ID AGRL2_BOVIN Reviewed; 1478 AA.
AC O97817; O97805; O97807; O97809; O97810; O97811; O97812; O97813; O97814;
AC O97815; O97816;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 132.
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=LPH2, LPHN2;
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; 2; 3; 4; 5; 6; 7; 8; 9; 10 AND 11).
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 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=11;
CC Name=1; Synonyms=bbbbf;
CC IsoId=O97817-1; Sequence=Displayed;
CC Name=2; Synonyms=babbf;
CC IsoId=O97817-2; Sequence=VSP_010100;
CC Name=3; Synonyms=baabf;
CC IsoId=O97817-3; Sequence=VSP_010100, VSP_010101;
CC Name=4; Synonyms=babaf;
CC IsoId=O97817-4; Sequence=VSP_010100, VSP_010102;
CC Name=5; Synonyms=bbabf;
CC IsoId=O97817-5; Sequence=VSP_010101;
CC Name=6; Synonyms=bbbaf;
CC IsoId=O97817-6; Sequence=VSP_010102;
CC Name=7; Synonyms=bbaaf;
CC IsoId=O97817-7; Sequence=VSP_010101, VSP_010102;
CC Name=8; Synonyms=bbbbe;
CC IsoId=O97817-8; Sequence=VSP_010103;
CC Name=9; Synonyms=bbabe;
CC IsoId=O97817-9; Sequence=VSP_010101, VSP_010103;
CC Name=10; Synonyms=bbbae;
CC IsoId=O97817-10; Sequence=VSP_010102, VSP_010103;
CC Name=11; Synonyms=bbaae;
CC IsoId=O97817-11; Sequence=VSP_010101, VSP_010102, VSP_010103;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000250}.
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; AF111072; AAD05308.1; -; mRNA.
DR EMBL; AF111074; AAD05310.1; -; mRNA.
DR EMBL; AF111076; AAD05312.1; -; mRNA.
DR EMBL; AF111077; AAD05313.1; -; mRNA.
DR EMBL; AF111078; AAD05314.1; -; mRNA.
DR EMBL; AF111079; AAD05315.1; -; mRNA.
DR EMBL; AF111080; AAD05316.1; -; mRNA.
DR EMBL; AF111081; AAD05317.1; -; mRNA.
DR EMBL; AF111082; AAD05318.1; -; mRNA.
DR EMBL; AF111083; AAD05319.1; -; mRNA.
DR EMBL; AF111084; AAD05320.1; -; mRNA.
DR PIR; T18370; T18370.
DR PIR; T18377; T18377.
DR PIR; T18380; T18380.
DR PIR; T18381; T18381.
DR PIR; T18382; T18382.
DR PIR; T18383; T18383.
DR PIR; T18384; T18384.
DR PIR; T18385; T18385.
DR PIR; T18386; T18386.
DR PIR; T18387; T18387.
DR PIR; T18388; T18388.
DR RefSeq; NP_851356.1; NM_181013.1. [O97817-1]
DR AlphaFoldDB; O97817; -.
DR SMR; O97817; -.
DR STRING; 9913.ENSBTAP00000055886; -.
DR MEROPS; P02.009; -.
DR GlyCosmos; O97817; 9 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000016334; -.
DR GeneID; 281278; -.
DR KEGG; bta:281278; -.
DR CTD; 23266; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR InParanoid; O97817; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd22845; Gal_Rha_Lectin_LPHN2; 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; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF61; ADHESION G PROTEIN-COUPLED RECEPTOR L2; 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 SUPFAM; SSF111418; Hormone receptor domain; 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; 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..1478
FT /note="Adhesion G protein-coupled receptor L2"
FT /id="PRO_0000012909"
FT TOPO_DOM 26..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..911
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 977..994
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1015
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1056
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1057..1077
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1078..1081
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1082..1102
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1103..1478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..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 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZZ7"
FT MOD_RES 1449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95490"
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 404..469
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010100"
FT VAR_SEQ 598..610
FT /note="Missing (in isoform 3, isoform 5, isoform 7, isoform
FT 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010101"
FT VAR_SEQ 1038..1053
FT /note="NNYRVCDGYYNTDLPG -> K (in isoform 4, isoform 6,
FT isoform 7, isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010102"
FT VAR_SEQ 1185..1227
FT /note="Missing (in isoform 8, isoform 9, isoform 10 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010103"
SQ SEQUENCE 1478 AA; 165547 MW; 643722171D6D413E CRC64;
MVSSGCRMRS LWFIIIISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
KYLEVQYECV PYMEQKVFVC PGTLKAIVDS PCIYEAEQKA GAWCKDPLQA ADKIYFMPWT
PYRTDTLIEY ASLEDFQNSR QTTTYKLPNR VDGTGFVVYD GAVFFNKERT RNIVKYDLRT
RIKSGEAIIN YANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEQNNGMI VISQLNPYTL
RFEATWETVY DKRAASNAFM ICGVLYVVRS VYQDNESETG KNAIDYIYNT RLNRGEYVDV
PFPNQYQYIA AVDYNPRDNQ LYVWNNNFIL RYSLEFGPPD PAQVPTTAVT ITSSAEMFKT
TVSTTSTTSQ KGPMSTTVAG SQEGSKGTKA PPAVSTTKIP PVTNIFPLPE RFCEALDARG
IRWPQTQRGM MVERPCPKGT RGTASYLCVL STGTWNPKGP DLSNCTSHWV NQLAQKIRSG
ENAASLANEL AKHTKGPVFA GDVSSSVRLM EQLVDILDAQ LQELKPSEKD SAGRSYNKLQ
KREKTCRAYL KAIVDTVDNL LRPEALESWK HMNSSEQAHT ATMLLDTLEE GAFVLADNLV
EPTRVSMPTE NIVLEVAVLS TEGQVQDFKF PLGIKGAGSS IQLSANTVKQ NSRNGLAKLV
FIIYRSLGQF LSTENATIKL GADFIGRNST IAVNSHVISV SINKESSRVY LTDPVLFTLP
HIDPDNYFNA NCSFWNYSER TMMGYWSTQG CKLVDTNKTR TTCACSHLTN FAILMAHREI
AYKDGVHELL LTVITWVGIV ISLVCLAICI FTFCFFRGLQ SDRNTIHKNL CINLFIAEFI
FLIGIDKTKY MIACPIFAGL LHFFFLAAFA WMCLEGVQLY LMLVEVFESE YSRKKYYYVA
GYLFPATVVG VSAAIDYKSY GTEKACWLHV DNYFIWSFIG PVTFIILLNI IFLVITLCKM
VKHSNTLKPD SSRLENINNY RVCDGYYNTD LPGSWVLGAF ALLCLLGLTW SFGLLFINEE
TIVMAYLFTI FNAFQGVFIF IFHCALQKKV RKEYGKCFRH SYCCGGLPTE SPHSSVKAST
TRTSARYSSG TQSRIRRMWN DTVRKQSESS FISGDINSTS TLNQGMTGNY LLTNPLLRPH
GTNNPYNTLL AETVVCNAPS APVFNSPGHS LNNARDTSAM DTLPLNGNFN NSYSLRKGDY
NDSVQVVDCG LSLNDTAFEK MIISELVHNN LRGSSKAHNL ELTLPVKPVI GGSSSEDDAI
VADASSLMHG DNPGLELHHK ELEAPLIPQR THSLLYQPQK KAKPEGTDSY VSQLTAEAED
HLQSPNRDSL YTSMPNLRDS PYQESSPDME EDLSPSRRSE NEDIYYKSMP NLGAGHQLQM
CYQISRGNSD GYIIPINKEG CIPEGDVREG QMQLVTSL
//
