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Database: UniProt
Entry: A0A2I3TIR5_PANTR
LinkDB: A0A2I3TIR5_PANTR
Original site: A0A2I3TIR5_PANTR 
ID   A0A2I3TIR5_PANTR        Unreviewed;      1477 AA.
AC   A0A2I3TIR5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000313|Ensembl:ENSPTRP00000089146.1};
GN   Name=ADGRL1 {ECO:0000313|Ensembl:ENSPTRP00000089146.1,
GN   ECO:0000313|VGNC:VGNC:6609};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000089146.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000089146.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000089146.1}
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; AACZ04031471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPTRT00000080887.1; ENSPTRP00000089146.1; ENSPTRG00000010588.6.
DR   VGNC; VGNC:6609; ADGRL1.
DR   GeneTree; ENSGT00940000159684; -.
DR   InParanoid; A0A2I3TIR5; -.
DR   Proteomes; UP000002277; Chromosome 19.
DR   Bgee; ENSPTRG00000010588; Expressed in dorsolateral prefrontal cortex and 19 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:UP000002277};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        850..877
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        889..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        921..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        957..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        996..1019
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1040..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1069..1092
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..119
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          131..390
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          469..528
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          852..1093
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          392..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1363..1432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1454..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1407..1427
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        132..314
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1477 AA;  162882 MW;  553D01EDBD680999 CRC64;
     TTGVLTPSPT LPAGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN ANYGRTDDKI
     CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK YLEVQYDCVP
     YKVEQKGKLF VCPGTLQKVL EPTSTHESEH QSGAWCKDPL QAGDRIYVMP WIPYRTDTLT
     EYASWEDYVA ARHTTTYRLP NRVDGTGFVV YDGAVFYNKE RTRNIVKYDL RTRIKSGETV
     INTANYHDTS PYRWGGKTDI DLAVDENGLW VIYATEGNNG RLVVSQLNPY TLRFEGTWET
     GYDKRSASNA FMVCGVLYVL RSVYVDDDSE AAGNRVDYAF NTNANREEPV SLTFPNPYQF
     ISSVDYNPRD NQLYVWNNYF VVRYSLEFGP PDPSAGPATS PPLSTTTTAR PTPLTSTASP
     AATTPLRRAP LTTHPVGAIN QLGPDLPPAT APVPSTRRPP APNLHVSPEL FCEPREVRRV
     QWPATQQGML VERPCPKGTR GIASFQCLPA LGLWNPRGPD LSNCTSPWVN QVAQKIKSGE
     NAANIASELA RHTRGSIYAG DVSSSVKLME QLLDILDAQL QALRPIERES AGKNYNKMHK
     RERTCKDYIK AVVETVDNLL RPEALESWKD MNATEQVHTA TMLLDVLEEG AFLLADNVRE
     PARFLAAKEN VVLEVTVLNT EGQVQELVFP QEEYPRKNSI QLSAKTIKQN SRNGVVKVVF
     ILYNNLGLFL STENATVKLA GEAGPGGPGG ASLVVNSQVI AASINKESSR VFLMDPVIFT
     VAHLEDKNHF NANCSFWNYS ERSMLGYWST QGCRLVESNK THTTCACSHL TNFAVLMAHR
     EIYQGRINEL LLSVITWVGI VISLVCLAIC ISTFCFLRGL QTDRNTIHKN LCINLFLAEL
     LFLVGIDKTQ YEIACPIFAG LLHYFFLAAF SWLCLEGVHL YLLLVEVFES EYSRTKYYYL
     GGYCFPALVV GIAAAIDYRS YGTEKACWLR VDNYFIWSFI GPVSFVIVVN LVFLMVTLHK
     MIRSSSVLKP DSSRLDNIKS WALGAIALLF LLGLTWAFGL LFINKESVVM AYLFTTFNAF
     QGVFIFVFHC ALQKKVHKEY SKCLRHSYCC IRSPPGGTHG SLKTSAMRSN TRYYTGTQPE
     RWGVAWPRRQ RVGGPRIPSH LGNRRSPPSW RVTSTVRRHP SASGFSTMGN HLLTNPVLQP
     RGGTSPYNTL IAESVGFNPS SPPVFNSPGE KHPLGGREAC GMDTLPLNGN FNNSYSLRSG
     DFPPGDGGPE PPRGRNLADA AAFEKMIISE LVHNNLRGSS SAAKGPPPPE PPVPPVPGGG
     GEEEAGGPGG ADRAEIELLY KALEEPLLLP RAQSVLYQSD LDESESCTAE DGATSRPLSS
     PPGRDSLYAS GANLRDSPSY PDSSPEGPSE ALPPPPPAPP GPPEIYYTSR PPALVARNPL
     QGYYQVRRPS HEGYLAAPGL EGPGPDGDGQ MQLVTSL
//
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