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Protein

Adhesion G protein-coupled receptor B3

Gene

Adgrb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (PubMed:23628982). Promotes myoblast fusion through ELMO/DOCK1 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • G-protein coupled receptor activity Source: UniProtKB-KW
  • GTPase activator activity Source: UniProtKB

GO - Biological processi

  • cell surface receptor signaling pathway Source: InterPro
  • myoblast fusion Source: UniProtKB
  • negative regulation of angiogenesis Source: InterPro
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of synapse assembly Source: MGI
  • regulation of dendrite morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor B3
Alternative name(s):
Brain-specific angiogenesis inhibitor 3
Gene namesi
Name:Adgrb3
Synonyms:Bai3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2441837. Adgrb3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 880855ExtracellularCuratedAdd
BLAST
Transmembranei881 – 90121Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini902 – 9109CytoplasmicCurated
Transmembranei911 – 93121Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini932 – 9398ExtracellularCurated
Transmembranei940 – 96021Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini961 – 98121CytoplasmicCuratedAdd
BLAST
Transmembranei982 – 100221Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini1003 – 102321ExtracellularCuratedAdd
BLAST
Transmembranei1024 – 104421Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini1045 – 109854CytoplasmicCuratedAdd
BLAST
Transmembranei1099 – 111921Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini1120 – 11256ExtracellularCurated
Transmembranei1126 – 114621Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini1147 – 1522376CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 15221497Adhesion G protein-coupled receptor B3PRO_0000012866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence analysis
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi303 ↔ 336PROSITE-ProRule annotation
Disulfide bondi307 ↔ 342PROSITE-ProRule annotation
Disulfide bondi318 ↔ 326PROSITE-ProRule annotation
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi357 ↔ 392PROSITE-ProRule annotation
Disulfide bondi361 ↔ 397PROSITE-ProRule annotation
Disulfide bondi372 ↔ 382PROSITE-ProRule annotation
Disulfide bondi412 ↔ 447PROSITE-ProRule annotation
Disulfide bondi416 ↔ 452PROSITE-ProRule annotation
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi427 ↔ 437PROSITE-ProRule annotation
Disulfide bondi467 ↔ 502PROSITE-ProRule annotation
Disulfide bondi471 ↔ 507PROSITE-ProRule annotation
Disulfide bondi482 ↔ 492PROSITE-ProRule annotation
Disulfide bondi514 ↔ 549PROSITE-ProRule annotation
Disulfide bondi537 ↔ 567PROSITE-ProRule annotation
Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence analysis
Modified residuei619 – 6191PhosphoserineBy similarity
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence analysis
Glycosylationi779 – 7791N-linked (GlcNAc...)Sequence analysis
Glycosylationi812 – 8121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi819 ↔ 851PROSITE-ProRule annotation
Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi839 ↔ 853PROSITE-ProRule annotation
Glycosylationi937 – 9371N-linked (GlcNAc...)Sequence analysis
Modified residuei1220 – 12201PhosphoserineCombined sources
Modified residuei1411 – 14111PhosphoserineCombined sources

Post-translational modificationi

The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ80ZF8.
PaxDbiQ80ZF8.
PRIDEiQ80ZF8.

PTM databases

iPTMnetiQ80ZF8.
PhosphoSiteiQ80ZF8.

Expressioni

Tissue specificityi

Brain-specific expression.1 Publication

Developmental stagei

Limited to the central nervous system (CNS) at all developmental stages. Peaks 1 day after birth.1 Publication

Gene expression databases

CleanExiMM_BAI3.
ExpressionAtlasiQ80ZF8. baseline and differential.
GenevisibleiQ80ZF8. MM.

Interactioni

Subunit structurei

Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts (via its TSRs) with C1QL1, C1QL2, C1QL3 and C1QL4. Interacts via (C-terminus) with ELMO1 (PubMed:23628982), ELMO2 and ELMO3.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035612.

Structurei

3D structure databases

ProteinModelPortaliQ80ZF8.
SMRiQ80ZF8. Positions 508-866.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 159130CUBAdd
BLAST
Domaini291 – 34353TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini345 – 39854TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 45354TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini455 – 50854TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini816 – 86853GPSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CUB domain.Curated
Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEA0. Eukaryota.
ENOG4111FBM. LUCA.
GeneTreeiENSGT00840000129679.
HOGENOMiHOG000230916.
HOVERGENiHBG004813.
InParanoidiQ80ZF8.
KOiK04598.
OMAiWDDSKTN.
TreeFamiTF331634.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR008077. GPCR_2_brain_angio_inhib.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSiPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80ZF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAVRNLLIY IFSTYLLVMF GFNAAQDFWC STLVKGVIYG SYSVSEMFPK
60 70 80 90 100
NFTNCTWTLE NPDPTKYSIY LKFSKKDLSC SNFSLLAYQF DHFSHEKIKD
110 120 130 140 150
LLRKNHSIMQ LCSSKNAFVF LQYDKNFIQI RRVFPTDFPG LQKKVEEDQK
160 170 180 190 200
SFFEFLVLNK VSPSQFGCHV LCTWLESCLK SENGRTESCG IMYTKCTCPQ
210 220 230 240 250
HLGEWGIDDQ SLVLLNNVVL PLNEQTEGCL TQELQTTQVC NLTREAKRPP
260 270 280 290 300
KEEFGMMGDH TIKSQRPRSV HEKRVPQEQA DAAKFMAQTG ESGVEEWSQW
310 320 330 340 350
SACSVTCGQG SQVRTRTCVS PYGTHCSGPL RESRVCNNTA LCPVHGVWEE
360 370 380 390 400
WSPWSLCSFT CGRGQRTRTR SCTPPQYGGR PCEGPETHHK PCNIALCPVD
410 420 430 440 450
GQWQEWSSWS HCSVTCSNGT QQRSRQCTAA AHGGSECRGP WAESRECYNP
460 470 480 490 500
ECTANGQWNQ WGHWSGCSKS CDGGWERRMR TCQGAAVTGQ QCEGTGEEVR
510 520 530 540 550
RCSEQRCPAP YEICPEDYLI SMVWKRTPAG DLAFNQCPLN ATGTTSRRCS
560 570 580 590 600
LSLHGVASWE QPSFARCISN EYRHLQHSIK EHLAKGQRML AGDGMSQVTK
610 620 630 640 650
TLLDLTQRKN FYAGDLLVSV EILRNVTDTF KRASYIPASD GVQNFFQIVS
660 670 680 690 700
NLLDEENKEK WEDAQQIYPG SIELMQVIED FIHIVGMGMM DFQNSYLMTG
710 720 730 740 750
NVVASIQKLP AASVLTDINF PMKGRKGMVD WARNSEDRVV IPKSIFTPVS
760 770 780 790 800
SKELDESSVF VLGAVLYKNL DLILPTLRNY TVVNSKVIVV TIRPEPKTTD
810 820 830 840 850
SFLEIELAHL ANGTLNPYCV LWDDSKSNES LGTWSTQGCK TVLTDASHTK
860 870 880 890 900
CLCDRLSTFA ILAQQPREIV MESSGTPSVT LIVGSGLSCL ALITLAVVYA
910 920 930 940 950
ALWRYIRSER SIILINFCLS IISSNILILV GQTQTHNKSI CTTTTAFLHF
960 970 980 990 1000
FFLASFCWVL TEAWQSYMAV TGKIRTRLIR KRFLCLGWGL PALVVATSVG
1010 1020 1030 1040 1050
FTRTKGYGTD HYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSR
1060 1070 1080 1090 1100
DGILDKKLKH RAGQMSEPHS GLTLKCAKCG VVSTTALSAT TASNAMASLW
1110 1120 1130 1140 1150
SSCVVLPLLA LTWMSAVLAM TDKRSILFQI LFAVFDSLQG FVIVMVHCIL
1160 1170 1180 1190 1200
RREVQDAFRC RLRNCQDPIN ADSSSSFPNG HAQIMTDFEK DVDIACRSVL
1210 1220 1230 1240 1250
HKDIGPCRAA TITGTLSRIS LNDDEEEKGT NPEGLSYSTL PGNVISKVII
1260 1270 1280 1290 1300
QQPTGLHMPM SMNELSNPCL KKENTELRRT VYLCTDDNLR GADMDIVHPQ
1310 1320 1330 1340 1350
ERMMESDYIV MPRSSVSTQP SMKEESKMNI GMETLPHERL LHYKVNPEFN
1360 1370 1380 1390 1400
MNPPVMDQFN MNLDQHLAPQ EHMQNLPFEP RTAVKNFMAS ELDDNVGLSR
1410 1420 1430 1440 1450
SETGSTISMS SLERRKSRYS DLDFEKVMHT RKRHMELFQE LNQKFQTLDR
1460 1470 1480 1490 1500
FRDIPNTSSM ENPAPNKNPW DTFKPPSEYQ HYTTINVLDT EAKDTLELRP
1510 1520
AEWEKCLNLP LDVQEGDFQT EV
Length:1,522
Mass (Da):171,314
Last modified:October 3, 2012 - v2
Checksum:i787882AC3F2B54EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151L → V in AAO27431 (Ref. 1) Curated
Sequence conflicti683 – 6831H → Y in AAO27431 (Ref. 1) Curated
Sequence conflicti783 – 7831V → I in AAO27431 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168406 mRNA. Translation: AAO27431.1.
AC116556 Genomic DNA. No translation available.
AC117221 Genomic DNA. No translation available.
AC121828 Genomic DNA. No translation available.
AC122187 Genomic DNA. No translation available.
AC129314 Genomic DNA. No translation available.
AC140308 Genomic DNA. No translation available.
CH466536 Genomic DNA. Translation: EDL14414.1.
CCDSiCCDS14855.1.
RefSeqiNP_783573.4. NM_175642.4.
UniGeneiMm.336569.

Genome annotation databases

EnsembliENSMUST00000041838; ENSMUSP00000035612; ENSMUSG00000033569.
ENSMUST00000135518; ENSMUSP00000119804; ENSMUSG00000033569.
ENSMUST00000151309; ENSMUSP00000116231; ENSMUSG00000033569.
GeneIDi210933.
KEGGimmu:210933.
UCSCiuc007amw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168406 mRNA. Translation: AAO27431.1.
AC116556 Genomic DNA. No translation available.
AC117221 Genomic DNA. No translation available.
AC121828 Genomic DNA. No translation available.
AC122187 Genomic DNA. No translation available.
AC129314 Genomic DNA. No translation available.
AC140308 Genomic DNA. No translation available.
CH466536 Genomic DNA. Translation: EDL14414.1.
CCDSiCCDS14855.1.
RefSeqiNP_783573.4. NM_175642.4.
UniGeneiMm.336569.

3D structure databases

ProteinModelPortaliQ80ZF8.
SMRiQ80ZF8. Positions 508-866.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035612.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ80ZF8.
PhosphoSiteiQ80ZF8.

Proteomic databases

MaxQBiQ80ZF8.
PaxDbiQ80ZF8.
PRIDEiQ80ZF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041838; ENSMUSP00000035612; ENSMUSG00000033569.
ENSMUST00000135518; ENSMUSP00000119804; ENSMUSG00000033569.
ENSMUST00000151309; ENSMUSP00000116231; ENSMUSG00000033569.
GeneIDi210933.
KEGGimmu:210933.
UCSCiuc007amw.2. mouse.

Organism-specific databases

CTDi577.
MGIiMGI:2441837. Adgrb3.

Phylogenomic databases

eggNOGiENOG410IEA0. Eukaryota.
ENOG4111FBM. LUCA.
GeneTreeiENSGT00840000129679.
HOGENOMiHOG000230916.
HOVERGENiHBG004813.
InParanoidiQ80ZF8.
KOiK04598.
OMAiWDDSKTN.
TreeFamiTF331634.

Miscellaneous databases

NextBioi373087.
PROiQ80ZF8.
SOURCEiSearch...

Gene expression databases

CleanExiMM_BAI3.
ExpressionAtlasiQ80ZF8. baseline and differential.
GenevisibleiQ80ZF8. MM.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR008077. GPCR_2_brain_angio_inhib.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSiPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse brain-specific angiogenesis inhibitor 3."
    Kim K.K., Kee H.J., Koh J.T.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Expression of brain-specific angiogenesis inhibitor 3 (BAI3) in normal brain and implications for BAI3 in ischemia-induced brain angiogenesis and malignant glioma."
    Kee H.J., Ahn K.Y., Choi K.C., Won Song J., Heo T., Jung S., Kim J.K., Bae C.S., Kim K.K.
    FEBS Lett. 569:307-316(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "The adhesion-GPCR BAI3, a gene linked to psychiatric disorders, regulates dendrite morphogenesis in neurons."
    Lanoue V., Usardi A., Sigoillot S.M., Talleur M., Iyer K., Mariani J., Isope P., Vodjdani G., Heintz N., Selimi F.
    Mol. Psychiatry 18:943-950(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELMO1, FUNCTION.

Entry informationi

Entry nameiAGRB3_MOUSE
AccessioniPrimary (citable) accession number: Q80ZF8
Secondary accession number(s): G3XA05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 3, 2012
Last modified: May 11, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.