AGRB3_MOUSE
ID AGRB3_MOUSE Reviewed; 1522 AA.
AC Q80ZF8; G3XA05;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Adhesion G protein-coupled receptor B3;
DE AltName: Full=Brain-specific angiogenesis inhibitor 3;
DE Flags: Precursor;
GN Name=Adgrb3; Synonyms=Bai3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RA Kim K.K., Kee H.J., Koh J.T.;
RT "Mouse brain-specific angiogenesis inhibitor 3.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15225653; DOI=10.1016/j.febslet.2004.06.011;
RA Kee H.J., Ahn K.Y., Choi K.C., Won Song J., Heo T., Jung S., Kim J.K.,
RA Bae C.S., Kim K.K.;
RT "Expression of brain-specific angiogenesis inhibitor 3 (BAI3) in normal
RT brain and implications for BAI3 in ischemia-induced brain angiogenesis and
RT malignant glioma.";
RL FEBS Lett. 569:307-316(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND SER-1411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH ELMO1, AND FUNCTION.
RX PubMed=23628982; DOI=10.1038/mp.2013.46;
RA Lanoue V., Usardi A., Sigoillot S.M., Talleur M., Iyer K., Mariani J.,
RA Isope P., Vodjdani G., Heintz N., Selimi F.;
RT "The adhesion-GPCR BAI3, a gene linked to psychiatric disorders, regulates
RT dendrite morphogenesis in neurons.";
RL Mol. Psychiatry 18:943-950(2013).
CC -!- FUNCTION: Receptor that plays a role in the regulation of
CC synaptogenesis and dendritic spine formation at least partly via
CC interaction with ELMO1 and RAC1 activity (PubMed:23628982). Promotes
CC myoblast fusion through ELMO/DOCK1 (By similarity).
CC {ECO:0000250|UniProtKB:O60242, ECO:0000269|PubMed:23628982}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region non-covalently linked to a seven-transmembrane moiety. Interacts
CC (via its TSRs) with C1QL1, C1QL2, C1QL3 and C1QL4. Interacts via (C-
CC terminus) with ELMO1 (PubMed:23628982), ELMO2 and ELMO3.
CC {ECO:0000250|UniProtKB:O60242, ECO:0000269|PubMed:23628982}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60242};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain-specific expression.
CC {ECO:0000269|PubMed:15225653}.
CC -!- DEVELOPMENTAL STAGE: Limited to the central nervous system (CNS) at all
CC developmental stages. Peaks 1 day after birth.
CC {ECO:0000269|PubMed:15225653}.
CC -!- PTM: The endogenous protein is proteolytically cleaved into 2 subunits,
CC an extracellular subunit and a seven-transmembrane subunit.
CC {ECO:0000250|UniProtKB:O60242}.
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; AY168406; AAO27431.1; -; mRNA.
DR EMBL; AC116556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466536; EDL14414.1; -; Genomic_DNA.
DR CCDS; CCDS14855.1; -.
DR RefSeq; NP_783573.4; NM_175642.4.
DR AlphaFoldDB; Q80ZF8; -.
DR SMR; Q80ZF8; -.
DR BioGRID; 229189; 3.
DR IntAct; Q80ZF8; 4.
DR MINT; Q80ZF8; -.
DR STRING; 10090.ENSMUSP00000116231; -.
DR GlyConnect; 2109; 1 N-Linked glycan (1 site).
DR GlyGen; Q80ZF8; 13 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q80ZF8; -.
DR PhosphoSitePlus; Q80ZF8; -.
DR MaxQB; Q80ZF8; -.
DR PaxDb; Q80ZF8; -.
DR PRIDE; Q80ZF8; -.
DR ProteomicsDB; 281957; -.
DR Antibodypedia; 2938; 239 antibodies from 32 providers.
DR DNASU; 210933; -.
DR Ensembl; ENSMUST00000041838; ENSMUSP00000035612; ENSMUSG00000033569.
DR Ensembl; ENSMUST00000135518; ENSMUSP00000119804; ENSMUSG00000033569.
DR Ensembl; ENSMUST00000151309; ENSMUSP00000116231; ENSMUSG00000033569.
DR GeneID; 210933; -.
DR KEGG; mmu:210933; -.
DR UCSC; uc007amw.2; mouse.
DR CTD; 577; -.
DR MGI; MGI:2441837; Adgrb3.
DR VEuPathDB; HostDB:ENSMUSG00000033569; -.
DR eggNOG; ENOG502QRKJ; Eukaryota.
DR GeneTree; ENSGT00940000155081; -.
DR InParanoid; Q80ZF8; -.
DR OMA; CESKNAF; -.
DR OrthoDB; 27621at2759; -.
DR PhylomeDB; Q80ZF8; -.
DR TreeFam; TF331634; -.
DR BioGRID-ORCS; 210933; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adgrb3; mouse.
DR PRO; PR:Q80ZF8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80ZF8; protein.
DR Bgee; ENSMUSG00000033569; Expressed in lateral septal nucleus and 116 other tissues.
DR ExpressionAtlas; Q80ZF8; baseline and differential.
DR Genevisible; Q80ZF8; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0099558; P:maintenance of synapse structure; IMP:MGI.
DR GO; GO:0061743; P:motor learning; IGI:MGI.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0016322; P:neuron remodeling; IGI:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
DR Gene3D; 2.20.100.10; -; 4.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR008077; GPCR_2_brain_angio_inhib.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF19188; AGRB_N; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00090; TSP_1; 4.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF82895; SSF82895; 4.
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; PS50092; TSP1; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1522
FT /note="Adhesion G protein-coupled receptor B3"
FT /id="PRO_0000012866"
FT TOPO_DOM 26..880
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..901
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 911..931
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..939
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 940..960
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 982..1002
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1023
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1024..1044
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1099..1119
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1120..1125
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1126..1146
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1147..1522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..159
FT /note="CUB"
FT DOMAIN 291..343
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 345..398
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 400..453
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 455..508
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 816..868
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60242"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 303..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 307..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 318..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 357..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 361..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 372..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 412..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 416..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 427..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 467..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 471..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 482..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 514..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 537..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 819..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 839..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 215
FT /note="L -> V (in Ref. 1; AAO27431)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="H -> Y (in Ref. 1; AAO27431)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="V -> I (in Ref. 1; AAO27431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1522 AA; 171314 MW; 787882AC3F2B54EB CRC64;
MKAVRNLLIY IFSTYLLVMF GFNAAQDFWC STLVKGVIYG SYSVSEMFPK NFTNCTWTLE
NPDPTKYSIY LKFSKKDLSC SNFSLLAYQF DHFSHEKIKD LLRKNHSIMQ LCSSKNAFVF
LQYDKNFIQI RRVFPTDFPG LQKKVEEDQK SFFEFLVLNK VSPSQFGCHV LCTWLESCLK
SENGRTESCG IMYTKCTCPQ HLGEWGIDDQ SLVLLNNVVL PLNEQTEGCL TQELQTTQVC
NLTREAKRPP KEEFGMMGDH TIKSQRPRSV HEKRVPQEQA DAAKFMAQTG ESGVEEWSQW
SACSVTCGQG SQVRTRTCVS PYGTHCSGPL RESRVCNNTA LCPVHGVWEE WSPWSLCSFT
CGRGQRTRTR SCTPPQYGGR PCEGPETHHK PCNIALCPVD GQWQEWSSWS HCSVTCSNGT
QQRSRQCTAA AHGGSECRGP WAESRECYNP ECTANGQWNQ WGHWSGCSKS CDGGWERRMR
TCQGAAVTGQ QCEGTGEEVR RCSEQRCPAP YEICPEDYLI SMVWKRTPAG DLAFNQCPLN
ATGTTSRRCS LSLHGVASWE QPSFARCISN EYRHLQHSIK EHLAKGQRML AGDGMSQVTK
TLLDLTQRKN FYAGDLLVSV EILRNVTDTF KRASYIPASD GVQNFFQIVS NLLDEENKEK
WEDAQQIYPG SIELMQVIED FIHIVGMGMM DFQNSYLMTG NVVASIQKLP AASVLTDINF
PMKGRKGMVD WARNSEDRVV IPKSIFTPVS SKELDESSVF VLGAVLYKNL DLILPTLRNY
TVVNSKVIVV TIRPEPKTTD SFLEIELAHL ANGTLNPYCV LWDDSKSNES LGTWSTQGCK
TVLTDASHTK CLCDRLSTFA ILAQQPREIV MESSGTPSVT LIVGSGLSCL ALITLAVVYA
ALWRYIRSER SIILINFCLS IISSNILILV GQTQTHNKSI CTTTTAFLHF FFLASFCWVL
TEAWQSYMAV TGKIRTRLIR KRFLCLGWGL PALVVATSVG FTRTKGYGTD HYCWLSLEGG
LLYAFVGPAA AVVLVNMVIG ILVFNKLVSR DGILDKKLKH RAGQMSEPHS GLTLKCAKCG
VVSTTALSAT TASNAMASLW SSCVVLPLLA LTWMSAVLAM TDKRSILFQI LFAVFDSLQG
FVIVMVHCIL RREVQDAFRC RLRNCQDPIN ADSSSSFPNG HAQIMTDFEK DVDIACRSVL
HKDIGPCRAA TITGTLSRIS LNDDEEEKGT NPEGLSYSTL PGNVISKVII QQPTGLHMPM
SMNELSNPCL KKENTELRRT VYLCTDDNLR GADMDIVHPQ ERMMESDYIV MPRSSVSTQP
SMKEESKMNI GMETLPHERL LHYKVNPEFN MNPPVMDQFN MNLDQHLAPQ EHMQNLPFEP
RTAVKNFMAS ELDDNVGLSR SETGSTISMS SLERRKSRYS DLDFEKVMHT RKRHMELFQE
LNQKFQTLDR FRDIPNTSSM ENPAPNKNPW DTFKPPSEYQ HYTTINVLDT EAKDTLELRP
AEWEKCLNLP LDVQEGDFQT EV
