 8 sites, No reported glycans.
DR EnsemblMetazoa; FBtr0424176; FBpp0382054; FBgn0141537.
DR GeneID; 6580110; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_003272_0_0_1; -.
DR InParanoid; B4KMZ1; -.
DR OMA; NMRVFIY; -.
DR OrthoDB; 1114672at2759; -.
DR PhylomeDB; B4KMZ1; -.
DR ChiTaRS; Cirl; fly.
DR Proteomes; UP000009192; 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..1725
FT /note="Latrophilin Cirl"
FT /id="PRO_0000393376"
FT TOPO_DOM 1..757
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 758..778
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 779..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 813..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..910
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 959..979
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..986
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 987..1007
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1008..1725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..107
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 696..743
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 164..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1153
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 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z7G7"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1725 AA; 188674 MW; 6D286D2E83BAE0AE CRC64;
MALNELGNCA PKYQTAYACE GKQLTIECEP GDLINLIRAN YGRFSITICN DHGNVEWSVN
CMFPKSLTVL NSKCSHKQSC SVLAATSMFG DPCPGTHKYL EAHYQCISAA QTSTTTNRPS
PPPWVLSNGP PIFGNGSGLI QVPPPLPPRL PSLPGVVGIH GINAVQPTHS TPSSSTAALP
GGRLKGVTSA TTKHPGGRHD GLPPPPQLHH HHHHTDETVP TKPSSSSSSN SGSAGNVTSP
SNTRILTGVG GAGSDDGTLL TTKSSPNRTP GTTASAANNS VNIGGAGTGS VVRTINNINL
NAAGMGTDDE SKLFCGAMHA RNLFWNMTRV GDVNVQPCPG GAAGIAKWRC VLMKRLPDSG
DDEYDDDLPA ASSTTPQPSN NGGDCVHNSS SCEPPVSMAH KVNQRLRNFE PTWHPLTPDL
TQCRSLWLNS LEMRVNQRDS SLTSIANDLS EVTSSKTLYG GDMLVTTKII QTMSEKMLHD
KETFPDQRQR EAIIMELLHG VVKTGSNLLD ESQLSSWLDL NPEDQMRVAT SLLTGLEYNA
FLLADTIIRE RNVVQKVKNI LLSVRVLETK TIHGSVVFPD SDQWPLSSDR IELPRTALLE
NSEGGLVRIV FAAFDRLESI LKPSYDHFDL KSARSYVRNT AILSNDSDAA TGDMQQRIRI
LNSKVISASL GKGRHIQLSQ PITLVLKHLK TENVSNPTCV FWNYIDHAWS ANGCSLESTN
RTHSVCSCNH LTNFAILMDV VDEHQHSLFT MFDGNMRIFI YISVAICVVF IIIALLTLKL
FNGVFVKSAR TSIYSSIYIC LLAIELLFLL GIEQTETSIF CGFITVFLHC AILSGTAWFC
YEAFHSYSTL TSDELLLEVD QTPKVNCYYL LSYGLSLSVV AISLVIDPST YTQNDYCVLM
EANALFYSTF VAPVLIFFVA AITYTFLSWI IMRRKSRTAL KTKEHTRLAN VRFDIRCSFV
FLLLLSVVWC CAYFYLRGAK LDEDGAPIYG YCFICFNTLL GIYIFVFHCI QNEKIRREYR
KYVRQHAWLP KCLRCSKTSI SSGVVAGNGG PGVGNTANQS AGTLSKSKSK LPLGAGDEAR
DGDAQQQQHD LPAAEDAIIM GAGSDCELNE AQQRRTLKSG LLTGSLQPAP VGAVVLERNT
LRSTGMASVG HASPTSSAGS THLIFAHKQQ QQQQQQLQQP GETYYHQPDY YSWKHPPGGQ
REYYNNAGGA VGAAVGGVGG ASPQQAHEVF YWTQKHNNQH GKKKRGGGAG AVPASPSGSL
HSRATATSQV LFYPSYKKTT GMKQGPPPQQ AYPHYAEALD PPNAAYYQQQ LQQQQLRQQR
QQQQQQLSSD EEQAEQHAHL LHLQHQQRRV GGQQLPAPPP HMAQYQQELL AQQQRQQYRN
KHSNCDLSQG MGLGINMGMG HGDAYYNQGG SSNGGGDAGG PVYEEILSNR NSDVQHYEVG
DFDVDEVYNN SVGTGVFNNM RAAVAAGGSR YGGGSLSGGS VTSRSQQQQQ QQLKQKQPPR
RCAADDDDDD DDDDDEYDDE VTAAEQLHDS VCDDEDNESD IDDDTHGLPP QSDERMRRLM
ALQDEDFKRR FQRQQRKNGM PLDYGASVQS AAAAHPDHNG AVFGVSGGVG EGSMRGAYRQ
QQTAKSPNAR LAVNELFGHG NAGPPLPPAN QTPAQKRQQL QKLSPQSTTS SSSHTSHSNP
QHAPAHHLQH HHTQQQQQQQ QQARHLSAML DENNTVRCYL EPLAK
//
