ID A0A287DF55_ICTTR Unreviewed; 1468 AA.
AC A0A287DF55;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000313|Ensembl:ENSSTOP00000032165.1};
GN Name=ADGRL1 {ECO:0000313|Ensembl:ENSSTOP00000032165.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000032165.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000032165.1}
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 EMBL; AGTP01088522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01088523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005336303.1; XM_005336246.1.
DR Ensembl; ENSSTOT00000033517.1; ENSSTOP00000032165.1; ENSSTOG00000024713.2.
DR GeneID; 101969905; -.
DR CTD; 22859; -.
DR GeneTree; ENSGT00940000159684; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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:UP000005215};
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..1468
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011608154"
FT TRANSMEM 852..879
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 998..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..129
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 472..531
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 854..1095
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 395..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1468 AA; 161741 MW; 4F2C999C3B1C0159 CRC64;
MARLAAVLWS LCVTAVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YIFVCPGTLQ KVLEPTSTHE SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD
TLTEYASWED YVAARHTTTY RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
ETVINTANYH DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRMVVSQL NPYTLRFEGT
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE EPVSLAFPNP
YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP ATSPPLSTTT AARPTPLTST
ASPAATTPLR RAPLTTHPVG AINQLGPDLP PATAPAPSTR RPPAPNLHVS PELFCEPREV
RRVQWPATQQ GMLVERPCPK GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK
SGENAANIAS ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL EEGAFLLADN
VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN SIQLSANTIK QNSRNGVVKV
VFILYNNLGL FLSTENATVK LAGEAGTGGP GGASLVVNSQ VIAASINKES SRVFLMDPVI
FTVAHLEAKN HFNANCSFWN YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA
HREIYQGRIN ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA
ELLFLVGIDK TQYEIACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF ESEYSRTKYY
YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS FIGPVSFVIV VNLVFLMVTL
HKMIRSSSVL KPDSSRLDNI KSWALGAIAL LFLLGLTWAF GLLFINKESV VMAYLFTTFN
AFQGVFIFVF HCALQKKVHK EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ
SRIRRMWNDT VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE
SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS GDFPPGDGGP
EPPRGRNLAD AAAFEKMIIS ELVHNNLRGS SSGAKGPPPP EPPVPPVPGG GGEEEAGGPG
GADRAEIELL YKALEEPLLL PRAQSVLYQS DLDESESCTA EDGATSRPLS SPPGRDSLYA
SGANLRDSPS YPDSSPEGPS EALPPPPPAP PGPPEIYYTS RPPALVARNP LQGYYQVRRP
SHEGYLAAPG LEGPGPDGDG QMQLVTSL
//
