ID AGRL1_HUMAN Reviewed; 1474 AA.
AC O94910; Q96IE7; Q9BU07; Q9HAR3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 193.
DE RecName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000312|HGNC:HGNC:20973};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 1 {ECO:0000250|UniProtKB:O88917};
DE Short=CIRL-1 {ECO:0000250|UniProtKB:O88917};
DE AltName: Full=Latrophilin-1 {ECO:0000312|HGNC:HGNC:20973};
DE AltName: Full=Lectomedin-2;
DE Flags: Precursor;
GN Name=ADGRL1 {ECO:0000312|HGNC:HGNC:20973};
GN Synonyms=KIAA0821 {ECO:0000312|HGNC:HGNC:20973},
GN LEC2 {ECO:0000250|UniProtKB:Q80TR1}, LPHN1 {ECO:0000312|HGNC:HGNC:20973};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Douangpanya J., Puri K., Hayflick J.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-1474.
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP VARIANTS DEDBANP 9-TRP--LEU-1474 DEL; 278-TRP--LEU-1474 DEL; CYS-346;
RP ARG-1005; 1136-ARG--LEU-1474 DEL; THR-1152; PHE-1164 AND 1178-ARG--LEU-1474
RP DEL, CHARACTERIZATION OF VARIANTS DEDBANP 9-TRP--LEU-1474 DEL; ARG-1005;
RP THR-1152 AND PHE-1164, INVOLVEMENT IN DEDBANP, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=35907405; DOI=10.1016/j.ajhg.2022.06.011;
RA Vitobello A., Mazel B., Lelianova V.G., Zangrandi A., Petitto E.,
RA Suckling J., Salpietro V., Meyer R., Elbracht M., Kurth I., Eggermann T.,
RA Benlaouer O., Lall G., Tonevitsky A.G., Scott D.A., Chan K.M.,
RA Rosenfeld J.A., Nambot S., Safraou H., Bruel A.L., Denomme-Pichon A.S.,
RA Tran Mau-Them F., Philippe C., Duffourd Y., Guo H., Petersen A.K.,
RA Granger L., Crunk A., Bayat A., Striano P., Zara F., Scala M., Thomas Q.,
RA Delahaye A., de Sainte Agathe J.M., Buratti J., Kozlov S.V., Faivre L.,
RA Thauvin-Robinet C., Ushkaryov Y.;
RT "ADGRL1 haploinsufficiency causes a variable spectrum of neurodevelopmental
RT disorders in humans and alters synaptic activity and behavior in a mouse
RT model.";
RL Am. J. Hum. Genet. 109:1436-1457(2022).
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 (PubMed:35907405). Receptor for TENM2 that mediates heterophilic
CC synaptic cell-cell contact and postsynaptic specialization. Receptor
CC probably implicated in the regulation of exocytosis (By similarity).
CC {ECO:0000250|UniProtKB:O88917, ECO:0000269|PubMed:35907405}.
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 -!- INTERACTION:
CC O94910; O00555: CACNA1A; NbExp=2; IntAct=EBI-3389315, EBI-766279;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35907405};
CC Multi-pass membrane protein. Cell projection, axon
CC {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}.
CC Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2
CC on the cell surface, across intercellular junctions and on nerve
CC terminals near synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94910-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94910-2; Sequence=VSP_010099;
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 (By similarity). {ECO:0000250|UniProtKB:O88917}.
CC -!- DISEASE: Developmental delay, behavioral abnormalities, and
CC neuropsychiatric disorders (DEDBANP) [MIM:620065]: An autosomal
CC dominant disorder characterized by mild global developmental delay,
CC normal or variably impaired intellectual development, and behavioral or
CC neuropsychiatric disorders, including autism spectrum disorder,
CC attention deficit-hyperactivity disorder, and executive functioning
CC deficits. Additional features may include speech delay, dysmorphic
CC features, hypotonia, sleep disturbances, and seizures.
CC {ECO:0000269|PubMed:35907405}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74844.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF307079; AAG27461.1; -; mRNA.
DR EMBL; AB020628; BAA74844.2; ALT_INIT; mRNA.
DR EMBL; AB065919; BAC06134.1; -; Genomic_DNA.
DR EMBL; BC002974; AAH02974.1; -; mRNA.
DR EMBL; BC007587; AAH07587.1; -; mRNA.
DR CCDS; CCDS12307.1; -. [O94910-2]
DR CCDS; CCDS32928.1; -. [O94910-1]
DR RefSeq; NP_001008701.1; NM_001008701.2. [O94910-1]
DR RefSeq; NP_055736.2; NM_014921.4. [O94910-2]
DR AlphaFoldDB; O94910; -.
DR BMRB; O94910; -.
DR SMR; O94910; -.
DR BioGRID; 116528; 76.
DR IntAct; O94910; 24.
DR MINT; O94910; -.
DR STRING; 9606.ENSP00000340688; -.
DR MEROPS; P02.010; -.
DR GlyCosmos; O94910; 8 sites, 1 glycan.
DR GlyGen; O94910; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O94910; -.
DR PhosphoSitePlus; O94910; -.
DR SwissPalm; O94910; -.
DR BioMuta; ADGRL1; -.
DR EPD; O94910; -.
DR jPOST; O94910; -.
DR MassIVE; O94910; -.
DR MaxQB; O94910; -.
DR PaxDb; 9606-ENSP00000340688; -.
DR PeptideAtlas; O94910; -.
DR ProteomicsDB; 50544; -. [O94910-1]
DR ProteomicsDB; 50545; -. [O94910-2]
DR Antibodypedia; 13625; 165 antibodies from 28 providers.
DR DNASU; 22859; -.
DR Ensembl; ENST00000340736.10; ENSP00000340688.5; ENSG00000072071.17. [O94910-1]
DR Ensembl; ENST00000361434.8; ENSP00000355328.2; ENSG00000072071.17. [O94910-2]
DR Ensembl; ENST00000672190.1; ENSP00000500240.1; ENSG00000288324.1. [O94910-1]
DR Ensembl; ENST00000673576.1; ENSP00000500478.1; ENSG00000288324.1. [O94910-2]
DR GeneID; 22859; -.
DR KEGG; hsa:22859; -.
DR MANE-Select; ENST00000361434.8; ENSP00000355328.2; NM_014921.5; NP_055736.2. [O94910-2]
DR UCSC; uc010xnn.3; human. [O94910-1]
DR AGR; HGNC:20973; -.
DR CTD; 22859; -.
DR DisGeNET; 22859; -.
DR GeneCards; ADGRL1; -.
DR HGNC; HGNC:20973; ADGRL1.
DR HPA; ENSG00000072071; Tissue enhanced (brain).
DR MalaCards; ADGRL1; -.
DR MIM; 616416; gene.
DR MIM; 620065; phenotype.
DR neXtProt; NX_O94910; -.
DR OpenTargets; ENSG00000072071; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA134868822; -.
DR VEuPathDB; HostDB:ENSG00000072071; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000159684; -.
DR HOGENOM; CLU_002753_1_1_1; -.
DR InParanoid; O94910; -.
DR OMA; EQSPPWA; -.
DR OrthoDB; 1114672at2759; -.
DR PhylomeDB; O94910; -.
DR TreeFam; TF351999; -.
DR PathwayCommons; O94910; -.
DR SignaLink; O94910; -.
DR BioGRID-ORCS; 22859; 13 hits in 1150 CRISPR screens.
DR ChiTaRS; ADGRL1; human.
DR GeneWiki; LPHN1; -.
DR GenomeRNAi; 22859; -.
DR Pharos; O94910; Tbio.
DR PRO; PR:O94910; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O94910; Protein.
DR Bgee; ENSG00000072071; Expressed in right hemisphere of cerebellum and 99 other cell types or tissues.
DR ExpressionAtlas; O94910; baseline and differential.
DR Genevisible; O94910; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:GDB.
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; IBA:GO_Central.
DR GO; GO:0016524; F:latrotoxin receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
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 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 1: Evidence at protein level;
KW Alternative splicing; Autism spectrum disorder; Autocatalytic cleavage;
KW Cell membrane; Cell projection; Disease variant; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Intellectual disability; Lectin;
KW Membrane; Methylation; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Synapse; Synaptosome; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..1474
FT /note="Adhesion G protein-coupled receptor L1"
FT /id="PRO_0000012907"
FT TOPO_DOM 25..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..893
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..914
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 915..920
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 965..985
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 986..1002
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1003..1023
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1024..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1075
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1076..1096
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1097..1474
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 799..850
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 400..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1474
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 1301..1315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1424
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 838..839
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O88917"
FT MOD_RES 1194
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT MOD_RES 1473
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 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
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 802..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 821..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 132..137
FT /note="KVEQKV -> I (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010099"
FT VARIANT 9..1474
FT /note="Missing (in DEDBANP; loss of protein expression;
FT loss of G protein-coupled receptor signaling)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087773"
FT VARIANT 278..1474
FT /note="Missing (in DEDBANP)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087774"
FT VARIANT 346
FT /note="Y -> C (in DEDBANP; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087775"
FT VARIANT 595
FT /note="E -> Q (in dbSNP:rs34759320)"
FT /id="VAR_049463"
FT VARIANT 1005
FT /note="W -> R (in DEDBANP; decreased G protein-coupled
FT receptor signaling)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087776"
FT VARIANT 1136..1474
FT /note="Missing (in DEDBANP)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087777"
FT VARIANT 1152
FT /note="M -> T (in DEDBANP; decreased G protein-coupled
FT receptor signaling; decreased cell surface localization)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087778"
FT VARIANT 1164
FT /note="S -> F (in DEDBANP; decreased G protein-coupled
FT receptor signaling; decreased cell surface localization)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087779"
FT VARIANT 1178..1474
FT /note="Missing (in DEDBANP)"
FT /evidence="ECO:0000269|PubMed:35907405"
FT /id="VAR_087780"
FT CONFLICT 1321
FT /note="E -> V (in Ref. 4; AAH02974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1474 AA; 162717 MW; 6152EB2DE1385F5C CRC64;
MARLAAVLWN LCVTAVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YKVEQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI
PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT
RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL
RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL
TFPNPYQFIS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT
PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP VPSTRRPPAP NLHVSPELFC
EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV
AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG
KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM LLDVLEEGAF
LLADNVREPA RFLAAKENVV LEVTVLNTEG QVQELVFPQE EYPRKNSIQL SAKTIKQNSR
NGVVKVVFIL YNNLGLFLST ENATVKLAGE AGPGGPGGAS LVVNSQVIAA SINKESSRVF
LMDPVIFTVA HLEDKNHFNA NCSFWNYSER SMLGYWSTQG CRLVESNKTH TTCACSHLTN
FAVLMAHREI YQGRINELLL SVITWVGIVI SLVCLAICIS TFCFLRGLQT DRNTIHKNLC
INLFLAELLF LVGIDKTQYE IACPIFAGLL HYFFLAAFSW LCLEGVHLYL LLVEVFESEY
SRTKYYYLGG YCFPALVVGI AAAIDYRSYG TEKACWLRVD NYFIWSFIGP VSFVIVVNLV
FLMVTLHKMI RSSSVLKPDS SRLDNIKSWA LGAIALLFLL GLTWAFGLLF INKESVVMAY
LFTTFNAFQG VFIFVFHCAL QKKVHKEYSK CLRHSYCCIR SPPGGTHGSL KTSAMRSNTR
YYTGTQSRIR RMWNDTVRKQ TESSFMAGDI NSTPTLNRGT MGNHLLTNPV LQPRGGTSPY
NTLIAESVGF NPSSPPVFNS PGSYREPKHP LGGREACGMD TLPLNGNFNN SYSLRSGDFP
PGDGGPEPPR GRNLADAAAF EKMIISELVH NNLRGSSSAA KGPPPPEPPV PPVPGGGGEE
EAGGPGGADR AEIELLYKAL EEPLLLPRAQ SVLYQSDLDE SESCTAEDGA TSRPLSSPPG
RDSLYASGAN LRDSPSYPDS SPEGPSEALP PPPPAPPGPP EIYYTSRPPA LVARNPLQGY
YQVRRPSHEG YLAAPGLEGP GPDGDGQMQL VTSL
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