AGRL2_RAT
ID AGRL2_RAT Reviewed; 1487 AA.
AC O88923; O88918; O88919; O88920; O88921; O88922; Q9Z174;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Adhesion G protein-coupled receptor L2;
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE Short=CIRL-2;
DE AltName: Full=Latrophilin-2;
DE Flags: Precursor;
GN Name=Adgrl2; Synonyms=Cirl2, Cl2, Lphn2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BINDING TO ALPHA-LATROTOXIN, AND
RP TISSUE SPECIFICITY.
RX PubMed=10026162; DOI=10.1074/jbc.274.9.5491;
RA Ichtchenko K., Bittner M.A., Krasnoperov V., Little A.R., Chepurny O.,
RA Holz R.W., Petrenko A.G.;
RT "A novel ubiquitously expressed alpha-latrotoxin receptor is a member of
RT the CIRL family of G-protein-coupled receptors.";
RL J. Biol. Chem. 274:5491-5498(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7).
RX PubMed=9830014; DOI=10.1074/jbc.273.49.32715;
RA Sugita S., Ichtchenko K., Khvotchev M., Suedhof T.C.;
RT "Alpha-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual
RT family of ubiquitous G-protein-linked receptors. G-protein coupling not
RT required for triggering exocytosis.";
RL J. Biol. Chem. 273:32715-32724(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:10026162}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region non-covalently linked to a seven-transmembrane moiety.
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; Synonyms=CL2A;
CC IsoId=O88923-7; Sequence=Displayed;
CC Name=2; Synonyms=CL2BC;
CC IsoId=O88923-1; Sequence=VSP_010112;
CC Name=3; Synonyms=CL2AA;
CC IsoId=O88923-2; Sequence=VSP_050429, VSP_050430, VSP_010112,
CC VSP_050428;
CC Name=4; Synonyms=CL2AB;
CC IsoId=O88923-3; Sequence=VSP_050429, VSP_050430, VSP_010112,
CC VSP_050427;
CC Name=5; Synonyms=CL2AC;
CC IsoId=O88923-4; Sequence=VSP_050429, VSP_050430, VSP_010112;
CC Name=6; Synonyms=CL2BA;
CC IsoId=O88923-5; Sequence=VSP_010112, VSP_050428;
CC Name=7; Synonyms=CL2BB;
CC IsoId=O88923-6; Sequence=VSP_010112, VSP_050427;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with highest concentrations
CC found in placenta, kidney, spleen, ovary, heart and lung.
CC {ECO:0000269|PubMed:10026162}.
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}.
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DR EMBL; AF063102; AAC77815.1; -; mRNA.
DR EMBL; AF081148; AAC62654.1; -; mRNA.
DR EMBL; AF081149; AAC62655.1; -; mRNA.
DR EMBL; AF081150; AAC62656.1; -; mRNA.
DR EMBL; AF081151; AAC62657.1; -; mRNA.
DR EMBL; AF081152; AAC62658.1; -; mRNA.
DR EMBL; AF081153; AAC62659.1; -; mRNA.
DR PIR; T14324; T14324.
DR PIR; T17157; T17157.
DR PIR; T17158; T17158.
DR PIR; T17159; T17159.
DR PIR; T17160; T17160.
DR PIR; T17185; T17185.
DR PIR; T46611; T46611.
DR RefSeq; NP_001177404.2; NM_001190475.2.
DR RefSeq; NP_001289137.1; NM_001302208.1.
DR RefSeq; NP_001289138.1; NM_001302209.1.
DR RefSeq; NP_001289139.1; NM_001302210.1.
DR RefSeq; NP_001289140.1; NM_001302211.1.
DR RefSeq; NP_001289141.1; NM_001302212.1.
DR RefSeq; NP_599235.3; NM_134408.3.
DR AlphaFoldDB; O88923; -.
DR SMR; O88923; -.
DR STRING; 10116.ENSRNOP00000042136; -.
DR GuidetoPHARMACOLOGY; 207; -.
DR MEROPS; P02.009; -.
DR MEROPS; P02.011; -.
DR GlyGen; O88923; 9 sites.
DR iPTMnet; O88923; -.
DR PhosphoSitePlus; O88923; -.
DR PaxDb; O88923; -.
DR PRIDE; O88923; -.
DR GeneID; 171447; -.
DR KEGG; rno:171447; -.
DR CTD; 23266; -.
DR RGD; 620835; Adgrl2.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR InParanoid; O88923; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; O88923; -.
DR PRO; PR:O88923; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
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:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
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 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..1487
FT /note="Adhesion G protein-coupled receptor L2"
FT /id="PRO_0000012911"
FT TOPO_DOM 26..855
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 856..876
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 885..905
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..911
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 912..932
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 957..977
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 978..994
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 995..1015
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1066..1086
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1087..1090
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1091..1111
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1487
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 139..398
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 789..840
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 422..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 828..829
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1038
FT /note="N -> K (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_050429"
FT VAR_SEQ 1039..1053
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_050430"
FT VAR_SEQ 1054..1062
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_010112"
FT VAR_SEQ 1183..1193
FT /note="Missing (in isoform 6 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_050428"
FT VAR_SEQ 1194..1236
FT /note="Missing (in isoform 7 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_050427"
FT CONFLICT 977
FT /note="S -> Y (in Ref. 2; AAC62654/AAC62655/AAC62656/
FT AAC62657/AAC62658/AAC62659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1487 AA; 166729 MW; 56179F1A95471B00 CRC64;
MVSSGCRMRS LWFIMIISFS PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCVVVTGSD VFPDPCPGTY
KYLEVQYECV PYMEQKVFVC PGTLKAIVDS PSIYEAEQKA GAWCKDPLQA ADKIYFMPWT
PYRTDTLIEY ASLEDFQNSR QTTTYKLPNR VDGTGFVVYD GAVFFNKERT RNIVKFDLRT
RIKSGEAIIN YANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEQNNGMI VISQLNPYTL
RFEATWETTY DKRAASNAFM ICGVLYVVRS VYQDNESEAG KNVIDYIYNT RLSRGEHVDV
PFPNQYQYIA AVDYNPRDNQ LYVWNNNFIL RYSLEFGPPD PAQVPTTAVT ITSSAELFKT
TVSTTSSTSQ RGPVSSTVAG PQEGSRGTKP PPAVSTTKIP PVTNIFPLPE RFCEALEMKG
IKWPQTQRGM MVERPCPKGT RGTASYLCMA STGTWNPKGP DLSNCTSHWV NQLAQKIRSG
ENAASLANEL AKHTKGTVFA GDVSSSVRLM EQLVDILDAQ LQELKPSEKD SAGRSYNKLQ
KREKTCRAYL KAIVDTVDNL LRAETLDCWK HMNSSEQAHT ATMLLDTLEE GAFVLADNLL
EPTRVSMPTD NIVLEVAVLS TEGQVQDFTF HLGFKGAFSS IQLSANTVKQ NSRNGLAKVV
FIIYRSLGPF LSTENATVKL GADLLGRNST IAVNSHVLSV SINKESSRVY LTDPVLFSMP
HIDSDNYFNA NCSFWNYSER TMMGYWSTQG CKLVDTNKTR TTCACSHLTN FAILMAHREI
VYKDGVHKLL LTVITWVGIV VSLVCLAICI FTFCFFRGLQ SDRNTIHKNL CINLFIAEFI
FLIGIDKTQY TIACPVFAGL LHFFFLAAFS WMCLEGVQLY LMLVEVFESE YSRKKYYYVA
GYLFPATVVG VSAAIDSKSY GTLEACWLHV DNYFIWSFIG PVTFIILLNI IFLVITLCKM
VKHSNTLKPD SSRLENINNY RVCDGYYNTD LPGYEDNKPF IKSWVLGAFA LLCLLGLTWS
FGLLFVNEET VVMAYLFTAF NAFQGLFIFI FHCALQKKVR KEYAKCFRHW YCCGGLPTES
PHSSVKASTS RTSARYSSGT QSRIRRMWND TVRKQSESSF ISGDINSTST LNQGMTGNYL
LTNPLLRPHG TNNPYNTLLA ETVVCNAPSA PVFNSPGHSL NNTRDTSAMD TLPLNGNFNN
SYSLRKADYH DGVQVVDCGL SLNDTAFEKM IISELVHNNL RGSNKTHNLE LKLPVKPVIG
GSSSEDDAIV ADASSLMHGD NPGLEFRHKE LEAPLIPQRT HSLLYQPQKK VKPEATDSYV
SQLTAEADEH LQSPNRDSLY TSMPNLRDSP YPESSPDMAE DLSPSRRSEN EDIYYKSMPN
LGAGRQLQMC YQISRGNSDG YIIPINKEGC IPEGDVREGQ MQLVTSL
