Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O88917

- LPHN1_RAT

UniProt

O88917 - LPHN1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Latrophilin-1

Gene

Lphn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 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: UniProtKB-KW
  2. cell adhesion molecule binding Source: UniProtKB
  3. G-protein coupled receptor activity Source: RGD
  4. latrotoxin receptor activity Source: RGD
  5. 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 via plasma membrane cell adhesion molecules Source: UniProtKB
  4. neuropeptide signaling pathway Source: InterPro
  5. positive regulation of synapse maturation Source: UniProtKB
  6. synaptic vesicle exocytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Lectin

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 857833ExtracellularSequence AnalysisAdd
BLAST
Transmembranei858 – 87821Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini879 – 89214CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei893 – 91321Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini914 – 9196ExtracellularSequence Analysis
Transmembranei920 – 94021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini941 – 96424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei965 – 98521Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini986 – 100116ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1002 – 102221Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini1023 – 104927CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1050 – 107021Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini1071 – 10744ExtracellularSequence Analysis
Transmembranei1075 – 109521Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini1096 – 1515420CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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 – 4853Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi508 – 5158Combined sources
Turni517 – 5193Combined sources
Helixi536 – 54510Combined sources
Helixi550 – 56011Combined sources
Helixi567 – 59024Combined sources
Helixi605 – 62723Combined sources
Helixi630 – 6323Combined sources
Helixi633 – 6364Combined sources
Helixi641 – 66323Combined sources
Beta strandi668 – 6758Combined sources
Beta strandi677 – 68711Combined sources
Beta strandi695 – 6973Combined sources
Beta strandi704 – 7096Combined sources
Helixi711 – 7166Combined sources
Beta strandi722 – 73211Combined sources
Helixi733 – 7364Combined sources
Beta strandi759 – 7624Combined sources
Beta strandi766 – 7738Combined sources
Beta strandi779 – 78911Combined sources
Beta strandi796 – 80611Combined sources
Turni808 – 8103Combined sources
Beta strandi813 – 8164Combined sources
Beta strandi820 – 8256Combined sources
Beta strandi827 – 83610Combined sources
Beta strandi839 – 8479Combined sources

3D structure databases

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

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

        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 YKVEQKVFVC PGTLQKVLEP
160 170 180 190 200
TSTHESEHQS GAWCKDPLQA GDRIYVMPWI PYRTDTLTEY ASWEDYVAAR
210 220 230 240 250
HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT RIKSGETVIN
260 270 280 290 300
TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL
310 320 330 340 350
RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT
360 370 380 390 400
NANREEPVSL AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD
410 420 430 440 450
PSAGPATSPP LSTTTTARPT PLTSTASPAA TTPLRRAPLT THPVGAINQL
460 470 480 490 500
GPDLPPATAP APSTRRPPAP NLHVSPELFC EPREVRRVQW PATQQGMLVE
510 520 530 540 550
RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV AQKIKSGENA
560 570 580 590 600
ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG
610 620 630 640 650
KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM
660 670 680 690 700
LLDVLEEGAF LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE
710 720 730 740 750
YASESSIQLS ANTIKQNSRN GVVKVVFILY NNLGLFLSTE NATVKLAGEA
760 770 780 790 800
GTGGPGGASL VVNSQVIAAS INKESSRVFL MDPVIFTVAH LEAKNHFNAN
810 820 830 840 850
CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF AVLMAHREIY
860 870 880 890 900
QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI
910 920 930 940 950
NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL
960 970 980 990 1000
LVEVFESEYS RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN
1010 1020 1030 1040 1050
YFIWSFIGPV SFVIVVNLVF LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL
1060 1070 1080 1090 1100
GAIALLFLLG LTWAFGLLFI NKESVVMAYL FTTFNAFQGV FIFVFHCALQ
1110 1120 1130 1140 1150
KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY YTGTQVPGQG
1160 1170 1180 1190 1200
RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV
1210 1220 1230 1240 1250
RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES
1260 1270 1280 1290 1300
VGFNPSSPPV FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG
1310 1320 1330 1340 1350
DFPPGDGGPE PPRGRNLADA AAFEKMIISE LVHNNLRGAS GGAKGPPPEP
1360 1370 1380 1390 1400
PVPPVPGVSE DEAGGPGGAD RAEIELLYKA LEEPLLLPRA QSVLYQSDLD
1410 1420 1430 1440 1450
ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD SSPEGPNEAL
1460 1470 1480 1490 1500
PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG
1510
PGPDGDGQMQ LVTSL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 122 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