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Protein

Adhesion G protein-coupled receptor B3

Gene

Adgrb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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
  • maintenance of synapse structure Source: MGI
  • motor learning Source: MGI
  • myoblast fusion Source: UniProtKB
  • negative regulation of angiogenesis Source: InterPro
  • neuron remodeling Source: MGI
  • positive regulation of synapse assembly Source: MGI
  • regulation of dendrite morphogenesis Source: UniProtKB

Keywordsi

Molecular functionG-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2441837 Adgrb3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 880ExtracellularCuratedAdd BLAST855
Transmembranei881 – 901Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini902 – 910CytoplasmicCurated9
Transmembranei911 – 931Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini932 – 939ExtracellularCurated8
Transmembranei940 – 960Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini961 – 981CytoplasmicCuratedAdd BLAST21
Transmembranei982 – 1002Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini1003 – 1023ExtracellularCuratedAdd BLAST21
Transmembranei1024 – 1044Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1045 – 1098CytoplasmicCuratedAdd BLAST54
Transmembranei1099 – 1119Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1120 – 1125ExtracellularCurated6
Transmembranei1126 – 1146Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1147 – 1522CytoplasmicCuratedAdd BLAST376

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001286626 – 1522Adhesion G protein-coupled receptor B3Add BLAST1497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi54N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi82N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi241N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi303 ↔ 336PROSITE-ProRule annotation
Disulfide bondi307 ↔ 342PROSITE-ProRule annotation
Disulfide bondi318 ↔ 326PROSITE-ProRule annotation
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi418N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi540N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei619PhosphoserineBy similarity1
Glycosylationi625N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi779N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi812N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi819 ↔ 851PROSITE-ProRule annotation
Glycosylationi828N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi839 ↔ 853PROSITE-ProRule annotation
Glycosylationi937N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1220PhosphoserineCombined sources1
Modified residuei1411PhosphoserineCombined sources1

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
PhosphoSitePlusiQ80ZF8

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

BgeeiENSMUSG00000033569
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

BioGridi229189, 2 interactors
IntActiQ80ZF8, 2 interactors
STRINGi10090.ENSMUSP00000035612

Structurei

3D structure databases

ProteinModelPortaliQ80ZF8
SMRiQ80ZF8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 159CUBAdd BLAST130
Domaini291 – 343TSP type-1 1PROSITE-ProRule annotationAdd BLAST53
Domaini345 – 398TSP type-1 2PROSITE-ProRule annotationAdd BLAST54
Domaini400 – 453TSP type-1 3PROSITE-ProRule annotationAdd BLAST54
Domaini455 – 508TSP type-1 4PROSITE-ProRule annotationAdd BLAST54
Domaini816 – 868GPSPROSITE-ProRule annotationAdd BLAST53

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEA0 Eukaryota
ENOG4111FBM LUCA
GeneTreeiENSGT00910000144013
HOGENOMiHOG000230916
HOVERGENiHBG004813
InParanoidiQ80ZF8
KOiK04598
OMAiGTLNPYC
OrthoDBiEOG091G00C7
TreeFamiTF331634

Family and domain databases

Gene3Di2.20.100.10, 4 hits
4.10.1240.10, 1 hit
InterProiView protein in InterPro
IPR032471 GAIN_dom_N
IPR017981 GPCR_2-like
IPR008077 GPCR_2_brain_angio_inhib
IPR036445 GPCR_2_extracell_dom_sf
IPR001879 GPCR_2_extracellular_dom
IPR000832 GPCR_2_secretin-like
IPR017983 GPCR_2_secretin-like_CS
IPR000203 GPS
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF00002 7tm_2, 1 hit
PF16489 GAIN, 1 hit
PF01825 GPS, 1 hit
PF02793 HRM, 1 hit
PF00090 TSP_1, 4 hits
PRINTSiPR01694 BAIPRECURSOR
PR00249 GPCRSECRETIN
SMARTiView protein in SMART
SM00303 GPS, 1 hit
SM00008 HormR, 1 hit
SM00209 TSP1, 4 hits
SUPFAMiSSF82895 SSF82895, 4 hits
PROSITEiView protein in PROSITE
PS00650 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

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)DescriptionActionsGraphical viewLength
Sequence conflicti215L → V in AAO27431 (Ref. 1) Curated1
Sequence conflicti683H → Y in AAO27431 (Ref. 1) Curated1
Sequence conflicti783V → I in AAO27431 (Ref. 1) Curated1

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

Similar proteinsi

Entry informationi

Entry nameiAGRB3_MOUSE
AccessioniPrimary (citable) accession number: Q80ZF8
Secondary accession number(s): G3XA05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 3, 2012
Last modified: March 28, 2018
This is version 124 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health