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Protein

Adhesion G protein-coupled receptor L1

Gene

Adgrl1

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

Functioni

Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42Carbohydrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Lectin

Protein family/group databases

MEROPSiP02.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor L1Imported
Alternative name(s):
Calcium-independent alpha-latrotoxin receptor 1By similarity
Short name:
CIRL-1By similarity
Latrophilin-1Imported
Lectomedin-2Imported
Gene namesi
Name:Adgrl1Imported
Synonyms:Kiaa0821Imported, Lec2Imported, Lphn1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1929461. Adgrl1.

Subcellular locationi

  • Cell membrane; Multi-pass membrane protein
  • Cell projectionaxon By similarity
  • Cell projectiongrowth cone By similarity
  • Cell junctionsynapse By similarity
  • Cell junctionsynapsepresynaptic cell membrane By similarity
  • Cell junctionsynapsesynaptosome By similarity

  • Note: Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 852ExtracellularSequence analysisAdd BLAST824
Transmembranei853 – 873Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini874 – 887CytoplasmicSequence analysisAdd BLAST14
Transmembranei888 – 908Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini909 – 914ExtracellularSequence analysis6
Transmembranei915 – 935Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini936 – 958CytoplasmicSequence analysisAdd BLAST23
Transmembranei959 – 979Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini980 – 996ExtracellularSequence analysisAdd BLAST17
Transmembranei997 – 1017Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1018 – 1044CytoplasmicSequence analysisAdd BLAST27
Transmembranei1045 – 1065Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1066 – 1069ExtracellularSequence analysis4
Transmembranei1070 – 1090Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1091 – 1466CytoplasmicSequence analysisAdd BLAST376

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42E → A or R: Abrogates L-rhamnose binding. 1 Publication1
Mutagenesisi42E → D or Q: 100-fold decreased affinity for L-rhamnose. 1 Publication1
Mutagenesisi120K → A or R: Abrogates L-rhamnose binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000007034229 – 1466Adhesion G protein-coupled receptor L1Add BLAST1438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 71PROSITE-ProRule annotation1 Publication
Disulfide bondi50 ↔ 128PROSITE-ProRule annotation1 Publication
Disulfide bondi83 ↔ 115PROSITE-ProRule annotation1 Publication
Disulfide bondi96 ↔ 102PROSITE-ProRule annotation1 Publication
Glycosylationi98N-linked (GlcNAc...)1 Publication1
Disulfide bondi135 ↔ 317PROSITE-ProRule annotation
Disulfide bondi475 ↔ 510PROSITE-ProRule annotation
Disulfide bondi498 ↔ 527PROSITE-ProRule annotation
Glycosylationi526N-linked (GlcNAc...)Sequence analysis1
Glycosylationi635N-linked (GlcNAc...)Sequence analysis1
Glycosylationi736N-linked (GlcNAc...)Sequence analysis1
Glycosylationi795N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi796 ↔ 827PROSITE-ProRule annotation
Glycosylationi800N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi815 ↔ 829PROSITE-ProRule annotation
Glycosylationi821N-linked (GlcNAc...)Sequence analysis1
Modified residuei1188Omega-N-methylarginineCombined sources1
Modified residuei1214PhosphoserineCombined sources1
Modified residuei1319PhosphoserineCombined sources1
Modified residuei1448PhosphoserineCombined sources1
Modified residuei1465PhosphoserineCombined sources1

Post-translational modificationi

Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei832 – 833Cleavage; by autolysisBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ80TR1.
PeptideAtlasiQ80TR1.
PRIDEiQ80TR1.

PTM databases

iPTMnetiQ80TR1.
PhosphoSitePlusiQ80TR1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000013033.
CleanExiMM_LPHN1.
ExpressionAtlasiQ80TR1. baseline and differential.
GenevisibleiQ80TR1. MM.

Interactioni

Subunit structurei

Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain (By similarity). Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (PubMed:22405201).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ80TR1. 1 interactor.
STRINGi10090.ENSMUSP00000118452.

Structurei

Secondary structure

11466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 41Combined sources6
Beta strandi44 – 49Combined sources6
Beta strandi54 – 66Combined sources13
Beta strandi68 – 71Combined sources4
Helixi75 – 78Combined sources4
Helixi87 – 96Combined sources10
Beta strandi99 – 107Combined sources9
Helixi108 – 110Combined sources3
Beta strandi121 – 131Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JX9NMR-A29-131[»]
2JXANMR-A29-131[»]
ProteinModelPortaliQ80TR1.
SMRiQ80TR1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80TR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 129SUEL-type lectinPROSITE-ProRule annotationAdd BLAST90
Domaini134 – 393Olfactomedin-likePROSITE-ProRule annotationAdd BLAST260
Domaini793 – 844GPSPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni117 – 120Carbohydrate binding4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi408 – 411Poly-Thr4
Compositional biasi1402 – 1412Poly-ProAdd BLAST11

Domaini

The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin.By similarity

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.
InParanoidiQ80TR1.
KOiK04592.
PhylomeDBiQ80TR1.
TreeFamiTF351999.

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.
IPR031234. Latrophilin-1.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF62. PTHR12011:SF62. 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. 1 hit.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TR1-1) [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
MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC
60 70 80 90 100
PGSDVIMVEN ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT
110 120 130 140 150
QCVVVAGSDA FPDPCPGTYK YLEVQYDCVP YIFVCPGTLQ KVLEPTSTHE
160 170 180 190 200
SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD TLTEYASWED YVAARHTTTY
210 220 230 240 250
RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG ETVINTANYH
260 270 280 290 300
DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT
310 320 330 340 350
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE
360 370 380 390 400
EPVSLAFPNP YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP
410 420 430 440 450
ATSPPLSTTT TARPTPLTST ASPAATTPLR RAPLTTHPVG AINQLGPDLP
460 470 480 490 500
PATAPAPSTR RPPAPNLHVS PELFCEPREV RRVQWPATQQ GMLVERPCPK
510 520 530 540 550
GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK SGENAANIAS
560 570 580 590 600
ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
610 620 630 640 650
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL
660 670 680 690 700
EEGAFLLADN VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN
710 720 730 740 750
SIQLSANTIK QNSRNGVVKV VFILYNNLGL FLSTENATVK LAGEAGTGGP
760 770 780 790 800
GGASLVVNSQ VIAASINKES SRVFLMDPVI FTVAHLEAKN HFNANCSFWN
810 820 830 840 850
YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA HREIYQGRIN
860 870 880 890 900
ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA
910 920 930 940 950
ELLFLVGIDK TQYEVACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF
960 970 980 990 1000
ESEYSRTKYY YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS
1010 1020 1030 1040 1050
FIGPVSFVIV VNLVFLMVTL HKMIRSSSVL KPDSSRLDNI KSWALGAIAL
1060 1070 1080 1090 1100
LFLLGLTWAF GLLFINKESV VMAYLFTTFN AFQGVFIFVF HCALQKKVHK
1110 1120 1130 1140 1150
EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ SRIRRMWNDT
1160 1170 1180 1190 1200
VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE
1210 1220 1230 1240 1250
SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS
1260 1270 1280 1290 1300
GDFPPGDGGP EPPRGRNLAD AAAFEKMIIS ELVHNNLRGA SGGAKGPPPE
1310 1320 1330 1340 1350
PPVPPVPGVS EDEAGGPGSA DRAEIELLYK ALEEPLLLPR AQSVLYQSDL
1360 1370 1380 1390 1400
DESESCTAED GATSRPLSSP PGRDSLYASG ANLRDSPSYP DSSPEGPNEA
1410 1420 1430 1440 1450
LPPPPPAPPG PPEIYYTSRP PALVARNPLQ GYYQVRRPSH EGYLAAPSLE
1460
GPGPDGDGQM QLVTSL
Length:1,466
Mass (Da):161,686
Last modified:January 9, 2007 - v2
Checksum:i937199B072336C9E
GO
Isoform 2 (identifier: Q80TR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: Missing.

Note: No experimental confirmation available.
Show »
Length:1,295
Mass (Da):142,775
Checksum:i23B2CAE4C15B72E4
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0221371 – 171Missing in isoform 2. 1 PublicationAdd BLAST171

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147519 mRNA. Translation: BAE27967.1.
AK122380 mRNA. Translation: BAC65662.1.
AC156028 Genomic DNA. No translation available.
AY255594 mRNA. Translation: AAO85106.1.
BC055793 mRNA. Translation: AAH55793.1.
CCDSiCCDS52613.1. [Q80TR1-1]
RefSeqiNP_851382.2. NM_181039.2. [Q80TR1-1]
XP_006531189.1. XM_006531126.2. [Q80TR1-2]
XP_006531190.1. XM_006531127.2. [Q80TR1-2]
XP_006531191.1. XM_006531128.2. [Q80TR1-2]
UniGeneiMm.260733.

Genome annotation databases

EnsembliENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
GeneIDi330814.
KEGGimmu:330814.
UCSCiuc009mlh.2. mouse. [Q80TR1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147519 mRNA. Translation: BAE27967.1.
AK122380 mRNA. Translation: BAC65662.1.
AC156028 Genomic DNA. No translation available.
AY255594 mRNA. Translation: AAO85106.1.
BC055793 mRNA. Translation: AAH55793.1.
CCDSiCCDS52613.1. [Q80TR1-1]
RefSeqiNP_851382.2. NM_181039.2. [Q80TR1-1]
XP_006531189.1. XM_006531126.2. [Q80TR1-2]
XP_006531190.1. XM_006531127.2. [Q80TR1-2]
XP_006531191.1. XM_006531128.2. [Q80TR1-2]
UniGeneiMm.260733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JX9NMR-A29-131[»]
2JXANMR-A29-131[»]
ProteinModelPortaliQ80TR1.
SMRiQ80TR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80TR1. 1 interactor.
STRINGi10090.ENSMUSP00000118452.

Protein family/group databases

MEROPSiP02.010.
GPCRDBiSearch...

PTM databases

iPTMnetiQ80TR1.
PhosphoSitePlusiQ80TR1.

Proteomic databases

PaxDbiQ80TR1.
PeptideAtlasiQ80TR1.
PRIDEiQ80TR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
GeneIDi330814.
KEGGimmu:330814.
UCSCiuc009mlh.2. mouse. [Q80TR1-1]

Organism-specific databases

CTDi22859.
MGIiMGI:1929461. Adgrl1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3545. Eukaryota.
KOG4193. Eukaryota.
KOG4729. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiQ80TR1.
KOiK04592.
PhylomeDBiQ80TR1.
TreeFamiTF351999.

Miscellaneous databases

ChiTaRSiLphn1. mouse.
EvolutionaryTraceiQ80TR1.
PROiQ80TR1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000013033.
CleanExiMM_LPHN1.
ExpressionAtlasiQ80TR1. baseline and differential.
GenevisibleiQ80TR1. 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.
IPR031234. Latrophilin-1.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF62. PTHR12011:SF62. 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. 1 hit.
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 nameiAGRL1_MOUSE
AccessioniPrimary (citable) accession number: Q80TR1
Secondary accession number(s): Q3UH90, Q7TNE5, Q80T49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 138 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

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.