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Protein

Adhesion G protein-coupled receptor L3

Gene

Adgrl3

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

Functioni

Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi332 – 3321Calcium1 Publication
Metal bindingi380 – 3801Calcium1 Publication
Metal bindingi381 – 3811Calcium; via carbonyl oxygen1 Publication
Metal bindingi435 – 4351Calcium; via carbonyl oxygen1 Publication

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • carbohydrate binding Source: UniProtKB-KW
  • G-protein coupled receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cell-cell adhesion Source: UniProtKB
  • cell surface receptor signaling pathway Source: InterPro
  • locomotion involved in locomotory behavior Source: UniProtKB
  • neuron migration Source: UniProtKB
  • positive regulation of synapse assembly Source: MGI
  • response to cocaine Source: UniProtKB
  • synapse assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Protein family/group databases

MEROPSiP02.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor L3Imported
Alternative name(s):
Latrophilin-3Imported
Lectomedin-3Imported
Gene namesi
Name:Adgrl3Imported
Synonyms:Kiaa0768Imported, Lec3Imported, Lphn3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2441950. Adgrl3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 949930ExtracellularSequence analysisAdd
BLAST
Transmembranei950 – 97021Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini971 – 9788CytoplasmicSequence analysis
Transmembranei979 – 99921Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini1000 – 10078ExtracellularSequence analysis
Transmembranei1008 – 102821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini1029 – 105022CytoplasmicSequence analysisAdd
BLAST
Transmembranei1051 – 107121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini1072 – 108817ExtracellularSequence analysisAdd
BLAST
Transmembranei1089 – 110921Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini1110 – 114233CytoplasmicSequence analysisAdd
BLAST
Transmembranei1143 – 116321Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini1164 – 11696ExtracellularSequence analysis
Transmembranei1170 – 119021Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini1191 – 1537347CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice are viable and present no obvious physical phenotype. Compared to wild-type, mutants are hyperactive, and their dorsal striatum contains higher levels of the neurotransmitters dopamine and serotonin. Cocaine treatment causes a higher increase in locomotor activity than in wild-type.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441P → N: Strongly reduces FLRT2 binding; when associated with T-246. 1 Publication
Mutagenesisi246 – 2461R → T: Strongly reduces FLRT2 binding; when associated with N-244. 1 Publication
Mutagenesisi267 – 2671T → N: Strongly reduces FLRT2 binding; when associated with T-269. 1 Publication
Mutagenesisi269 – 2691K → T: Strongly reduces FLRT2 binding; when associated with N-267. 1 Publication
Mutagenesisi292 – 2921R → N: Abolishes interaction with FLRT2; when associated with T-294. 1 Publication
Mutagenesisi294 – 2941R → T: Abolishes interaction with FLRT2; when associated with N-292. 1 Publication
Mutagenesisi323 – 3231Y → A: Abolishes FLRT3 binding. 1 Publication
Mutagenesisi324 – 3241R → N: Abolishes interaction with FLRT2; when associated with T-326. 1 Publication
Mutagenesisi326 – 3261G → T: Abolishes interaction with FLRT2; when associated with N-324. 1 Publication
Mutagenesisi332 – 3321D → A: Strongly reduces FLRT3 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 15371518Adhesion G protein-coupled receptor L3PRO_0000070344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 134Combined sources
Disulfide bondi113 ↔ 191Combined sources
Disulfide bondi146 ↔ 178Combined sources
Disulfide bondi159 ↔ 165Combined sources
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication
Disulfide bondi203 ↔ 385PROSITE-ProRule annotationCombined sources
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence analysis
Glycosylationi617 – 6171N-linked (GlcNAc...)Sequence analysis
Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence analysis
Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence analysis
Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence analysis
Glycosylationi911 – 9111N-linked (GlcNAc...)Sequence analysis
Glycosylationi1000 – 10001N-linked (GlcNAc...)Sequence analysis
Glycosylationi1166 – 11661N-linked (GlcNAc...)Sequence analysis
Modified residuei1254 – 12541PhosphoserineCombined sources
Modified residuei1522 – 15221PhosphoserineCombined sources

Post-translational modificationi

Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit.By similarity
O-glycosylated (major) and N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ80TS3.
PaxDbiQ80TS3.
PeptideAtlasiQ80TS3.
PRIDEiQ80TS3.

PTM databases

iPTMnetiQ80TS3.
PhosphoSiteiQ80TS3.

Expressioni

Gene expression databases

BgeeiQ80TS3.
CleanExiMM_LPHN3.
ExpressionAtlasiQ80TS3. baseline and differential.
GenevisibleiQ80TS3. MM.

Interactioni

Subunit structurei

Interacts (via olfactomedin-like domain) with FLRT3 (via extracellular domain); the interaction is direct(PubMed:22405201, PubMed:24739570, PubMed:26235031). Identified in a complex with FLRT3 and UNC5B; does not interact with UNC5B by itself. Identified in a complex with FLRT3 and UNC5D; does not interact with UNC5D by itself (By similarity). Interacts (via olfactomedin-like domain) with FLRT1 (via extracellular domain) (PubMed:22405201). Interacts (via olfactomedin-like domain) with FLRT2 (via extracellular domain) (PubMed:22405201, PubMed:25728924). Interacts (via extracellular domain) with TENM1 (PubMed:24739570). Interacts (via extracellular domain) with TENM3 (PubMed:22405201).By similarity4 Publications

Protein-protein interaction databases

DIPiDIP-32218N.
IntActiQ80TS3. 1 interaction.
STRINGi10090.ENSMUSP00000072336.

Structurei

Secondary structure

1
1537
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 21813Combined sources
Beta strandi220 – 2278Combined sources
Beta strandi237 – 2415Combined sources
Turni244 – 2463Combined sources
Beta strandi249 – 2557Combined sources
Helixi256 – 2616Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi274 – 2774Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi285 – 2906Combined sources
Beta strandi293 – 3008Combined sources
Turni301 – 3044Combined sources
Beta strandi305 – 3117Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi330 – 3367Combined sources
Beta strandi339 – 3468Combined sources
Turni347 – 3515Combined sources
Beta strandi352 – 3587Combined sources
Turni360 – 3623Combined sources
Beta strandi365 – 37410Combined sources
Helixi375 – 3773Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi387 – 3937Combined sources
Beta strandi405 – 4128Combined sources
Turni413 – 4164Combined sources
Beta strandi417 – 4248Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi434 – 4385Combined sources
Turni439 – 4424Combined sources
Beta strandi443 – 4486Combined sources
Beta strandi451 – 46010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RMKX-ray1.61A199-495[»]
4RMLX-ray1.60A199-495[»]
4YEBX-ray3.19A199-495[»]
5AFBX-ray2.16A97-459[»]
5FTTX-ray3.40C/D/G/H92-463[»]
5FTUX-ray6.01C/D/G/H/K/L92-463[»]
ProteinModelPortaliQ80TS3.
SMRiQ80TS3. Positions 97-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 19290SUEL-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini202 – 461260Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST
Domaini883 – 93452GPSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 34731Interaction with FLRT3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1470 – 14734Poly-Ala

Domaini

The Olfactomedin-like domain is required for the synapse-promoting function and the interaction with FLRT3. The Olfactomedin-like and the SUEL-type lectin domains are required for the interaction with TENM1.1 Publication

Sequence similaritiesi

Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation
Contains 1 SUEL-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3545. Eukaryota.
KOG4193. Eukaryota.
KOG4729. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiQ80TS3.
KOiK04594.
PhylomeDBiQ80TS3.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR003924. GPCR_2_latrophilin.
IPR003334. GPCR_2_latrophilin_rcpt_C.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR015630. Latrophilin-3.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF60. PTHR12011:SF60. 2 hits.
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF02140. Gal_Lectin. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF02354. Latrophilin. 2 hits.
PF02191. OLF. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]
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.
PS51132. OLF. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TS3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWPPQLLILT MLLAPVVHGG KHNERHPALA APLRHAERSP GGALPPRHLL
60 70 80 90 100
QQPAAERSTA HRGQGPRGAA RGVRGPGAPG AQIAAQAFSR APIPMAVVRR
110 120 130 140 150
ELSCESYPIE LRCPGTDVIM IESANYGRTD DKICDSDPAQ MENIRCYLPD
160 170 180 190 200
AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG TYKYLEVQYE CVPYKVEQKV
210 220 230 240 250
FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM PWTPYRTDTL
260 270 280 290 300
TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
310 320 330 340 350
LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN
360 370 380 390 400
GKIVISQLNP YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN
410 420 430 440 450
EATGNKIDYI YNTDQSKDSL VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY
460 470 480 490 500
HVVKYSLDFG PLDSRSGPVH HGQVSYISPP IHLDSELERP PVRGISTTGS
510 520 530 540 550
LGMGSTTTST TLRTTTWNIG RSTTASLPGR RNRSTSTPSP AVEVLDDVTT
560 570 580 590 600
HLPSAASQIP AMEESCEAVE AREIMWFKTR QGQVAKQPCP AGTIGVSTYL
610 620 630 640 650
CLAPDGIWDP QGPDLSNCSS PWVNHITQKL KSGETAANIA RELAEQTRNH
660 670 680 690 700
LNAGDITYSV RAMDQLVGLL DVQLRNLTPG GKDSAARSLN KLQKRERSCR
710 720 730 740 750
AYVQAMVETV NNLLQPQALN AWRDLTTSDQ LRAATMLLDT VEESAFVLAD
760 770 780 790 800
NLLKTDIVRE NTDNIQLEVA RLSTEGNLED LKFPENMGHG STIQLSANTL
810 820 830 840 850
KQNGRNGEIR VAFVLYNNLG PYLSTENASM KLGTEAMSTN HSVIVNSPVI
860 870 880 890 900
TAAINKEFSN KVYLADPVVF TVKHIKQSEE NFNPNCSFWS YSKRTMTGYW
910 920 930 940 950
STQGCRLLTT NKTHTTCSCN HLTNFAVLMA HVEVKHSDAV HDLLLDVITW
960 970 980 990 1000
VGILLSLVCL LICIFTFCFF RGLQSDRNTI HKNLCISLFV AELLFLIGIN
1010 1020 1030 1040 1050
RTDQPIACAV FAALLHFFFL AAFTWMFLEG VQLYIMLVEV FESEHSRRKY
1060 1070 1080 1090 1100
FYLVGYGMPA LIVAVSAAVD YRSYGTDKVC WLRLDTYFIW SFIGPATLII
1110 1120 1130 1140 1150
MLNVIFLGIA LYKMFHHTAI LKPESGCLDN INYEDNRPFI KSWVIGAIAL
1160 1170 1180 1190 1200
LCLLGLTWAF GLMYINESTV IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK
1210 1220 1230 1240 1250
EYGKCLRTHC CSGKSTESSI GSGKTSGSRT PGRYSTGSQS RIRRMWNDTV
1260 1270 1280 1290 1300
RKQSESSFIT GDINSSASLN REGLLNNARD TSVMDTLPLN GNHGNSYSIA
1310 1320 1330 1340 1350
GGEYLSNCVQ IIDRGYNHNE TALEKKILKE LTSNYIPSYL NNHERSSEQN
1360 1370 1380 1390 1400
RNMMNKLVNN LGSGSEDDAI VLDDAASFNH EESLGLELIH EESDAPLLPP
1410 1420 1430 1440 1450
RVYSTDNHQP HHYSRRRFPQ DHSESFFPLL TDEHTEDLQS PHRDSLYTSM
1460 1470 1480 1490 1500
PALAGVPAAD SVTTSTQTEA AAAKGGDAED VYYKSMPNLG SRNHVHPLHA
1510 1520 1530
YYQLGRGSSD GFIVPPNKDG ASPEGTSKGP AHLVTSL
Length:1,537
Mass (Da):171,080
Last modified:January 9, 2007 - v3
Checksum:iF55EAB142C987A69
GO
Isoform 2 (identifier: Q80TS3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1132-1140: Missing.
     1272-1351: EGLLNNARDT...NHERSSEQNR → GAMANHLISN...KCHGYSTTEW
     1352-1537: Missing.

Show »
Length:1,342
Mass (Da):149,585
Checksum:iDC564A59AC9FA61D
GO
Isoform 3 (identifier: Q80TS3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1272-1272: E → EPYRETK

Note: No experimental confirmation available.
Show »
Length:1,543
Mass (Da):171,855
Checksum:i777BF282BBB9F19A
GO
Isoform 4 (identifier: Q80TS3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-239: Missing.

Note: No experimental confirmation available.
Show »
Length:1,298
Mass (Da):144,737
Checksum:i6049A189631565C6
GO
Isoform 5 (identifier: Q80TS3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1132-1140: Missing.

Note: No experimental confirmation available.
Show »
Length:1,528
Mass (Da):169,930
Checksum:i0821FFBFD18CA9BB
GO
Isoform 6 (identifier: Q80TS3-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-200: KVEQKV → I
     650-650: H → Q
     651-1537: Missing.

Note: No experimental confirmation available.
Show »
Length:645
Mass (Da):71,505
Checksum:i4F331FC4398D65BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811A → S in AAH94668 (PubMed:15489334).Curated
Sequence conflicti1252 – 12521K → R in BAE27870 (PubMed:16141072).Curated
Sequence conflicti1375 – 13751A → T in BAE26219 (PubMed:16141072).Curated
Sequence conflicti1495 – 14951V → M in BAE26219 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 239239Missing in isoform 4. 1 PublicationVSP_022138Add
BLAST
Alternative sequencei195 – 2006KVEQKV → I in isoform 6. 1 PublicationVSP_022139
Alternative sequencei650 – 6501H → Q in isoform 6. 1 PublicationVSP_022140
Alternative sequencei651 – 1537887Missing in isoform 6. 1 PublicationVSP_022141Add
BLAST
Alternative sequencei1132 – 11409Missing in isoform 2 and isoform 5. 2 PublicationsVSP_010121
Alternative sequencei1272 – 135180EGLLN…SEQNR → GAMANHLISNALLRPHGTNN PYNTLLGEPAVCNNPSISMY NTQEPYRETSMGVKLNIAYQ IGASEQCQGYKCHGYSTTEW in isoform 2. 1 PublicationVSP_010122Add
BLAST
Alternative sequencei1272 – 12721E → EPYRETK in isoform 3. 1 PublicationVSP_022142
Alternative sequencei1352 – 1537186Missing in isoform 2. 1 PublicationVSP_010123Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK145069 mRNA. Translation: BAE26219.1.
AK147374 mRNA. Translation: BAE27870.1.
BC058992 mRNA. Translation: AAH58992.1.
BC088989 mRNA. Translation: AAH88989.1.
BC094668 mRNA. Translation: AAH94668.1.
AK122367 mRNA. Translation: BAC65649.1.
AY255584 mRNA. Translation: AAO85096.1.
CCDSiCCDS39122.1. [Q80TS3-3]
RefSeqiNP_941991.1. NM_198702.2. [Q80TS3-3]
XP_011247767.1. XM_011249465.1. [Q80TS3-3]
XP_011247768.1. XM_011249466.1. [Q80TS3-1]
XP_011247770.1. XM_011249468.1. [Q80TS3-5]
XP_011247773.1. XM_011249471.1. [Q80TS3-2]
UniGeneiMm.273631.
Mm.461016.

Genome annotation databases

EnsembliENSMUST00000072521; ENSMUSP00000072336; ENSMUSG00000037605. [Q80TS3-3]
ENSMUST00000117407; ENSMUSP00000112388; ENSMUSG00000037605. [Q80TS3-2]
ENSMUST00000122356; ENSMUSP00000113600; ENSMUSG00000037605. [Q80TS3-5]
GeneIDi319387.
KEGGimmu:319387.
UCSCiuc008xwk.1. mouse. [Q80TS3-6]
uc008xwn.1. mouse. [Q80TS3-1]
uc008xwp.1. mouse. [Q80TS3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK145069 mRNA. Translation: BAE26219.1.
AK147374 mRNA. Translation: BAE27870.1.
BC058992 mRNA. Translation: AAH58992.1.
BC088989 mRNA. Translation: AAH88989.1.
BC094668 mRNA. Translation: AAH94668.1.
AK122367 mRNA. Translation: BAC65649.1.
AY255584 mRNA. Translation: AAO85096.1.
CCDSiCCDS39122.1. [Q80TS3-3]
RefSeqiNP_941991.1. NM_198702.2. [Q80TS3-3]
XP_011247767.1. XM_011249465.1. [Q80TS3-3]
XP_011247768.1. XM_011249466.1. [Q80TS3-1]
XP_011247770.1. XM_011249468.1. [Q80TS3-5]
XP_011247773.1. XM_011249471.1. [Q80TS3-2]
UniGeneiMm.273631.
Mm.461016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RMKX-ray1.61A199-495[»]
4RMLX-ray1.60A199-495[»]
4YEBX-ray3.19A199-495[»]
5AFBX-ray2.16A97-459[»]
5FTTX-ray3.40C/D/G/H92-463[»]
5FTUX-ray6.01C/D/G/H/K/L92-463[»]
ProteinModelPortaliQ80TS3.
SMRiQ80TS3. Positions 97-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-32218N.
IntActiQ80TS3. 1 interaction.
STRINGi10090.ENSMUSP00000072336.

Protein family/group databases

MEROPSiP02.011.
GPCRDBiSearch...

PTM databases

iPTMnetiQ80TS3.
PhosphoSiteiQ80TS3.

Proteomic databases

MaxQBiQ80TS3.
PaxDbiQ80TS3.
PeptideAtlasiQ80TS3.
PRIDEiQ80TS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072521; ENSMUSP00000072336; ENSMUSG00000037605. [Q80TS3-3]
ENSMUST00000117407; ENSMUSP00000112388; ENSMUSG00000037605. [Q80TS3-2]
ENSMUST00000122356; ENSMUSP00000113600; ENSMUSG00000037605. [Q80TS3-5]
GeneIDi319387.
KEGGimmu:319387.
UCSCiuc008xwk.1. mouse. [Q80TS3-6]
uc008xwn.1. mouse. [Q80TS3-1]
uc008xwp.1. mouse. [Q80TS3-3]

Organism-specific databases

CTDi23284.
MGIiMGI:2441950. Adgrl3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3545. Eukaryota.
KOG4193. Eukaryota.
KOG4729. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiQ80TS3.
KOiK04594.
PhylomeDBiQ80TS3.

Miscellaneous databases

ChiTaRSiLphn3. mouse.
PROiQ80TS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ80TS3.
CleanExiMM_LPHN3.
ExpressionAtlasiQ80TS3. baseline and differential.
GenevisibleiQ80TS3. MM.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR003924. GPCR_2_latrophilin.
IPR003334. GPCR_2_latrophilin_rcpt_C.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR015630. Latrophilin-3.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF60. PTHR12011:SF60. 2 hits.
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF02140. Gal_Lectin. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF02354. Latrophilin. 2 hits.
PF02191. OLF. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]
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.
PS51132. OLF. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 672-1537 (ISOFORM 5).
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 6).
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-1537 (ISOFORM 1).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-981.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1254 AND SER-1522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Lung.
  6. "Initial characterization of mice null for Lphn3, a gene implicated in ADHD and addiction."
    Wallis D., Hill D.S., Mendez I.A., Abbott L.C., Finnell R.H., Wellman P.J., Setlow B.
    Brain Res. 1463:85-92(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development."
    O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S., Yates J.R. III, Ghosh A.
    Neuron 73:903-910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TENM3; FLRT1; FLRT2 AND FLRT3, SUBCELLULAR LOCATION, FUNCTION.
  8. "LPHN3, a presynaptic adhesion-GPCR implicated in ADHD, regulates the strength of neocortical layer 2/3 synaptic input to layer 5."
    O'Sullivan M.L., Martini F., von Daake S., Comoletti D., Ghosh A.
    Neural Dev. 9:7-7(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION, INTERACTION WITH FLRT3 AND TENM1, DOMAIN, SUBCELLULAR LOCATION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 97-459 IN COMPLEX WITH CALCIUM IONS, FUNCTION, INTERACTION WITH FLRT2, DISULFIDE BONDS, GLYCOSYLATION AT ASN-161, MUTAGENESIS OF PRO-244; ARG-246; THR-267; LYS-269; ARG-292; ARG-294; ARG-324 AND GLY-326.
  10. "Structural and mechanistic insights into the latrophilin3-FLRT3 complex that mediates glutamatergic synapse development."
    Ranaivoson F.M., Liu Q., Martini F., Bergami F., von Daake S., Li S., Lee D., Demeler B., Hendrickson W.A., Comoletti D.
    Structure 23:1665-1677(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 199-495 IN COMPLEX WITH FLRT3 AND CALCIUM IONS, INTERACTION WITH FLRT3, MUTAGENESIS OF TYR-323 AND ASP-332.

Entry informationi

Entry nameiAGRL3_MOUSE
AccessioniPrimary (citable) accession number: Q80TS3
Secondary accession number(s): Q3UHI7
, Q3UM79, Q504Z9, Q5HZJ6, Q80T56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.