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Q80TR1 (LPHN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Latrophilin-1
Alternative name(s):
Calcium-independent alpha-latrotoxin receptor 1
Short name=CIRL-1
Lectomedin-2
Gene names
Name:Lphn1
Synonyms:Kiaa0821, Lec2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 propably implicated in the regulation of exocytosis By similarity.

Subunit structure

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.

Subcellular location

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.

Domain

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

Post-translational modification

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.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 1 GPS domain.

Contains 1 olfactomedin-like domain.

Contains 1 SUEL-type lectin domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling using intracellular calcium source

Inferred from sequence or structural similarity. Source: UniProtKB

heterophilic cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

positive regulation of synapse maturation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

presynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

cell adhesion molecule binding

Inferred from sequence or structural similarity. Source: UniProtKB

latrotoxin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80TR1-1)

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.
Isoform 2 (identifier: Q80TR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 14661438Latrophilin-1
PRO_0000070342

Regions

Topological domain29 – 852824Extracellular Potential
Transmembrane853 – 87321Helical; Name=1; Potential
Topological domain874 – 88714Cytoplasmic Potential
Transmembrane888 – 90821Helical; Name=2; Potential
Topological domain909 – 9146Extracellular Potential
Transmembrane915 – 93521Helical; Name=3; Potential
Topological domain936 – 95823Cytoplasmic Potential
Transmembrane959 – 97921Helical; Name=4; Potential
Topological domain980 – 99617Extracellular Potential
Transmembrane997 – 101721Helical; Name=5; Potential
Topological domain1018 – 104427Cytoplasmic Potential
Transmembrane1045 – 106521Helical; Name=6; Potential
Topological domain1066 – 10694Extracellular Potential
Transmembrane1070 – 109021Helical; Name=7; Potential
Topological domain1091 – 1466376Cytoplasmic Potential
Domain40 – 12990SUEL-type lectin
Domain134 – 393260Olfactomedin-like
Domain793 – 84452GPS
Region117 – 1204Carbohydrate binding
Compositional bias408 – 4114Poly-Thr
Compositional bias1402 – 141211Poly-Pro

Sites

Binding site421Carbohydrate
Site832 – 8332Cleavage By similarity
Site832 – 8332Cleavage; by autocatalysis By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Ref.6
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation6351N-linked (GlcNAc...) Potential
Glycosylation7361N-linked (GlcNAc...) Potential
Glycosylation7951N-linked (GlcNAc...) Potential
Glycosylation8001N-linked (GlcNAc...) Potential
Glycosylation8211N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 71 Ref.6
Disulfide bond50 ↔ 128 Ref.6
Disulfide bond83 ↔ 115 Ref.6
Disulfide bond96 ↔ 102 Ref.6
Disulfide bond135 ↔ 317 By similarity
Disulfide bond475 ↔ 510 By similarity
Disulfide bond498 ↔ 527 By similarity
Disulfide bond796 ↔ 827 By similarity
Disulfide bond815 ↔ 829 By similarity

Natural variations

Alternative sequence1 – 171171Missing in isoform 2.
VSP_022137

Experimental info

Mutagenesis421E → A or R: Abrogates L-rhamnose binding. Ref.6
Mutagenesis421E → D or Q: 100-fold decreased affinity for L-rhamnose. Ref.6
Mutagenesis1201K → A or R: Abrogates L-rhamnose binding. Ref.6

Secondary structure

.................. 1466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 937199B072336C9E

FASTA1,466161,686
        10         20         30         40         50         60 
MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN 

        70         80         90        100        110        120 
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK 

       130        140        150        160        170        180 
YLEVQYDCVP YIFVCPGTLQ KVLEPTSTHE SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD 

       190        200        210        220        230        240 
TLTEYASWED YVAARHTTTY RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG 

       250        260        270        280        290        300 
ETVINTANYH DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT 

       310        320        330        340        350        360 
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE EPVSLAFPNP 

       370        380        390        400        410        420 
YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP ATSPPLSTTT TARPTPLTST 

       430        440        450        460        470        480 
ASPAATTPLR RAPLTTHPVG AINQLGPDLP PATAPAPSTR RPPAPNLHVS PELFCEPREV 

       490        500        510        520        530        540 
RRVQWPATQQ GMLVERPCPK GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK 

       550        560        570        580        590        600 
SGENAANIAS ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK 

       610        620        630        640        650        660 
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL EEGAFLLADN 

       670        680        690        700        710        720 
VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN SIQLSANTIK QNSRNGVVKV 

       730        740        750        760        770        780 
VFILYNNLGL FLSTENATVK LAGEAGTGGP GGASLVVNSQ VIAASINKES SRVFLMDPVI 

       790        800        810        820        830        840 
FTVAHLEAKN HFNANCSFWN YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA 

       850        860        870        880        890        900 
HREIYQGRIN ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA 

       910        920        930        940        950        960 
ELLFLVGIDK TQYEVACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF ESEYSRTKYY 

       970        980        990       1000       1010       1020 
YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS FIGPVSFVIV VNLVFLMVTL 

      1030       1040       1050       1060       1070       1080 
HKMIRSSSVL KPDSSRLDNI KSWALGAIAL LFLLGLTWAF GLLFINKESV VMAYLFTTFN 

      1090       1100       1110       1120       1130       1140 
AFQGVFIFVF HCALQKKVHK EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ 

      1150       1160       1170       1180       1190       1200 
SRIRRMWNDT VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE 

      1210       1220       1230       1240       1250       1260 
SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS GDFPPGDGGP 

      1270       1280       1290       1300       1310       1320 
EPPRGRNLAD AAAFEKMIIS ELVHNNLRGA SGGAKGPPPE PPVPPVPGVS EDEAGGPGSA 

      1330       1340       1350       1360       1370       1380 
DRAEIELLYK ALEEPLLLPR AQSVLYQSDL DESESCTAED GATSRPLSSP PGRDSLYASG 

      1390       1400       1410       1420       1430       1440 
ANLRDSPSYP DSSPEGPNEA LPPPPPAPPG PPEIYYTSRP PALVARNPLQ GYYQVRRPSH 

      1450       1460 
EGYLAAPSLE GPGPDGDGQM QLVTSL 

« Hide

Isoform 2 [UniParc].

Checksum: 23B2CAE4C15B72E4
Show »

FASTA1,295142,775

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 2).
Strain: C57BL/6.
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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 61-1466 (ISOFORM 1).
Tissue: Brain.
[4]"The G protein-coupled receptor repertoires of human and mouse."
Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E., Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C., Bergmann J.E., Gaitanaris G.A.
Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-978.
[5]"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] OF 1145-1466.
Strain: C57BL/6.
Tissue: Brain.
[6]"Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain."
Vakonakis I., Langenhan T., Promel S., Russ A., Campbell I.D.
Structure 16:944-953(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 29-132 IN COMPLEX WITH D-GALACTOSE AND L-RHAMNOSE, GLYCOSYLATION AT ASN-98, MUTAGENESIS OF GLU-42 AND LYS-120, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS52613.1. [Q80TR1-1]
RefSeqNP_851382.2. NM_181039.2. [Q80TR1-1]
XP_006531189.1. XM_006531126.1. [Q80TR1-2]
XP_006531190.1. XM_006531127.1. [Q80TR1-2]
XP_006531191.1. XM_006531128.1. [Q80TR1-2]
UniGeneMm.260733.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JX9NMR-A29-131[»]
2JXANMR-A29-131[»]
ProteinModelPortalQ80TR1.
SMRQ80TR1. Positions 29-131, 469-832, 855-1094.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80TR1. 1 interaction.
STRING10090.ENSMUSP00000115295.

Protein family/group databases

MEROPSS63.013.
GPCRDBSearch...

PTM databases

PhosphoSiteQ80TR1.

Proteomic databases

MaxQBQ80TR1.
PaxDbQ80TR1.
PRIDEQ80TR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
GeneID330814.
KEGGmmu:330814.
UCSCuc009mlh.2. mouse. [Q80TR1-1]

Organism-specific databases

CTD22859.
MGIMGI:1929461. Lphn1.
RougeSearch...

Phylogenomic databases

eggNOGNOG253931.
GeneTreeENSGT00710000106375.
HOGENOMHOG000049065.
HOVERGENHBG052337.
InParanoidQ80TR1.
KOK04592.
OrthoDBEOG76DTRK.
PhylomeDBQ80TR1.
TreeFamTF351999.

Gene expression databases

ArrayExpressQ80TR1.
BgeeQ80TR1.
CleanExMM_LPHN1.
GenevestigatorQ80TR1.

Family and domain databases

InterProIPR022624. DUF3497.
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.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF12003. DUF3497. 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]
PRINTSPR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.
SMARTSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]
PROSITEPS00650. 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]
ProtoNetSearch...

Other

ChiTaRSLPHN1. mouse.
EvolutionaryTraceQ80TR1.
NextBio399562.
PROQ80TR1.
SOURCESearch...

Entry information

Entry nameLPHN1_MOUSE
AccessionPrimary (citable) accession number: Q80TR1
Secondary accession number(s): Q3UH90, Q7TNE5, Q80T49
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries