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O88917

- LPHN1_RAT

UniProt

O88917 - LPHN1_RAT

Protein

Latrophilin-1

Gene

Lphn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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 propably implicated in the regulation of exocytosis.
    Isoform 2: Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421CarbohydrateBy similarity
    Sitei837 – 8382Cleavage; by autocatalysis

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. cell adhesion molecule binding Source: UniProtKB
    3. G-protein coupled receptor activity Source: RGD
    4. latrotoxin receptor activity Source: RGD
    5. protein binding Source: RGD
    6. toxic substance binding Source: RGD

    GO - Biological processi

    1. brain development Source: RGD
    2. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
    3. heterophilic cell-cell adhesion Source: UniProtKB
    4. neuropeptide signaling pathway Source: InterPro
    5. positive regulation of synapse maturation Source: UniProtKB
    6. synaptic vesicle exocytosis Source: RGD

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Ligandi

    Lectin

    Protein family/group databases

    MEROPSiS63.013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Latrophilin-1
    Alternative name(s):
    Calcium-independent alpha-latrotoxin receptor 1
    Short name:
    CIRL-1
    Gene namesi
    Name:Lphn1
    Synonyms:Cirl, Cirl1, Cl1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620768. Lphn1.

    Subcellular locationi

    Cell membrane 2 Publications; Multi-pass membrane protein 2 Publications
    Isoform 2 : Cell membrane. Cell projectionaxon. Cell projectiongrowth cone. Cell junctionsynapse. Cell junctionsynapsepresynaptic cell membrane. Cell junctionsynapsesynaptosome
    Note: Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts.

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. growth cone Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. neuron projection Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. postsynaptic density Source: RGD
    8. presynaptic membrane Source: UniProtKB
    9. synapse Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi802 – 8021S → R: Strongly reduced cleavage. 1 Publication
    Mutagenesisi804 – 8041W → I: Abolishes cleavage. 1 Publication
    Mutagenesisi815 – 8151W → S: Abolishes cleavage. Abolishes cell surface localization. 1 Publication
    Mutagenesisi834 – 8341C → S: Strongly reduced cleavage. 2 Publications
    Mutagenesisi834 – 8341C → W: Abolishes cleavage. Abolishes cell surface localization. 2 Publications
    Mutagenesisi836 – 8361H → S: Abolishes cleavage. No effect on cell surface localization. 1 Publication
    Mutagenesisi837 – 8371L → A: Abolishes cleavage. No effect on cell surface localization. 1 Publication
    Mutagenesisi838 – 8381T → G: Abolishes cleavage. No effect on cell surface localization. 2 Publications
    Mutagenesisi838 – 8381T → P: Abolishes cleavage. Abolishes cell surface localization. 2 Publications
    Mutagenesisi840 – 8401F → A: Strongly reduced cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 15151491Latrophilin-1PRO_0000012908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 71PROSITE-ProRule annotation
    Disulfide bondi50 ↔ 128PROSITE-ProRule annotation
    Disulfide bondi83 ↔ 115PROSITE-ProRule annotation
    Disulfide bondi96 ↔ 102PROSITE-ProRule annotation
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi140 ↔ 322PROSITE-ProRule annotation
    Disulfide bondi480 ↔ 5151 PublicationPROSITE-ProRule annotation
    Disulfide bondi503 ↔ 5321 PublicationPROSITE-ProRule annotation
    Glycosylationi531 – 5311N-linked (GlcNAc...)1 Publication
    Glycosylationi640 – 6401N-linked (GlcNAc...)1 Publication
    Glycosylationi741 – 7411N-linked (GlcNAc...)1 Publication
    Glycosylationi800 – 8001N-linked (GlcNAc...)1 Publication
    Disulfide bondi801 ↔ 8321 PublicationPROSITE-ProRule annotation
    Glycosylationi805 – 8051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi820 ↔ 8341 PublicationPROSITE-ProRule annotation
    Glycosylationi826 – 8261N-linked (GlcNAc...)1 Publication

    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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO88917.
    PRIDEiO88917.

    PTM databases

    PhosphoSiteiO88917.

    Expressioni

    Tissue specificityi

    Expressed in the brain (at protein level). Brain specific distribution but low levels are also detected in most tissues.2 Publications

    Gene expression databases

    GenevestigatoriO88917.

    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. Isoform 2 interacts with TENM2.3 Publications

    Protein-protein interaction databases

    BioGridi249249. 2 interactions.
    IntActiO88917. 1 interaction.
    MINTiMINT-143437.

    Structurei

    Secondary structure

    1
    1515
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi483 – 4853
    Beta strandi488 – 4903
    Beta strandi498 – 5025
    Beta strandi508 – 5158
    Turni517 – 5193
    Helixi536 – 54510
    Helixi550 – 56011
    Helixi567 – 59024
    Helixi605 – 62723
    Helixi630 – 6323
    Helixi633 – 6364
    Helixi641 – 66323
    Beta strandi668 – 6758
    Beta strandi677 – 68711
    Beta strandi695 – 6973
    Beta strandi704 – 7096
    Helixi711 – 7166
    Beta strandi722 – 73211
    Helixi733 – 7364
    Beta strandi759 – 7624
    Beta strandi766 – 7738
    Beta strandi779 – 78911
    Beta strandi796 – 80611
    Turni808 – 8103
    Beta strandi813 – 8164
    Beta strandi820 – 8256
    Beta strandi827 – 83610
    Beta strandi839 – 8479

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DLQX-ray1.85A460-837[»]
    B838-850[»]
    ProteinModelPortaliO88917.
    SMRiO88917. Positions 29-134.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 857833ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini879 – 89214CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini914 – 9196ExtracellularSequence Analysis
    Topological domaini941 – 96424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini986 – 100116ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1023 – 104927CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1071 – 10744ExtracellularSequence Analysis
    Topological domaini1096 – 1515420CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei858 – 87821Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei893 – 91321Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei920 – 94021Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei965 – 98521Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei1002 – 102221Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei1050 – 107021Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei1075 – 109521Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 12990SUEL-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini139 – 398260Olfactomedin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini798 – 84952GPSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 1204Carbohydrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi413 – 4164Poly-Thr
    Compositional biasi1451 – 146111Poly-ProAdd
    BLAST

    Domaini

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

    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

    eggNOGiNOG253931.
    HOGENOMiHOG000049065.
    HOVERGENiHBG052337.
    InParanoidiO88917.
    KOiK04592.
    PhylomeDBiO88917.

    Family and domain databases

    InterProiIPR022624. 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]
    PfamiPF00002. 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]
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O88917-1) [UniParc]FASTAAdd to Basket

    Also known as: CL1BB

    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

    MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC     50
    PGSDVIMVEN ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT 100
    QCVVVAGSDA FPDPCPGTYK YLEVQYDCVP YKVEQKVFVC PGTLQKVLEP 150
    TSTHESEHQS GAWCKDPLQA GDRIYVMPWI PYRTDTLTEY ASWEDYVAAR 200
    HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT RIKSGETVIN 250
    TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL 300
    RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT 350
    NANREEPVSL AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD 400
    PSAGPATSPP LSTTTTARPT PLTSTASPAA TTPLRRAPLT THPVGAINQL 450
    GPDLPPATAP APSTRRPPAP NLHVSPELFC EPREVRRVQW PATQQGMLVE 500
    RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV AQKIKSGENA 550
    ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG 600
    KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM 650
    LLDVLEEGAF LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE 700
    YASESSIQLS ANTIKQNSRN GVVKVVFILY NNLGLFLSTE NATVKLAGEA 750
    GTGGPGGASL VVNSQVIAAS INKESSRVFL MDPVIFTVAH LEAKNHFNAN 800
    CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF AVLMAHREIY 850
    QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI 900
    NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL 950
    LVEVFESEYS RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN 1000
    YFIWSFIGPV SFVIVVNLVF LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL 1050
    GAIALLFLLG LTWAFGLLFI NKESVVMAYL FTTFNAFQGV FIFVFHCALQ 1100
    KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY YTGTQVPGQG 1150
    RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV 1200
    RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES 1250
    VGFNPSSPPV FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG 1300
    DFPPGDGGPE PPRGRNLADA AAFEKMIISE LVHNNLRGAS GGAKGPPPEP 1350
    PVPPVPGVSE DEAGGPGGAD RAEIELLYKA LEEPLLLPRA QSVLYQSDLD 1400
    ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD SSPEGPNEAL 1450
    PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG 1500
    PGPDGDGQMQ LVTSL 1515
    Length:1,515
    Mass (Da):166,615
    Last modified:November 1, 1998 - v1
    Checksum:i0BF3B900C54F17B7
    GO
    Isoform 2 (identifier: O88917-2) [UniParc]FASTAAdd to Basket

    Also known as: CL1AA

    The sequence of this isoform differs from the canonical sequence as follows:
         132-137: KVEQKV → I
         1146-1189: Missing.

    Show »
    Length:1,466
    Mass (Da):161,545
    Checksum:i5926609E031565F9
    GO
    Isoform 3 (identifier: O88917-3) [UniParc]FASTAAdd to Basket

    Also known as: CL1AB

    The sequence of this isoform differs from the canonical sequence as follows:
         132-137: KVEQKV → I

    Show »
    Length:1,510
    Mass (Da):166,016
    Checksum:i6A22505113DFCD5B
    GO
    Isoform 4 (identifier: O88917-4) [UniParc]FASTAAdd to Basket

    Also known as: CL1BA

    The sequence of this isoform differs from the canonical sequence as follows:
         1146-1189: Missing.

    Show »
    Length:1,471
    Mass (Da):162,144
    Checksum:i9F560F544B4191C6
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei132 – 1376KVEQKV → I in isoform 2 and isoform 3. 2 PublicationsVSP_050398
    Alternative sequencei1146 – 118944Missing in isoform 2 and isoform 4. 3 PublicationsVSP_050399Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081144 mRNA. Translation: AAC62650.1.
    AF081145 mRNA. Translation: AAC62651.1.
    AF081146 mRNA. Translation: AAC62652.1.
    AF081147 mRNA. Translation: AAC62653.1.
    U72487 mRNA. Translation: AAC53268.1.
    U78105 mRNA. Translation: AAC98700.1.
    PIRiT17138.
    T17145.
    T17149.
    T17156.
    RefSeqiNP_075251.1. NM_022962.1. [O88917-4]
    UniGeneiRn.10776.

    Genome annotation databases

    GeneIDi65096.
    KEGGirno:65096.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081144 mRNA. Translation: AAC62650.1 .
    AF081145 mRNA. Translation: AAC62651.1 .
    AF081146 mRNA. Translation: AAC62652.1 .
    AF081147 mRNA. Translation: AAC62653.1 .
    U72487 mRNA. Translation: AAC53268.1 .
    U78105 mRNA. Translation: AAC98700.1 .
    PIRi T17138.
    T17145.
    T17149.
    T17156.
    RefSeqi NP_075251.1. NM_022962.1. [O88917-4 ]
    UniGenei Rn.10776.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DLQ X-ray 1.85 A 460-837 [» ]
    B 838-850 [» ]
    ProteinModelPortali O88917.
    SMRi O88917. Positions 29-134.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249249. 2 interactions.
    IntActi O88917. 1 interaction.
    MINTi MINT-143437.

    Chemistry

    GuidetoPHARMACOLOGYi 206.

    Protein family/group databases

    MEROPSi S63.013.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei O88917.

    Proteomic databases

    PaxDbi O88917.
    PRIDEi O88917.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 65096.
    KEGGi rno:65096.

    Organism-specific databases

    CTDi 22859.
    RGDi 620768. Lphn1.

    Phylogenomic databases

    eggNOGi NOG253931.
    HOGENOMi HOG000049065.
    HOVERGENi HBG052337.
    InParanoidi O88917.
    KOi K04592.
    PhylomeDBi O88917.

    Miscellaneous databases

    NextBioi 613919.
    PROi O88917.

    Gene expression databases

    Genevestigatori O88917.

    Family and domain databases

    InterProi IPR022624. 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 ]
    Pfami PF00002. 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 ]
    PRINTSi PR00249. GPCRSECRETIN.
    PR01444. LATROPHILIN.
    SMARTi SM00303. GPS. 1 hit.
    SM00008. HormR. 1 hit.
    SM00284. OLF. 1 hit.
    [Graphical view ]
    PROSITEi 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.
    PS51132. OLF. 1 hit.
    PS50228. SUEL_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis."
      Sugita S., Ichtchenko K., Khvotchev M., Suedhof T.C.
      J. Biol. Chem. 273:32715-32724(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY.
    2. "Alpha-latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor."
      Krasnoperov V.G., Bittner M.A., Beavis R., Kuang Y., Salnikow K.V., Chepurny O.G., Little A.R., Plotnikov A.N., Wu D., Holz R.W., Petrenko A.G.
      Neuron 18:925-937(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 838-850, PROTEOLYTIC PROCESSING, INTERACTION WITH SYNTAXIN.
    3. "Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors."
      Lelianova V.G., Davletov B.A., Sterling A., Rahman M.A., Grishin E.V., Totty N.F., Ushkaryov Y.A.
      J. Biol. Chem. 272:21504-21508(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
    4. "Isolation and biochemical characterization of a Ca2+-independent alpha-latrotoxin-binding protein."
      Davletov B.A., Shamotienko O.G., Lelianova V.G., Grishin E.V., Ushkaryov Y.A.
      J. Biol. Chem. 271:23239-23245(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION (ISOFORM 2).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    5. "Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants."
      Krasnoperov V., Bittner M.A., Holz R.W., Chepurny O., Petrenko A.G.
      J. Biol. Chem. 274:3590-3596(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family."
      Tobaben S., Suedhof T.C., Stahl B.
      J. Biol. Chem. 275:36204-36210(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PROTEINS OF THE SHANK FAMILY.
    7. "Post-translational proteolytic processing of the calcium-independent receptor of alpha-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled receptor. Role of the G protein-coupled receptor proteolysis site (GPS) motif."
      Krasnoperov V., Lu Y., Buryanovsky L., Neubert T.A., Ichtchenko K., Petrenko A.G.
      J. Biol. Chem. 277:46518-46526(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-815; CYS-834 AND THR-838.
    8. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities."
      Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G., Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S., Tonevitsky A.G., Dell A., Volynski K.E., Ushkaryov Y.A.
      Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TENM2 LIGAND-BINDING, INTERACTION WITH TENM2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis."
      Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C., Brunger A.T.
      EMBO J. 31:1364-1378(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 460-850, GLYCOSYLATION AT ASN-531; ASN-640; ASN-741; ASN-800 AND ASN-826, DISULFIDE BONDS, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-802; TRP-804; CYS-834; HIS-836; LEU-837; THR-838 AND PHE-840, AUTOCATALYTIC PROCESSING.

    Entry informationi

    Entry nameiLPHN1_RAT
    AccessioniPrimary (citable) accession number: O88917
    Secondary accession number(s): O09026, O35818, O88916
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3