AGRL1_BOVIN
ID AGRL1_BOVIN Reviewed; 1472 AA.
AC O97831; O97830;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000250|UniProtKB:O94910};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 1 {ECO:0000250|UniProtKB:O94910};
DE Short=CIRL-1 {ECO:0000250|UniProtKB:O94910};
DE AltName: Full=Latrophilin-1 {ECO:0000250|UniProtKB:O94910};
DE Flags: Precursor;
GN Name=ADGRL1 {ECO:0000250|UniProtKB:O94910};
GN Synonyms=LPHN1 {ECO:0000250|UniProtKB:O94910};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=9261169; DOI=10.1074/jbc.272.34.21504;
RA Lelianova V.G., Davletov B.A., Sterling A., Rahman M.A., Grishin E.V.,
RA Totty N.F., Ushkaryov Y.A.;
RT "Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin
RT family of G protein-coupled receptors.";
RL J. Biol. Chem. 272:21504-21508(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10025961; DOI=10.1016/s0014-5793(99)00005-8;
RA Matsushita H., Lelianova V.G., Ushkaryov Y.A.;
RT "The latrophilin family: multiply spliced G protein-coupled receptors with
RT differential tissue distribution.";
RL FEBS Lett. 443:348-352(1999).
CC -!- FUNCTION: Calcium-independent receptor of high affinity for alpha-
CC latrotoxin, an excitatory neurotoxin present in black widow spider
CC venom which triggers massive exocytosis from neurons and neuroendocrine
CC cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell
CC contact and postsynaptic specialization. Receptor probably implicated
CC in the regulation of exocytosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (p120) non-covalently linked to a seven-transmembrane moiety
CC (p85). Interacts with syntaxin and with proteins of the SHANK family
CC via the PDZ domain. Interacts (via extracellular domain) with FLRT1,
CC FLRT2 and FLRT3 (via extracellular domain) (By similarity).
CC {ECO:0000250|UniProtKB:O88917, ECO:0000250|UniProtKB:Q80TR1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:O88917}. Synapse
CC {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell
CC surface, across intercellular junctions and on nerve terminals near
CC synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O97831-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O97831-2; Sequence=VSP_022136;
CC -!- TISSUE SPECIFICITY: Brain-specific expression but low levels are also
CC detected in kidney, lung and spleen. {ECO:0000269|PubMed:10025961}.
CC -!- DOMAIN: The extracellular domain coupled to the a single transmembrane
CC region are sufficient for full responsiveness to alpha-latrotoxin.
CC {ECO:0000250}.
CC -!- PTM: Autoproteolytically cleaved into 2 subunits, an extracellular
CC subunit and a seven-transmembrane subunit. This proteolytic processing
CC takes place early in the biosynthetic pathway, either in the
CC endoplasmic reticulum or in the early compartment of the Golgi
CC apparatus. {ECO:0000250|UniProtKB:O88917}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AF111097; AAD09191.1; -; mRNA.
DR EMBL; AF111098; AAD09192.1; -; mRNA.
DR PIR; T18411; T18411.
DR PIR; T18413; T18413.
DR RefSeq; NP_001107200.1; NM_001113728.1. [O97831-1]
DR RefSeq; XP_005208683.1; XM_005208626.3. [O97831-2]
DR AlphaFoldDB; O97831; -.
DR BMRB; O97831; -.
DR SMR; O97831; -.
DR STRING; 9913.ENSBTAP00000036113; -.
DR MEROPS; P02.010; -.
DR PaxDb; O97831; -.
DR Ensembl; ENSBTAT00000036251; ENSBTAP00000036113; ENSBTAG00000003675. [O97831-2]
DR GeneID; 788252; -.
DR KEGG; bta:788252; -.
DR CTD; 22859; -.
DR VEuPathDB; HostDB:ENSBTAG00000003675; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000159684; -.
DR InParanoid; O97831; -.
DR OrthoDB; 388923at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000003675; Expressed in vas deferens and 103 other tissues.
DR ExpressionAtlas; O97831; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0016524; F:latrotoxin receptor activity; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 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.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; PTHR12011:SF62; 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 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lectin; Membrane; Methylation;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Synapse; Synaptosome;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..1472
FT /note="Adhesion G protein-coupled receptor L1"
FT /id="PRO_0000012906"
FT TOPO_DOM 25..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..878
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..892
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..919
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..940
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 985..1001
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1023..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1050..1070
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1071..1074
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..129
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 139..398
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 798..849
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 400..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT BINDING 117..120
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT SITE 837..838
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O88917"
FT MOD_RES 1193
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT MOD_RES 1471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 50..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 83..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 96..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 140..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 480..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 503..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 801..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 820..834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 132..137
FT /note="KVKQKV -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10025961,
FT ECO:0000303|PubMed:9261169"
FT /id="VSP_022136"
SQ SEQUENCE 1472 AA; 162205 MW; 860D7C75AA0D2F24 CRC64;
MARLAAVLWS LCVTAILVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YKVKQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI
PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT
RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL
RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL
AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT
PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP APSTRRPPAP NLHVSPELFC
EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV
AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG
KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQAHTATM LLDVLEEGAF
LLADNVREPA RFLAAKQNVV LEVTVLNTEG QVQELVFPQE YPSENSIQLS ANTIKQNSRN
GVVKVVFILY NNLGLFLSTE NATVKLAGEA GSGGPGGASL VVNSQVIAAS INKESSRVFL
MDPVIFTVAH LEAKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF
AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI
NLFLAELLFL VGIDKTQYEI ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS
RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF
LMVTLHKMVR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL
FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNARY
YTGTQSRIRR MWNDTVRKQT ESSFMAGDIN STPTLNRGTM GNHLLTNPVL QPRGGTSPYN
TLIAESVGFN PSSPPVFNSP GSYREPKHPL GGREACGMDT LPLNGNFNNS YSLRSGDFPP
GDGAPEPPRG RNLADAAAFE KMIISELVHN NLRGGSSGAK GPPPPEPPVP PVPGGSGEEE
AGGPGADRAE IELLYKALEE PLLLPRAQSV LYQSDLDESE SCTAEDGATS RPLSSPPGRD
SLYASGANLR DSPSYPDSSP EGPSEALPPP PPAPPGPPEI YYTSRPPALV ARNPLQGYYQ
VRRPSHEGYL AAPGLEGPGP DGDGQMQLVT SL
