O88917 (LPHN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Latrophilin-1

Alternative name(s):
Calcium-independent alpha-latrotoxin receptor 1
Short name=CIRL-1

Gene names

Name:	Lphn1
Synonyms:	Cirl, Cirl1, Cl1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 propably implicated in the regulation of exocytosis. Isoform 2: Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization.
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. Isoform 2 interacts with TENM2. Ref.2 Ref.6 Ref.8
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.8 Ref.9. Isoform 2: Cell membrane. Cell projection › axon. Cell projection › growth cone. Cell junction › synapse. Cell junction › synapse › presynaptic cell membrane. Cell junction › synapse › synaptosome. Note: Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. Ref.8 Ref.9
Tissue specificity	Expressed in the brain (at protein level). Brain specific distribution but low levels are also detected in most tissues. Ref.1 Ref.8
Domain	The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin.
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. Ref.2 Ref.9
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 component	Cell junction Cell membrane Cell projection Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Ligand	Lectin
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from expression pattern PubMed 10964907. Source: RGD calcium-mediated signaling using intracellular calcium source Inferred from direct assay Ref.8. Source: UniProtKB heterophilic cell-cell adhesion Inferred from direct assay Ref.8. Source: UniProtKB neuropeptide signaling pathway Inferred from electronic annotation. Source: InterPro positive regulation of synapse maturation Inferred from direct assay Ref.8. Source: UniProtKB synaptic vesicle exocytosis Traceable author statement Ref.3. Source: RGD
Cellular_component	axon Inferred from direct assay Ref.8. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW growth cone Inferred from direct assay Ref.8. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB postsynaptic density Inferred from direct assay PubMed 10964907. Source: RGD presynaptic membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	G-protein coupled receptor activity Inferred from direct assay Ref.3. Source: RGD carbohydrate binding Inferred from electronic annotation. Source: InterPro cell adhesion molecule binding Inferred from direct assay Ref.8. Source: UniProtKB latrotoxin receptor activity Inferred from direct assay Ref.3. Source: RGD toxin binding Inferred from physical interaction Ref.3. Source: RGD
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88917-1)

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.

Isoform 2 (identifier: O88917-2)

Also known as: CL1AA;

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

Isoform 3 (identifier: O88917-3)

Also known as: CL1AB;

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

Isoform 4 (identifier: O88917-4)

Also known as: CL1BA;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.2

Chain

25 – 1515

1491

Latrophilin-1

PRO_0000012908

Regions

Topological domain

25 – 857

833

Extracellular Potential

Transmembrane

858 – 878

21

Helical; Name=1; Potential

Topological domain

879 – 892

14

Cytoplasmic Potential

Transmembrane

893 – 913

21

Helical; Name=2; Potential

Topological domain

914 – 919

6

Extracellular Potential

Transmembrane

920 – 940

21

Helical; Name=3; Potential

Topological domain

941 – 964

24

Cytoplasmic Potential

Transmembrane

965 – 985

21

Helical; Name=4; Potential

Topological domain

986 – 1001

16

Extracellular Potential

Transmembrane

1002 – 1022

21

Helical; Name=5; Potential

Topological domain

1023 – 1049

27

Cytoplasmic Potential

Transmembrane

1050 – 1070

21

Helical; Name=6; Potential

Topological domain

1071 – 1074

4

Extracellular Potential

Transmembrane

1075 – 1095

21

Helical; Name=7; Potential

Topological domain

1096 – 1515

420

Cytoplasmic Potential

Domain

40 – 129

90

SUEL-type lectin

Domain

139 – 398

260

Olfactomedin-like

Domain

798 – 849

52

GPS

Region

117 – 120

4

Carbohydrate binding By similarity

Compositional bias

413 – 416

4

Poly-Thr

Compositional bias

1451 – 1461

11

Poly-Pro

Sites

Binding site

42

1

Carbohydrate By similarity

Site

837 – 838

2

Cleavage; by autocatalysis

Amino acid modifications

Modified residue

1418

1

Phosphoserine By similarity

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

531

1

N-linked (GlcNAc...) Ref.9

Glycosylation

640

1

N-linked (GlcNAc...) Ref.9

Glycosylation

741

1

N-linked (GlcNAc...) Ref.9

Glycosylation

800

1

N-linked (GlcNAc...) Ref.9

Glycosylation

805

1

N-linked (GlcNAc...) Potential

Glycosylation

826

1

N-linked (GlcNAc...) Ref.9

Disulfide bond

41 ↔ 71

By similarity

Disulfide bond

50 ↔ 128

By similarity

Disulfide bond

83 ↔ 115

By similarity

Disulfide bond

96 ↔ 102

By similarity

Disulfide bond

140 ↔ 322

By similarity

Disulfide bond

480 ↔ 515

Ref.9

Disulfide bond

503 ↔ 532

Ref.9

Disulfide bond

801 ↔ 832

Ref.9

Disulfide bond

820 ↔ 834

Ref.9

Natural variations

Alternative sequence

132 – 137

6

KVEQKV → I in isoform 2 and isoform 3.

VSP_050398

Alternative sequence

1146 – 1189

44

Missing in isoform 2 and isoform 4.

VSP_050399

Experimental info

Mutagenesis

802

1

S → R: Strongly reduced cleavage. Ref.9

Mutagenesis

804

1

W → I: Abolishes cleavage. Ref.9

Mutagenesis

815

1

W → S: Abolishes cleavage. Abolishes cell surface localization. Ref.7

Mutagenesis

834

1

C → S: Strongly reduced cleavage. Ref.7 Ref.9

Mutagenesis

834

1

C → W: Abolishes cleavage. Abolishes cell surface localization. Ref.7 Ref.9

Mutagenesis

836

1

H → S: Abolishes cleavage. No effect on cell surface localization. Ref.9

Mutagenesis

837

1

L → A: Abolishes cleavage. No effect on cell surface localization. Ref.9

Mutagenesis

838

1

T → G: Abolishes cleavage. No effect on cell surface localization. Ref.7 Ref.9

Mutagenesis

838

1

T → P: Abolishes cleavage. Abolishes cell surface localization. Ref.7 Ref.9

Mutagenesis

840

1

F → A: Strongly reduced cleavage. Ref.9

Secondary structure

1

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1515

Helix Strand Turn

Details...

Beta strand

483 – 485

3

Beta strand

488 – 490

3

Beta strand

498 – 502

5

Beta strand

508 – 515

8

Turn

517 – 519

3

Helix

536 – 545

10

Helix

550 – 560

11

Helix

567 – 590

24

Helix

605 – 627

23

Helix

630 – 632

3

Helix

633 – 636

4

Helix

641 – 663

23

Beta strand

668 – 675

8

Beta strand

677 – 687

11

Beta strand

695 – 697

3

Beta strand

704 – 709

6

Helix

711 – 716

6

Beta strand

722 – 732

11

Helix

733 – 736

4

Beta strand

759 – 762

4

Beta strand

766 – 773

8

Beta strand

779 – 789

11

Beta strand

796 – 806

11

Turn

808 – 810

3

Beta strand

813 – 816

4

Beta strand

820 – 825

6

Beta strand

827 – 836

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CL1BB) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 0BF3B900C54F17B7	FASTA	1,515	166,615
	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 YKVEQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI 190 200 210 220 230 240 PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT 250 260 270 280 290 300 RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL 310 320 330 340 350 360 RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL 370 380 390 400 410 420 AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT 430 440 450 460 470 480 PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP APSTRRPPAP NLHVSPELFC 490 500 510 520 530 540 EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV 550 560 570 580 590 600 AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG 610 620 630 640 650 660 KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM LLDVLEEGAF 670 680 690 700 710 720 LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE YASESSIQLS ANTIKQNSRN 730 740 750 760 770 780 GVVKVVFILY NNLGLFLSTE NATVKLAGEA GTGGPGGASL VVNSQVIAAS INKESSRVFL 790 800 810 820 830 840 MDPVIFTVAH LEAKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF 850 860 870 880 890 900 AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI 910 920 930 940 950 960 NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS 970 980 990 1000 1010 1020 RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF 1030 1040 1050 1060 1070 1080 LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL 1090 1100 1110 1120 1130 1140 FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY 1150 1160 1170 1180 1190 1200 YTGTQVPGQG RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV 1210 1220 1230 1240 1250 1260 RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES VGFNPSSPPV 1270 1280 1290 1300 1310 1320 FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG DFPPGDGGPE PPRGRNLADA 1330 1340 1350 1360 1370 1380 AAFEKMIISE LVHNNLRGAS GGAKGPPPEP PVPPVPGVSE DEAGGPGGAD RAEIELLYKA 1390 1400 1410 1420 1430 1440 LEEPLLLPRA QSVLYQSDLD ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD 1450 1460 1470 1480 1490 1500 SSPEGPNEAL PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG 1510 PGPDGDGQMQ LVTSL
	Isoform 2 (CL1AA) [UniParc]. Checksum: 5926609E031565F9	FASTA	1,466	161,545
	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 LSTEGQVQEL VFPQEYASES 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 CCIRSPPGGA 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 EDEAGGPGGA 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
	Isoform 3 (CL1AB) [UniParc]. Checksum: 6A22505113DFCD5B	FASTA	1,510	166,016
	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 LSTEGQVQEL VFPQEYASES 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 CCIRSPPGGA HGSLKTSAMR SNTRYYTGTQ 1150 1160 1170 1180 1190 1200 VPGQGRHIHQ VSLGPRGRSA LPESQKDPGG QSGPGDPLTF GLCPSRIRRM WNDTVRKQTE 1210 1220 1230 1240 1250 1260 SSFMAGDINS TPTLNRGTMG NHLLTNPVLQ PRGGTSPYNT LIAESVGFNP SSPPVFNSPG 1270 1280 1290 1300 1310 1320 SYREPKHPLG GREACGMDTL PLNGNFNNSY SLRSGDFPPG DGGPEPPRGR NLADAAAFEK 1330 1340 1350 1360 1370 1380 MIISELVHNN LRGASGGAKG PPPEPPVPPV PGVSEDEAGG PGGADRAEIE LLYKALEEPL 1390 1400 1410 1420 1430 1440 LLPRAQSVLY QSDLDESESC TAEDGATSRP LSSPPGRDSL YASGANLRDS PSYPDSSPEG 1450 1460 1470 1480 1490 1500 PNEALPPPPP APPGPPEIYY TSRPPALVAR NPLQGYYQVR RPSHEGYLAA PSLEGPGPDG 1510 DGQMQLVTSL
	Isoform 4 (CL1BA) [UniParc]. Checksum: 9F560F544B4191C6	FASTA	1,471	162,144
	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 YKVEQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI 190 200 210 220 230 240 PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT 250 260 270 280 290 300 RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL 310 320 330 340 350 360 RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL 370 380 390 400 410 420 AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT 430 440 450 460 470 480 PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP APSTRRPPAP NLHVSPELFC 490 500 510 520 530 540 EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV 550 560 570 580 590 600 AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG 610 620 630 640 650 660 KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM LLDVLEEGAF 670 680 690 700 710 720 LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE YASESSIQLS ANTIKQNSRN 730 740 750 760 770 780 GVVKVVFILY NNLGLFLSTE NATVKLAGEA GTGGPGGASL VVNSQVIAAS INKESSRVFL 790 800 810 820 830 840 MDPVIFTVAH LEAKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF 850 860 870 880 890 900 AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI 910 920 930 940 950 960 NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS 970 980 990 1000 1010 1020 RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF 1030 1040 1050 1060 1070 1080 LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL 1090 1100 1110 1120 1130 1140 FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY 1150 1160 1170 1180 1190 1200 YTGTQSRIRR MWNDTVRKQT ESSFMAGDIN STPTLNRGTM GNHLLTNPVL QPRGGTSPYN 1210 1220 1230 1240 1250 1260 TLIAESVGFN PSSPPVFNSP GSYREPKHPL GGREACGMDT LPLNGNFNNS YSLRSGDFPP 1270 1280 1290 1300 1310 1320 GDGGPEPPRG RNLADAAAFE KMIISELVHN NLRGASGGAK GPPPEPPVPP VPGVSEDEAG 1330 1340 1350 1360 1370 1380 GPGGADRAEI ELLYKALEEP LLLPRAQSVL YQSDLDESES CTAEDGATSR PLSSPPGRDS 1390 1400 1410 1420 1430 1440 LYASGANLRD SPSYPDSSPE GPNEALPPPP PAPPGPPEIY YTSRPPALVA RNPLQGYYQV 1450 1460 1470 RRPSHEGYLA APSLEGPGPD GDGQMQLVTS L

References

[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]	"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.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00208999.
IPI00325093.
IPI00411236.
IPI00411237.

PIR

T17138.
T17145.
T17149.
T17156.

RefSeq

NP_075251.1. NM_022962.1.

UniGene

Rn.10776.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DLQ	X-ray	1.85	A	460-837	[»]
			B	838-850	[»]

ProteinModelPortal

O88917.

SMR

O88917. Positions 29-134.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-143437.

Protein family/group databases

MEROPS

S63.013.

GPCRDB

Search...

PTM databases

PhosphoSite

O88917.

Proteomic databases

PaxDb

O88917.

PRIDE

O88917.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

65096.

KEGG

rno:65096.

Organism-specific databases

CTD

22859.

RGD

620768. Lphn1.

Phylogenomic databases

eggNOG

NOG253931.

HOGENOM

HOG000049065.

HOVERGEN

HBG052337.

InParanoid

O88917.

KO

K04592.

OrthoDB

EOG4RJG0S.

Gene expression databases

ArrayExpress

O88917.

Genevestigator

O88917.

GermOnline

ENSRNOG00000029134. Rattus norvegicus.

Family and domain databases

InterPro

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_dom.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like.
[Graphical view]

Pfam

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]

PRINTS

PR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.

SMART

SM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]

PROSITE

PS00649. G_PROTEIN_RECEP_F2_1. False negative.
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]

ProtoNet

Search...

Other

NextBio

613919.

Entry information

Entry name

LPHN1_RAT

Accession

Primary (citable) accession number: O88917
Secondary accession number(s): O09026, O35818, O88916

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program