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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)DescriptionActionsGraphical viewLength
Metal bindingi332Calcium1 Publication1
Metal bindingi380Calcium1 Publication1
Metal bindingi381Calcium; via carbonyl oxygen1 Publication1
Metal bindingi435Calcium; via carbonyl oxygen1 Publication1

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)DescriptionActionsGraphical viewLength
Topological domaini20 – 949ExtracellularSequence analysisAdd BLAST930
Transmembranei950 – 970Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini971 – 978CytoplasmicSequence analysis8
Transmembranei979 – 999Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini1000 – 1007ExtracellularSequence analysis8
Transmembranei1008 – 1028Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini1029 – 1050CytoplasmicSequence analysisAdd BLAST22
Transmembranei1051 – 1071Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini1072 – 1088ExtracellularSequence analysisAdd BLAST17
Transmembranei1089 – 1109Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1110 – 1142CytoplasmicSequence analysisAdd BLAST33
Transmembranei1143 – 1163Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1164 – 1169ExtracellularSequence analysis6
Transmembranei1170 – 1190Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1191 – 1537CytoplasmicSequence analysisAdd BLAST347

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)DescriptionActionsGraphical viewLength
Mutagenesisi244P → N: Strongly reduces FLRT2 binding; when associated with T-246. 1 Publication1
Mutagenesisi246R → T: Strongly reduces FLRT2 binding; when associated with N-244. 1 Publication1
Mutagenesisi267T → N: Strongly reduces FLRT2 binding; when associated with T-269. 1 Publication1
Mutagenesisi269K → T: Strongly reduces FLRT2 binding; when associated with N-267. 1 Publication1
Mutagenesisi292R → N: Abolishes interaction with FLRT2; when associated with T-294. 1 Publication1
Mutagenesisi294R → T: Abolishes interaction with FLRT2; when associated with N-292. 1 Publication1
Mutagenesisi323Y → A: Abolishes FLRT3 binding. 1 Publication1
Mutagenesisi324R → N: Abolishes interaction with FLRT2; when associated with T-326. 1 Publication1
Mutagenesisi326G → T: Abolishes interaction with FLRT2; when associated with N-324. 1 Publication1
Mutagenesisi332D → A: Strongly reduces FLRT3 binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000007034420 – 1537Adhesion G protein-coupled receptor L3Add BLAST1518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104 ↔ 134Combined sources
Disulfide bondi113 ↔ 191Combined sources
Disulfide bondi146 ↔ 178Combined sources
Disulfide bondi159 ↔ 165Combined sources
Glycosylationi161N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Disulfide bondi203 ↔ 385PROSITE-ProRule annotationCombined sources
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Glycosylationi617N-linked (GlcNAc...)Sequence analysis1
Glycosylationi827N-linked (GlcNAc...)Sequence analysis1
Glycosylationi840N-linked (GlcNAc...)Sequence analysis1
Glycosylationi885N-linked (GlcNAc...)Sequence analysis1
Glycosylationi911N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1000N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1166N-linked (GlcNAc...)Sequence analysis1
Modified residuei1254PhosphoserineCombined sources1
Modified residuei1522PhosphoserineCombined sources1

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

PaxDbiQ80TS3.
PeptideAtlasiQ80TS3.
PRIDEiQ80TS3.

PTM databases

iPTMnetiQ80TS3.
PhosphoSitePlusiQ80TS3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037605.
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 interactor.
STRINGi10090.ENSMUSP00000072336.

Structurei

Secondary structure

11537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi101 – 104Combined sources4
Beta strandi108 – 112Combined sources5
Beta strandi118 – 129Combined sources12
Beta strandi131 – 134Combined sources4
Turni138 – 141Combined sources4
Helixi151 – 158Combined sources8
Turni159 – 161Combined sources3
Beta strandi163 – 168Combined sources6
Turni171 – 173Combined sources3
Beta strandi184 – 192Combined sources9
Beta strandi199 – 202Combined sources4
Beta strandi206 – 218Combined sources13
Beta strandi220 – 227Combined sources8
Beta strandi230 – 232Combined sources3
Beta strandi237 – 241Combined sources5
Turni244 – 246Combined sources3
Beta strandi249 – 255Combined sources7
Helixi256 – 261Combined sources6
Beta strandi265 – 269Combined sources5
Beta strandi274 – 277Combined sources4
Beta strandi280 – 282Combined sources3
Beta strandi285 – 290Combined sources6
Beta strandi293 – 300Combined sources8
Turni301 – 304Combined sources4
Beta strandi305 – 311Combined sources7
Beta strandi318 – 321Combined sources4
Beta strandi330 – 336Combined sources7
Beta strandi339 – 346Combined sources8
Turni347 – 351Combined sources5
Beta strandi352 – 358Combined sources7
Turni360 – 362Combined sources3
Beta strandi365 – 374Combined sources10
Helixi375 – 377Combined sources3
Beta strandi378 – 384Combined sources7
Beta strandi387 – 393Combined sources7
Beta strandi405 – 412Combined sources8
Turni413 – 416Combined sources4
Beta strandi417 – 424Combined sources8
Beta strandi428 – 430Combined sources3
Beta strandi434 – 438Combined sources5
Turni439 – 442Combined sources4
Beta strandi443 – 448Combined sources6
Beta strandi451 – 460Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini103 – 192SUEL-type lectinPROSITE-ProRule annotationAdd BLAST90
Domaini202 – 461Olfactomedin-likePROSITE-ProRule annotationAdd BLAST260
Domaini883 – 934GPSPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 347Interaction with FLRT3Add BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1470 – 1473Poly-Ala4

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)DescriptionActionsGraphical viewLength
Sequence conflicti381A → S in AAH94668 (PubMed:15489334).Curated1
Sequence conflicti1252K → R in BAE27870 (PubMed:16141072).Curated1
Sequence conflicti1375A → T in BAE26219 (PubMed:16141072).Curated1
Sequence conflicti1495V → M in BAE26219 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0221381 – 239Missing in isoform 4. 1 PublicationAdd BLAST239
Alternative sequenceiVSP_022139195 – 200KVEQKV → I in isoform 6. 1 Publication6
Alternative sequenceiVSP_022140650H → Q in isoform 6. 1 Publication1
Alternative sequenceiVSP_022141651 – 1537Missing in isoform 6. 1 PublicationAdd BLAST887
Alternative sequenceiVSP_0101211132 – 1140Missing in isoform 2 and isoform 5. 2 Publications9
Alternative sequenceiVSP_0101221272 – 1351EGLLN…SEQNR → GAMANHLISNALLRPHGTNN PYNTLLGEPAVCNNPSISMY NTQEPYRETSMGVKLNIAYQ IGASEQCQGYKCHGYSTTEW in isoform 2. 1 PublicationAdd BLAST80
Alternative sequenceiVSP_0221421272E → EPYRETK in isoform 3. 1 Publication1
Alternative sequenceiVSP_0101231352 – 1537Missing in isoform 2. 1 PublicationAdd BLAST186

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_011249465.2. [Q80TS3-3]
XP_011247768.1. XM_011249466.2. [Q80TS3-1]
XP_011247770.1. XM_011249468.2. [Q80TS3-5]
XP_011247773.1. XM_011249471.2. [Q80TS3-2]
XP_017176402.1. XM_017320913.1. [Q80TS3-1]
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_011249465.2. [Q80TS3-3]
XP_011247768.1. XM_011249466.2. [Q80TS3-1]
XP_011247770.1. XM_011249468.2. [Q80TS3-5]
XP_011247773.1. XM_011249471.2. [Q80TS3-2]
XP_017176402.1. XM_017320913.1. [Q80TS3-1]
UniGeneiMm.273631.
Mm.461016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiP02.011.
GPCRDBiSearch...

PTM databases

iPTMnetiQ80TS3.
PhosphoSitePlusiQ80TS3.

Proteomic databases

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

BgeeiENSMUSG00000037605.
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...

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: November 2, 2016
This is version 132 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.