ID G1KL00_ANOCA Unreviewed; 1477 AA.
AC G1KL00;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Adhesion G protein-coupled receptor L1 {ECO:0008006|Google:ProtNLM};
GN Name=adgrl1 {ECO:0000313|Ensembl:ENSACAP00000011003.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011003.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000011003.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011003.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000011003.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_008102814.1; XM_008104607.2.
DR STRING; 28377.ENSACAP00000011003; -.
DR MEROPS; P02.010; -.
DR Ensembl; ENSACAT00000011231.4; ENSACAP00000011003.4; ENSACAG00000010837.4.
DR GeneID; 100554478; -.
DR CTD; 22859; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000159684; -.
DR HOGENOM; CLU_002753_1_1_1; -.
DR OrthoDB; 1114672at2759; -.
DR TreeFam; TF351999; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000010837; Expressed in testis and 9 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016524; F:latrotoxin receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR CDD; cd16007; 7tmB2_Latrophilin-1; 1.
DR CDD; cd22844; Gal_Rha_Lectin_LPHN1; 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; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR031234; Latrophilin-1_TM.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 1.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1477
FT /note="Adhesion G protein-coupled receptor L1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032287035"
FT TRANSMEM 855..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 962..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1045..1068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..130
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 140..399
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 478..537
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 857..1098
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1287..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 141..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1477 AA; 164469 MW; A9B2CD68289A2834 CRC64;
MARLIHALWS LCITTVLVTS ATQAGLSRAG LPFGLVRREL ACEGYPIELR CPGSDVIMVE
NANYGRTDDK ICDADPFQME NVQCYLPDAF KIMSQRCNNR TQCVVVAGSD AFPDPCPGTY
KYLEVQYDCV PYKVEQKVFV CPGTLHKILE PTSAHESEHQ SGAWCKDPLQ AGDRIYVMPW
IPYRTDTLTE YASWEDYVGA RHTTTYRLPN RVDGTGFVVY DGAVFYNKER TRNIIKYDLR
TRIKSGETVI NTANYHDTSP YRWGGKTDID LAVDENGLWV IYATEGNNGR LVVSQLNPYT
LRFENTWETG YDKRSASNAF MVCGVLYVVR TVYVDDDSEA AGNRVDYAFN TNMNREEPIS
LTFPNPYQFI SSIDYNPRDN QLYVWNNYFV LRYSLEFGPP DPSTGPVTST PLSTTTTTHL
TTVTSTISSA ATTTTRQAPL TTHPIGAINQ KGTELHPVTA VLPSTRRPPA NNQHLSPELF
CEAKEVRRVQ WPATQQGMLV ERPCPKGTRG IASFQCLATL GIWNPRGPDL SNCTSPWVNQ
VAQKIKSGEN AANIASELAR HTRGAIYAGD VSSSVKLMEQ LLDILDAQLQ ALRPIERESA
GKNYNKMHKR ERTCKDYIKA VVETVDNLLR PEALESWKDM NATEQVHTAT MLLDILEEGA
FLLADNVKEP ARFVTAKNNV VLEVSVLNTE GQVPDIVFPH DHTTRNSIQL SANTIKQNSR
NGVVKVVFIL YNNLGFFLST ENATIKLGSE IGPLSPSLVV NSQVIAASIN KESSRVFLMD
PVIFTLSHLE DKNHFNANCS FWNYSERSMM GYWSTQGCRL VETNKTHTTC ACSHLTNFAV
LMAHREIYQG RINELLLSVI TWVGIVISLV CLAICISTFC FLRGLQTDRN TIHKNLCINL
FITELLFLIG IDKTQYEIAC PIFAGLLHYF FLAAFSWMCL EAIHLYLMLV EVFESEYSRK
KYYYLGGYCF PALVVGIAAA IDYRSYGTEK ACWLRVDNYF IWSFIGPVSF VIVINLVFLM
ITLHKMIRNT SVLKPDSSRL DNIKSWALGA ITLLFLLGLT WAFGLLFINK ESIVMAYLFT
TFNAFQGMFI FVFHCALQKK VHREFSKCLR HASCCLRSPP GATLGSLKTS AIRSNNRYYT
GTQSRIRRMW NDTVRKQTES SFMAGDLNST PTLNRGTMGN HLLTNPVLQT RGGTSPYNTL
IAESVGFNPA SPPVFNSPEH PLNNSRDACG MDTLPLNGNF NNSYSLRSGD FSADGTKMAD
CRRNLNDAAA FEKMIISELV HNNLRGGGSG VVKGGGGSTE TSNPPGPPPP PSVGAGGGGT
NNEDDAIVPD APSLTHEENM EIELMYKALE EPLLLQRAQS ILYQSDLEES ESCTADLTEG
GDGQAPSPNR DSLYTSMTNL RDSPYPDSSP EAVGEVLPHA QAINEIYYTN RPALVPRNQL
QAYYQVRRPS NDGYLVPGSL ENPAVEGDGQ MQLVTSL
//
