AGRL2_HUMAN
ID AGRL2_HUMAN Reviewed; 1459 AA.
AC O95490; A5XEI2; B1ALT8; B1ALT9; B1ALU0; B1ALU2; B1ALU4; B1ALU5; B1ALU6;
AC O94882; Q5VX76; Q9UKY5; Q9UKY6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000303|PubMed:25713288};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE Short=CIRL-2;
DE AltName: Full=Latrophilin homolog 1;
DE AltName: Full=Latrophilin-2;
DE AltName: Full=Lectomedin-1;
DE Flags: Precursor;
GN Name=ADGRL2 {ECO:0000312|HGNC:HGNC:18582};
GN Synonyms=KIAA0786, LEC1, LPHH1, LPHN2;
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), AND TISSUE SPECIFICITY.
RX PubMed=10030676; DOI=10.1038/sj.onc.1202487;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Isolation and characterisation of a human homologue of the latrophilin
RT gene from a region of 1p31.1 implicated in breast cancer.";
RL Oncogene 17:3513-3519(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10760572; DOI=10.1016/s0167-4781(00)00020-8;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Genomic structure and expression profile of LPHH1, a 7TM gene variably
RT expressed in breast cancer cell lines.";
RL Biochim. Biophys. Acta 1491:75-92(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RA Hayflick J.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-1459 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1070 (ISOFORM 6).
RX PubMed=17456239; DOI=10.1186/gb-2007-8-4-r64;
RA Clark T.A., Schweitzer A.C., Chen T.X., Staples M.K., Lu G., Wang H.,
RA Williams A., Blume J.E.;
RT "Discovery of tissue-specific exons using comprehensive human exon
RT microarrays.";
RL Genome Biol. 8:R64.1-R64.16(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-629.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP VARIANT THR-467.
RX PubMed=23647072; DOI=10.1111/epi.12201;
RA Veeramah K.R., Johnstone L., Karafet T.M., Wolf D., Sprissler R.,
RA Salogiannis J., Barth-Maron A., Greenberg M.E., Stuhlmann T., Weinert S.,
RA Jentsch T.J., Pazzi M., Restifo L.L., Talwar D., Erickson R.P.,
RA Hammer M.F.;
RT "Exome sequencing reveals new causal mutations in children with epileptic
RT encephalopathies.";
RL Epilepsia 54:1270-1281(2013).
RN [13]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
CC -!- FUNCTION: Calcium-independent receptor of low 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 probably implicated in the regulation of exocytosis.
CC {ECO:0000250|UniProtKB:O88923}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region non-covalently linked to a seven-transmembrane moiety.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O95490-1; Sequence=Displayed;
CC Name=2; Synonyms=Lectomedin-1 gamma;
CC IsoId=O95490-2; Sequence=VSP_010104, VSP_010107;
CC Name=3; Synonyms=Lectomedin-1 beta;
CC IsoId=O95490-3; Sequence=VSP_010104, VSP_010105, VSP_010106;
CC Name=4; Synonyms=Lectomedin-1 alpha;
CC IsoId=O95490-4; Sequence=VSP_010104, VSP_010107, VSP_010108,
CC VSP_010109;
CC Name=5;
CC IsoId=O95490-5; Sequence=VSP_010107;
CC Name=6;
CC IsoId=O95490-6; Sequence=VSP_042267;
CC Name=7;
CC IsoId=O95490-7; Sequence=VSP_010104, VSP_042267;
CC -!- TISSUE SPECIFICITY: Expressed very widely in all normal tissues tested.
CC Expression is variable in tumor cell lines, apparently elevated in some
CC lines and absent or markedly reduced in others.
CC {ECO:0000269|PubMed:10030676}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {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}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LPHH1ID313.html";
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DR EMBL; AJ131581; CAA10458.1; -; mRNA.
DR EMBL; AJ244492; CAB60229.1; -; Genomic_DNA.
DR EMBL; AJ244493; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244494; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244496; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244497; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244498; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244499; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244501; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244502; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244503; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244504; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244505; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244506; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244507; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244510; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244511; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244512; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244516; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AF104266; AAD54675.1; -; mRNA.
DR EMBL; AF104938; AAD54676.1; -; mRNA.
DR EMBL; AF104939; AAD54677.1; -; mRNA.
DR EMBL; AC113949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06327.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06330.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06333.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06335.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06336.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06339.1; -; Genomic_DNA.
DR EMBL; AB018329; BAA34506.1; -; mRNA.
DR EMBL; DQ925675; ABL59902.1; -; mRNA.
DR CCDS; CCDS689.1; -. [O95490-2]
DR CCDS; CCDS72811.1; -. [O95490-4]
DR CCDS; CCDS76174.1; -. [O95490-3]
DR CCDS; CCDS81345.1; -. [O95490-5]
DR RefSeq; NP_001284633.1; NM_001297704.1. [O95490-2]
DR RefSeq; NP_001284634.1; NM_001297705.1. [O95490-4]
DR RefSeq; NP_001284635.1; NM_001297706.1. [O95490-3]
DR RefSeq; NP_001317574.1; NM_001330645.1. [O95490-5]
DR RefSeq; NP_036434.1; NM_012302.3. [O95490-2]
DR RefSeq; XP_005270723.1; XM_005270666.4. [O95490-1]
DR RefSeq; XP_016856276.1; XM_017000787.1.
DR AlphaFoldDB; O95490; -.
DR SMR; O95490; -.
DR BioGRID; 116868; 74.
DR IntAct; O95490; 23.
DR MINT; O95490; -.
DR STRING; 9606.ENSP00000322270; -.
DR MEROPS; P02.009; -.
DR TCDB; 9.A.14.6.9; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 994; 2 N-Linked glycans (1 site).
DR GlyGen; O95490; 12 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; O95490; -.
DR PhosphoSitePlus; O95490; -.
DR BioMuta; ADGRL2; -.
DR EPD; O95490; -.
DR jPOST; O95490; -.
DR MassIVE; O95490; -.
DR MaxQB; O95490; -.
DR PaxDb; O95490; -.
DR PeptideAtlas; O95490; -.
DR PRIDE; O95490; -.
DR ProteomicsDB; 50917; -. [O95490-1]
DR ProteomicsDB; 50918; -. [O95490-2]
DR ProteomicsDB; 50919; -. [O95490-3]
DR ProteomicsDB; 50920; -. [O95490-4]
DR ProteomicsDB; 50921; -. [O95490-5]
DR ProteomicsDB; 50922; -. [O95490-6]
DR ProteomicsDB; 50923; -. [O95490-7]
DR Antibodypedia; 2953; 151 antibodies from 29 providers.
DR DNASU; 23266; -.
DR Ensembl; ENST00000319517.10; ENSP00000322270.6; ENSG00000117114.21. [O95490-2]
DR Ensembl; ENST00000359929.7; ENSP00000353006.2; ENSG00000117114.21. [O95490-2]
DR Ensembl; ENST00000370713.5; ENSP00000359748.1; ENSG00000117114.21. [O95490-3]
DR Ensembl; ENST00000370715.5; ENSP00000359750.1; ENSG00000117114.21. [O95490-4]
DR Ensembl; ENST00000370717.6; ENSP00000359752.3; ENSG00000117114.21. [O95490-1]
DR Ensembl; ENST00000370723.5; ENSP00000359758.1; ENSG00000117114.21. [O95490-7]
DR Ensembl; ENST00000370725.5; ENSP00000359760.1; ENSG00000117114.21. [O95490-6]
DR Ensembl; ENST00000370728.5; ENSP00000359763.1; ENSG00000117114.21. [O95490-1]
DR Ensembl; ENST00000370730.5; ENSP00000359765.1; ENSG00000117114.21. [O95490-5]
DR Ensembl; ENST00000674393.1; ENSP00000501431.1; ENSG00000117114.21. [O95490-2]
DR Ensembl; ENST00000674419.1; ENSP00000501462.1; ENSG00000117114.21. [O95490-5]
DR GeneID; 23266; -.
DR KEGG; hsa:23266; -.
DR UCSC; uc001dit.5; human. [O95490-1]
DR CTD; 23266; -.
DR DisGeNET; 23266; -.
DR GeneCards; ADGRL2; -.
DR HGNC; HGNC:18582; ADGRL2.
DR HPA; ENSG00000117114; Low tissue specificity.
DR MIM; 607018; gene.
DR neXtProt; NX_O95490; -.
DR OpenTargets; ENSG00000117114; -.
DR PharmGKB; PA38589; -.
DR VEuPathDB; HostDB:ENSG00000117114; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000156348; -.
DR HOGENOM; CLU_002753_1_0_1; -.
DR InParanoid; O95490; -.
DR OMA; TEPTIGC; -.
DR PhylomeDB; O95490; -.
DR TreeFam; TF351999; -.
DR PathwayCommons; O95490; -.
DR SignaLink; O95490; -.
DR BioGRID-ORCS; 23266; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; ADGRL2; human.
DR GeneWiki; LPHN2; -.
DR GenomeRNAi; 23266; -.
DR Pharos; O95490; Tbio.
DR PRO; PR:O95490; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95490; protein.
DR Bgee; ENSG00000117114; Expressed in adrenal tissue and 172 other tissues.
DR ExpressionAtlas; O95490; baseline and differential.
DR Genevisible; O95490; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016524; F:latrotoxin receptor activity; NAS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
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 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; IPR031240; Latrophilin-2.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF61; PTHR12011:SF61; 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; SSF111418; SSF111418; 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; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1459
FT /note="Adhesion G protein-coupled receptor L2"
FT /id="PRO_0000012910"
FT TOPO_DOM 26..851
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 852..872
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..901
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..907
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 908..928
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 929..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 953..973
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 974..990
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 991..1011
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1038..1058
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..1062
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1063..1083
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1084..1459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 41..130
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 135..394
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 784..836
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 422..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 824..825
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 136..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 595..607
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:10030676, ECO:0000303|Ref.3"
FT /id="VSP_010104"
FT VAR_SEQ 1034
FT /note="K -> NNYRVCDGYYNTDLPG (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:17456239"
FT /id="VSP_042267"
FT VAR_SEQ 1134..1136
FT /note="SRI -> DIH (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010105"
FT VAR_SEQ 1137..1459
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010106"
FT VAR_SEQ 1167..1209
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10030676, ECO:0000303|Ref.3"
FT /id="VSP_010107"
FT VAR_SEQ 1210..1233
FT /note="HSLNNARDTSAMDTLPLNGNFNNS -> LTSHGLRAHLQDLYHLELLLGQIA
FT (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010108"
FT VAR_SEQ 1234..1459
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010109"
FT VARIANT 467
FT /note="R -> T (found in a child with sporadic epilepsy;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23647072"
FT /id="VAR_077836"
FT CONFLICT 1059
FT /note="N -> S (in Ref. 7; ABL59902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1459 AA; 163349 MW; 30707B7C3C069029 CRC64;
MVSSGCRMRS LWFIIVISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
KYLEVQYECV PYIFVCPGTL KAIVDSPCIY EAEQKAGAWC KDPLQAADKI YFMPWTPYRT
DTLIEYASLE DFQNSRQTTT YKLPNRVDGT GFVVYDGAVF FNKERTRNIV KFDLRTRIKS
GEAIINYANY HDTSPYRWGG KTDIDLAVDE NGLWVIYATE QNNGMIVISQ LNPYTLRFEA
TWETVYDKRA ASNAFMICGV LYVVRSVYQD NESETGKNSI DYIYNTRLNR GEYVDVPFPN
QYQYIAAVDY NPRDNQLYVW NNNFILRYSL EFGPPDPAQV PTTAVTITSS AELFKTIIST
TSTTSQKGPM STTVAGSQEG SKGTKPPPAV STTKIPPITN IFPLPERFCE ALDSKGIKWP
QTQRGMMVER PCPKGTRGTA SYLCMISTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKLQKREK
TCRAYLKAIV DTVDNLLRPE ALESWKHMNS SEQAHTATML LDTLEEGAFV LADNLLEPTR
VSMPTENIVL EVAVLSTEGQ IQDFKFPLGI KGAGSSIQLS ANTVKQNSRN GLAKLVFIIY
RSLGQFLSTE NATIKLGADF IGRNSTIAVN SHVISVSINK ESSRVYLTDP VLFTLPHIDP
DNYFNANCSF WNYSERTMMG YWSTQGCKLV DTNKTRTTCA CSHLTNFAIL MAHREIAYKD
GVHELLLTVI TWVGIVISLV CLAICIFTFC FFRGLQSDRN TIHKNLCINL FIAEFIFLIG
IDKTKYAIAC PIFAGLLHFF FLAAFAWMCL EGVQLYLMLV EVFESEYSRK KYYYVAGYLF
PATVVGVSAA IDYKSYGTEK ACWLHVDNYF IWSFIGPVTF IILLNIIFLV ITLCKMVKHS
NTLKPDSSRL ENIKSWVLGA FALLCLLGLT WSFGLLFINE ETIVMAYLFT IFNAFQGVFI
FIFHCALQKK VRKEYGKCFR HSYCCGGLPT ESPHSSVKAS TTRTSARYSS GTQSRIRRMW
NDTVRKQSES SFISGDINST STLNQGMTGN YLLTNPLLRP HGTNNPYNTL LAETVVCNAP
SAPVFNSPGH SLNNARDTSA MDTLPLNGNF NNSYSLHKGD YNDSVQVVDC GLSLNDTAFE
KMIISELVHN NLRGSSKTHN LELTLPVKPV IGGSSSEDDA IVADASSLMH SDNPGLELHH
KELEAPLIPQ RTHSLLYQPQ KKVKSEGTDS YVSQLTAEAE DHLQSPNRDS LYTSMPNLRD
SPYPESSPDM EEDLSPSRRS ENEDIYYKSM PNLGAGHQLQ MCYQISRGNS DGYIIPINKE
GCIPEGDVRE GQMQLVTSL
