Q80TR1 (LPHN1_MOUSE) 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
Lectomedin-2

Gene names

Name:	Lphn1
Synonyms:	Kiaa0821, Lec2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	1466 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 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 projection › axon By similarity. Cell projection › growth cone By similarity. Cell junction › synapse By similarity. Cell junction › synapse › presynaptic cell membrane By similarity. Cell junction › synapse › synaptosome 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 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 Reference proteome
Gene Ontology (GO)
Biological_process	calcium-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_component	axon 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB presynaptic membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	G-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 1466

1438

Latrophilin-1

PRO_0000070342

Regions

Topological domain

29 – 852

824

Extracellular Potential

Transmembrane

853 – 873

21

Helical; Name=1; Potential

Topological domain

874 – 887

14

Cytoplasmic Potential

Transmembrane

888 – 908

21

Helical; Name=2; Potential

Topological domain

909 – 914

6

Extracellular Potential

Transmembrane

915 – 935

21

Helical; Name=3; Potential

Topological domain

936 – 958

23

Cytoplasmic Potential

Transmembrane

959 – 979

21

Helical; Name=4; Potential

Topological domain

980 – 996

17

Extracellular Potential

Transmembrane

997 – 1017

21

Helical; Name=5; Potential

Topological domain

1018 – 1044

27

Cytoplasmic Potential

Transmembrane

1045 – 1065

21

Helical; Name=6; Potential

Topological domain

1066 – 1069

4

Extracellular Potential

Transmembrane

1070 – 1090

21

Helical; Name=7; Potential

Topological domain

1091 – 1466

376

Cytoplasmic Potential

Domain

40 – 129

90

SUEL-type lectin

Domain

134 – 393

260

Olfactomedin-like

Domain

793 – 844

52

GPS

Region

117 – 120

4

Carbohydrate binding

Compositional bias

408 – 411

4

Poly-Thr

Compositional bias

1402 – 1412

11

Poly-Pro

Sites

Binding site

42

1

Carbohydrate

Site

832 – 833

2

Cleavage By similarity

Site

832 – 833

2

Cleavage; by autocatalysis By similarity

Amino acid modifications

Modified residue

1369

1

Phosphoserine Ref.6

Glycosylation

98

1

N-linked (GlcNAc...) Ref.7

Glycosylation

526

1

N-linked (GlcNAc...) Potential

Glycosylation

635

1

N-linked (GlcNAc...) Potential

Glycosylation

736

1

N-linked (GlcNAc...) Potential

Glycosylation

795

1

N-linked (GlcNAc...) Potential

Glycosylation

800

1

N-linked (GlcNAc...) Potential

Glycosylation

821

1

N-linked (GlcNAc...) Potential

Disulfide bond

41 ↔ 71

Ref.7

Disulfide bond

50 ↔ 128

Ref.7

Disulfide bond

83 ↔ 115

Ref.7

Disulfide bond

96 ↔ 102

Ref.7

Disulfide bond

135 ↔ 317

By similarity

Disulfide bond

475 ↔ 510

By similarity

Disulfide bond

498 ↔ 527

By similarity

Disulfide bond

796 ↔ 827

By similarity

Disulfide bond

815 ↔ 829

By similarity

Natural variations

Alternative sequence

1 – 171

171

Missing in isoform 2.

VSP_022137

Experimental info

Mutagenesis

42

1

E → A or R: Abrogates L-rhamnose binding. Ref.7

Mutagenesis

42

1

E → D or Q: 100-fold decreased affinity for L-rhamnose. Ref.7

Mutagenesis

120

1

K → A or R: Abrogates L-rhamnose binding. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1466

Helix Strand Turn

Details...

Beta strand

36 – 41

6

Beta strand

44 – 49

6

Beta strand

54 – 66

13

Beta strand

68 – 71

4

Helix

75 – 78

4

Helix

87 – 96

10

Beta strand

99 – 107

9

Helix

108 – 110

3

Beta strand

121 – 131

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 937199B072336C9E	FASTA	1,466	161,686
	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
	Isoform 2 [UniParc]. Checksum: 23B2CAE4C15B72E4	FASTA	1,295	142,775
	10 20 30 40 50 60 MPWIPYRTDT LTEYASWEDY VAARHTTTYR LPNRVDGTGF VVYDGAVFYN KERTRNIVKY 70 80 90 100 110 120 DLRTRIKSGE TVINTANYHD TSPYRWGGKT DIDLAVDENG LWVIYATEGN NGRLVVSQLN 130 140 150 160 170 180 PYTLRFEGTW ETGYDKRSAS NAFMVCGVLY VLRSVYVDDD SEAAGNRVDY AFNTNANREE 190 200 210 220 230 240 PVSLAFPNPY QFVSSVDYNP RDNQLYVWNN YFVVRYSLEF GPPDPSAGPA TSPPLSTTTT 250 260 270 280 290 300 ARPTPLTSTA SPAATTPLRR APLTTHPVGA INQLGPDLPP ATAPAPSTRR PPAPNLHVSP 310 320 330 340 350 360 ELFCEPREVR RVQWPATQQG MLVERPCPKG TRGIASFQCL PALGLWNPRG PDLSNCTSPW 370 380 390 400 410 420 VNQVAQKIKS GENAANIASE LARHTRGSIY AGDVSSSVKL MEQLLDILDA QLQALRPIER 430 440 450 460 470 480 ESAGKNYNKM HKRERTCKDY IKAVVETVDN LLRPEALESW KDMNATEQVH TATMLLDVLE 490 500 510 520 530 540 EGAFLLADNV REPARFLAAK QNVVLEVTVL NTEGQVQELV FPQEYPSENS IQLSANTIKQ 550 560 570 580 590 600 NSRNGVVKVV FILYNNLGLF LSTENATVKL AGEAGTGGPG GASLVVNSQV IAASINKESS 610 620 630 640 650 660 RVFLMDPVIF TVAHLEAKNH FNANCSFWNY SERSMLGYWS TQGCRLVESN KTHTTCACSH 670 680 690 700 710 720 LTNFAVLMAH REIYQGRINE LLLSVITWVG IVISLVCLAI CISTFCFLRG LQTDRNTIHK 730 740 750 760 770 780 NLCINLFLAE LLFLVGIDKT QYEVACPIFA GLLHYFFLAA FSWLCLEGVH LYLLLVEVFE 790 800 810 820 830 840 SEYSRTKYYY LGGYCFPALV VGIAAAIDYR SYGTEKACWL RVDNYFIWSF IGPVSFVIVV 850 860 870 880 890 900 NLVFLMVTLH KMIRSSSVLK PDSSRLDNIK SWALGAIALL FLLGLTWAFG LLFINKESVV 910 920 930 940 950 960 MAYLFTTFNA FQGVFIFVFH CALQKKVHKE YSKCLRHSYC CIRSPPGGTH GSLKTSAMRS 970 980 990 1000 1010 1020 NTRYYTGTQS RIRRMWNDTV RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT 1030 1040 1050 1060 1070 1080 SPYNTLIAES VGFNPSSPPV FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG 1090 1100 1110 1120 1130 1140 DFPPGDGGPE PPRGRNLADA AAFEKMIISE LVHNNLRGAS GGAKGPPPEP PVPPVPGVSE 1150 1160 1170 1180 1190 1200 DEAGGPGSAD RAEIELLYKA LEEPLLLPRA QSVLYQSDLD ESESCTAEDG ATSRPLSSPP 1210 1220 1230 1240 1250 1260 GRDSLYASGA NLRDSPSYPD SSPEGPNEAL PPPPPAPPGP PEIYYTSRPP ALVARNPLQG 1270 1280 1290 YYQVRRPSHE GYLAAPSLEG PGPDGDGQMQ LVTSL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1369, MASS SPECTROMETRY. Tissue: Brain cortex.
[7]	"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.

IPI

IPI00623958.
IPI00816879.

RefSeq

NP_851382.2. NM_181039.2.

UniGene

Mm.260733.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JX9	NMR	-	A	29-131	[»]
2JXA	NMR	-	A	29-131	[»]

ProteinModelPortal

Q80TR1.

SMR

Q80TR1. Positions 29-131, 469-832.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q80TR1. 1 interaction.

STRING

10090.ENSMUSP00000115295.

Protein family/group databases

MEROPS

S63.013.

GPCRDB

Search...

PTM databases

PhosphoSite

Q80TR1.

Proteomic databases

PaxDb

Q80TR1.

PRIDE

Q80TR1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033.
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033.

GeneID

330814.

KEGG

mmu:330814.

UCSC

uc009mlg.2. mouse.
uc009mli.2. mouse.

Organism-specific databases

CTD

22859.

MGI

MGI:1929461. Lphn1.

Rouge

Search...

Phylogenomic databases

eggNOG

NOG253931.

GeneTree

ENSGT00680000099540.

HOGENOM

HOG000049065.

HOVERGEN

HBG052337.

InParanoid

Q80TR1.

KO

K04592.

Gene expression databases

ArrayExpress

Q80TR1.

Bgee

Q80TR1.

CleanEx

MM_LPHN1.

Genevestigator

Q80TR1.

GermOnline

ENSMUSG00000013033. Mus musculus.

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

ChiTaRS

LPHN1. mouse.

EvolutionaryTrace

Q80TR1.

NextBio

399562.

SOURCE

Search...

Entry information

Entry name

LPHN1_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program