AGRL3_BOVIN
ID AGRL3_BOVIN Reviewed; 1580 AA.
AC O97827; O97818; O97819; O97820; O97821; O97822; O97823; O97824; O97825;
AC O97826; O97828; O97829;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000250|UniProtKB:Q9HAR2};
DE AltName: Full=Latrophilin-3 {ECO:0000303|PubMed:10025961};
DE Flags: Precursor;
GN Name=ADGRL3 {ECO:0000250|UniProtKB:Q9HAR2};
GN Synonyms=LPH3 {ECO:0000303|PubMed:10025961},
GN LPHN3 {ECO:0000250|UniProtKB:Q9HAR2};
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; 11 AND
RP 12), AND TISSUE SPECIFICITY.
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: Plays a role in cell-cell adhesion and neuron guidance via
CC its interactions with FLRT2 and FLRT3 that are expressed at the surface
CC of adjacent cells. Plays a role in the development of glutamatergic
CC synapses in the cortex. Important in determining the connectivity rates
CC between the principal neurons in the cortex.
CC {ECO:0000250|UniProtKB:Q80TS3}.
CC -!- SUBUNIT: Interacts (via olfactomedin-like domain) with FLRT3 (via
CC extracellular domain); the interaction is direct. Identified in a
CC complex with FLRT3 and UNC5B; does not interact with UNC5B by itself.
CC Identified in a complex with FLRT3 and UNC5D; does not interact with
CC UNC5D by itself (By similarity). Interacts (via olfactomedin-like
CC domain) with FLRT1 (via extracellular domain). Interacts (via
CC olfactomedin-like domain) with FLRT2 (via extracellular domain).
CC Interacts (via extracellular domain) with TENM1. Interacts (via
CC extracellular domain) with TENM3 (By similarity).
CC {ECO:0000250|UniProtKB:Q80TS3, ECO:0000250|UniProtKB:Q9HAR2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80TS3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80TS3}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction
CC {ECO:0000250|UniProtKB:Q80TS3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=bbbf;
CC IsoId=O97827-1; Sequence=Displayed;
CC Name=2; Synonyms=abbf;
CC IsoId=O97827-2; Sequence=VSP_010113;
CC Name=3; Synonyms=abah;
CC IsoId=O97827-3; Sequence=VSP_010113, VSP_010114;
CC Name=4; Synonyms=abah;
CC IsoId=O97827-4; Sequence=VSP_010113, VSP_010114, VSP_010119,
CC VSP_010120;
CC Name=5; Synonyms=abag;
CC IsoId=O97827-5; Sequence=VSP_010113, VSP_010114, VSP_010116,
CC VSP_010117;
CC Name=6; Synonyms=abbg;
CC IsoId=O97827-6; Sequence=VSP_010113, VSP_010116, VSP_010117;
CC Name=7; Synonyms=bbaf;
CC IsoId=O97827-7; Sequence=VSP_010114;
CC Name=8; Synonyms=abbh;
CC IsoId=O97827-8; Sequence=VSP_010113, VSP_010119, VSP_010120;
CC Name=9; Synonyms=bbah;
CC IsoId=O97827-9; Sequence=VSP_010114, VSP_010119, VSP_010120;
CC Name=10; Synonyms=bbbh;
CC IsoId=O97827-10; Sequence=VSP_010119, VSP_010120;
CC Name=11; Synonyms=bbag;
CC IsoId=O97827-11; Sequence=VSP_010115, VSP_010116, VSP_010117;
CC Name=12; Synonyms=bbbg;
CC IsoId=O97827-12; Sequence=VSP_010116, VSP_010117;
CC -!- TISSUE SPECIFICITY: Brain-specific distribution but low levels are also
CC detected in lung and spleen. {ECO:0000269|PubMed:10025961}.
CC -!- DOMAIN: The Olfactomedin-like domain is required for the synapse-
CC promoting function and the interaction with FLRT3. The Olfactomedin-
CC like and the SUEL-type lectin domains are required for the interaction
CC with TENM1 (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000250}.
CC -!- PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AF111085; AAD05321.1; -; mRNA.
DR EMBL; AF111086; AAD05322.1; -; mRNA.
DR EMBL; AF111087; AAD05323.1; -; mRNA.
DR EMBL; AF111088; AAD05324.1; -; mRNA.
DR EMBL; AF111089; AAD05325.1; -; mRNA.
DR EMBL; AF111090; AAD05326.1; -; mRNA.
DR EMBL; AF111091; AAD05327.1; -; mRNA.
DR EMBL; AF111092; AAD05328.1; -; mRNA.
DR EMBL; AF111095; AAD05331.1; -; mRNA.
DR EMBL; AF111093; AAD05329.1; -; mRNA.
DR EMBL; AF111094; AAD05330.1; -; mRNA.
DR EMBL; AF111096; AAD05332.1; -; mRNA.
DR PIR; T18389; T18389.
DR PIR; T18390; T18390.
DR PIR; T18391; T18391.
DR PIR; T18392; T18392.
DR PIR; T18393; T18393.
DR PIR; T18394; T18394.
DR PIR; T18395; T18395.
DR PIR; T18398; T18398.
DR PIR; T18405; T18405.
DR PIR; T18407; T18407.
DR PIR; T18408; T18408.
DR PIR; T18409; T18409.
DR RefSeq; NP_851376.1; NM_181033.2. [O97827-1]
DR RefSeq; XP_005208058.1; XM_005208001.3. [O97827-1]
DR RefSeq; XP_005208068.1; XM_005208011.3.
DR RefSeq; XP_015327119.1; XM_015471633.1.
DR RefSeq; XP_015327122.1; XM_015471636.1.
DR RefSeq; XP_015327123.1; XM_015471637.1.
DR RefSeq; XP_015327124.1; XM_015471638.1.
DR RefSeq; XP_015327125.1; XM_015471639.1.
DR RefSeq; XP_015327126.1; XM_015471640.1.
DR RefSeq; XP_015327127.1; XM_015471641.1.
DR RefSeq; XP_015327128.1; XM_015471642.1.
DR RefSeq; XP_015327129.1; XM_015471643.1.
DR RefSeq; XP_015327130.1; XM_015471644.1.
DR AlphaFoldDB; O97827; -.
DR SMR; O97827; -.
DR STRING; 9913.ENSBTAP00000039471; -.
DR MEROPS; P02.011; -.
DR PaxDb; O97827; -.
DR PRIDE; O97827; -.
DR Ensembl; ENSBTAT00000018508; ENSBTAP00000018508; ENSBTAG00000013918. [O97827-7]
DR Ensembl; ENSBTAT00000051991; ENSBTAP00000049222; ENSBTAG00000013918. [O97827-1]
DR Ensembl; ENSBTAT00000066218; ENSBTAP00000055267; ENSBTAG00000013918. [O97827-10]
DR GeneID; 282651; -.
DR KEGG; bta:282651; -.
DR CTD; 23284; -.
DR VEuPathDB; HostDB:ENSBTAG00000013918; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000155527; -.
DR HOGENOM; CLU_002753_0_2_1; -.
DR InParanoid; O97827; -.
DR OMA; SASLNRX; -.
DR OrthoDB; 388923at2759; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000013918; Expressed in semen and 84 other tissues.
DR ExpressionAtlas; O97827; baseline and differential.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
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:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
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; IPR015630; Latrophilin-3.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF60; PTHR12011:SF60; 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 junction; Cell membrane; Cell projection;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1580
FT /note="Adhesion G protein-coupled receptor L3"
FT /id="PRO_0000012912"
FT TOPO_DOM 20..949
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..970
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1000..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1088
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1163
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1164..1169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1191..1580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 103..192
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 202..461
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 883..934
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..347
FT /note="Interaction with FLRT3"
FT /evidence="ECO:0000250|UniProtKB:Q9HAR2"
FT REGION 494..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT SITE 922..923
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..134
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 113..191
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 146..178
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 159..165
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 203..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 19..86
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010113"
FT VAR_SEQ 1131..1139
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010114"
FT VAR_SEQ 1132..1140
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010115"
FT VAR_SEQ 1272..1308
FT /note="GAMANHLISNALLRPHGTNNPYNTLLGEPAVCNNPSV -> EPYRETSMGVK
FT LNIAYQIGASEQCQGYKCHGYSTTEW (in isoform 5, isoform 6,
FT isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010116"
FT VAR_SEQ 1309..1580
FT /note="Missing (in isoform 5, isoform 6, isoform 11 and
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010117"
FT VAR_SEQ 1316..1351
FT /note="GLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNC -> PYRETSMGVKLN
FT IAYQIGASEQCQGYKCHGYSTTEW (in isoform 4, isoform 8, isoform
FT 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010119"
FT VAR_SEQ 1352..1580
FT /note="Missing (in isoform 4, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:10025961"
FT /id="VSP_010120"
SQ SEQUENCE 1580 AA; 176051 MW; D527CBF4B937DA8D CRC64;
MWPSQLLVFM MLLAPIIHGG KHSERHPALA SPLRHAERGP GGALPPRHLL QQPAAERATA
HRGPGPRGAT RGVRGPGAHG AQISAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYKVEQKV FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM
PWTPYRTDTL TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN GKIVISQLNP
YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN EATGNKIDYI YNTDQSKDSL
VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY HVVKYSLDFG PLDSRSGQAH HGQVSYISPP
IHLDSDLERP PVREISTTGP LGTGSTTTST TLRTTTWSPG RSTTPSVSGR RNRSTSTPSP
AIEVLNDITT HVPSASPQIP ALEESCEAVE AREIMWFKTR QGQMAKQPCP AGTIGVSTYL
CLAPDGIWDP QGPDLSNCSS PWVNHITQKL KSGETAANIA RELAEQTRNH LNAGDITYSV
RAMDQLVGLL DVQLRNLTPG GKDSAARSLN KLQKRERSCR AYVQAMVETV NNLLQPQALN
AWRDLTTSDQ LRAATMLLDT VEESAFVLAD NLLKTDIVRE NTDNIQLEVA RLSTEGNLED
LKFPENTGHG STIQLSANTL KQNGRNGEIR VAFVLYNNLG PYLSTENASM KLGTEAMSTN
HSVIVNSPVI TAAINKEFSN KVYLADPVVF TVKHIKQSEE NFNPNCSFWS YSKRTMTGYW
STQGCRLLTT NKTHTTCSCN HLTNFAVLMA HVEVKHSDAV HDLLLDVITW VGILLSLVCL
LICIFTFCFF RGLQSDRNTI HKNLCISLFV AELLFLIGIN RTDQPIACAV FAALLHFFFL
AAFTWMFLEG VQLYIMLVEV FESEHSRRKY FYLVGYGMPA LIVAVSAAVD YRSYGTDKVC
WLRLDTYFIW SFIGPATLII MLNVIFLGIA LYKMFHHTAI LKPESGCLDN INYEDNRPFI
KSWVIGAIAL LCLLGLTWAF GLMYINESTV IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK
EYGKCLRTHC CSGRSTESSI GSGKTSGSRT PGRYSTGSQS RIRRMWNDTV RKQSESSFIT
GDINSSASLN RGAMANHLIS NALLRPHGTN NPYNTLLGEP AVCNNPSVSM YNAQEGLLNN
ARDTSVMDTL PLNGNHGNSY SIASGEYLSN CVQIIDRGYN HNETALEKKI LKELTSNYIP
SYLNNHERSS EQNRNLMNKL VNNLGSGSED DAIVLDDATS FNHEESLGLE LIHEESDAPL
LPPRVYSTEN HQLHHYTRRR IPQDHSESFF PLLTNEHTED LQSPHRDSLY TSMPALAGVP
TAESVTTSTQ TEPPPAKCGD AEDVYYKSMP NLGSRNHVHQ LHTYYQLGRG SSDGFIVPPN
KDGTPPEGSS KGPAHLVTSL
