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Protein

Latrophilin-1

Gene

Lphn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor propably implicated in the regulation of exocytosis (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421Carbohydrate
Sitei832 – 8332Cleavage; by autolysisBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. cell adhesion molecule binding Source: UniProtKB
  3. G-protein coupled receptor activity Source: UniProtKB-KW
  4. latrotoxin receptor activity Source: UniProtKB

GO - Biological processi

  1. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  2. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  3. positive regulation of synapse assembly Source: MGI
  4. positive regulation of synapse maturation Source: UniProtKB
Complete GO annotation...

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
Lectomedin-2
Gene namesi
Name:Lphn1
Synonyms:Kiaa0821, Lec2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1929461. Lphn1.

Subcellular locationi

  1. Cell membrane; Multi-pass membrane protein
  2. Cell projectionaxon By similarity
  3. Cell projectiongrowth cone By similarity
  4. Cell junctionsynapse By similarity
  5. Cell junctionsynapsepresynaptic cell membrane By similarity
  6. Cell junctionsynapsesynaptosome By similarity

  7. Note: Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 852824ExtracellularSequence AnalysisAdd
BLAST
Transmembranei853 – 87321Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini874 – 88714CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei888 – 90821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini909 – 9146ExtracellularSequence Analysis
Transmembranei915 – 93521Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini936 – 95823CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei959 – 97921Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini980 – 99617ExtracellularSequence AnalysisAdd
BLAST
Transmembranei997 – 101721Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini1018 – 104427CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1045 – 106521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini1066 – 10694ExtracellularSequence Analysis
Transmembranei1070 – 109021Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini1091 – 1466376CytoplasmicSequence 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. presynaptic membrane Source: UniProtKB
  8. 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
Mutagenesisi42 – 421E → A or R: Abrogates L-rhamnose binding. 1 Publication
Mutagenesisi42 – 421E → D or Q: 100-fold decreased affinity for L-rhamnose. 1 Publication
Mutagenesisi120 – 1201K → A or R: Abrogates L-rhamnose binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 14661438Latrophilin-1PRO_0000070342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 71PROSITE-ProRule annotation1 Publication
Disulfide bondi50 ↔ 128PROSITE-ProRule annotation1 Publication
Disulfide bondi83 ↔ 115PROSITE-ProRule annotation1 Publication
Disulfide bondi96 ↔ 102PROSITE-ProRule annotation1 Publication
Glycosylationi98 – 981N-linked (GlcNAc...)1 Publication
Disulfide bondi135 ↔ 317PROSITE-ProRule annotation
Disulfide bondi475 ↔ 510PROSITE-ProRule annotation
Disulfide bondi498 ↔ 527PROSITE-ProRule annotation
Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi736 – 7361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi796 ↔ 827PROSITE-ProRule annotation
Glycosylationi800 – 8001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi815 ↔ 829PROSITE-ProRule annotation
Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence Analysis

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ80TR1.
PaxDbiQ80TR1.
PRIDEiQ80TR1.

PTM databases

PhosphoSiteiQ80TR1.

Expressioni

Gene expression databases

BgeeiQ80TR1.
CleanExiMM_LPHN1.
ExpressionAtlasiQ80TR1. baseline and differential.
GenevestigatoriQ80TR1.

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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ80TR1. 1 interaction.
STRINGi10090.ENSMUSP00000115295.

Structurei

Secondary structure

1
1466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 416Combined sources
Beta strandi44 – 496Combined sources
Beta strandi54 – 6613Combined sources
Beta strandi68 – 714Combined sources
Helixi75 – 784Combined sources
Helixi87 – 9610Combined sources
Beta strandi99 – 1079Combined sources
Helixi108 – 1103Combined sources
Beta strandi121 – 13111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JX9NMR-A29-131[»]
2JXANMR-A29-131[»]
ProteinModelPortaliQ80TR1.
SMRiQ80TR1. Positions 29-131, 469-832, 855-1094.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80TR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 12990SUEL-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 393260Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST
Domaini793 – 84452GPSPROSITE-ProRule annotationAdd
BLAST

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi408 – 4114Poly-Thr
Compositional biasi1402 – 141211Poly-ProAdd
BLAST

Domaini

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

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.
GeneTreeiENSGT00760000118787.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiQ80TR1.
KOiK04592.
OrthoDBiEOG76DTRK.
PhylomeDBiQ80TR1.
TreeFamiTF351999.

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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TR1-1) [UniParc]FASTAAdd to basket

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 YIFVCPGTLQ KVLEPTSTHE
160 170 180 190 200
SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD TLTEYASWED YVAARHTTTY
210 220 230 240 250
RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG ETVINTANYH
260 270 280 290 300
DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT
310 320 330 340 350
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE
360 370 380 390 400
EPVSLAFPNP YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP
410 420 430 440 450
ATSPPLSTTT TARPTPLTST ASPAATTPLR RAPLTTHPVG AINQLGPDLP
460 470 480 490 500
PATAPAPSTR RPPAPNLHVS PELFCEPREV RRVQWPATQQ GMLVERPCPK
510 520 530 540 550
GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK SGENAANIAS
560 570 580 590 600
ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
610 620 630 640 650
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL
660 670 680 690 700
EEGAFLLADN VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN
710 720 730 740 750
SIQLSANTIK QNSRNGVVKV VFILYNNLGL FLSTENATVK LAGEAGTGGP
760 770 780 790 800
GGASLVVNSQ VIAASINKES SRVFLMDPVI FTVAHLEAKN HFNANCSFWN
810 820 830 840 850
YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA HREIYQGRIN
860 870 880 890 900
ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA
910 920 930 940 950
ELLFLVGIDK TQYEVACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF
960 970 980 990 1000
ESEYSRTKYY YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS
1010 1020 1030 1040 1050
FIGPVSFVIV VNLVFLMVTL HKMIRSSSVL KPDSSRLDNI KSWALGAIAL
1060 1070 1080 1090 1100
LFLLGLTWAF GLLFINKESV VMAYLFTTFN AFQGVFIFVF HCALQKKVHK
1110 1120 1130 1140 1150
EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ SRIRRMWNDT
1160 1170 1180 1190 1200
VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE
1210 1220 1230 1240 1250
SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS
1260 1270 1280 1290 1300
GDFPPGDGGP EPPRGRNLAD AAAFEKMIIS ELVHNNLRGA SGGAKGPPPE
1310 1320 1330 1340 1350
PPVPPVPGVS EDEAGGPGSA DRAEIELLYK ALEEPLLLPR AQSVLYQSDL
1360 1370 1380 1390 1400
DESESCTAED GATSRPLSSP PGRDSLYASG ANLRDSPSYP DSSPEGPNEA
1410 1420 1430 1440 1450
LPPPPPAPPG PPEIYYTSRP PALVARNPLQ GYYQVRRPSH EGYLAAPSLE
1460
GPGPDGDGQM QLVTSL
Length:1,466
Mass (Da):161,686
Last modified:January 9, 2007 - v2
Checksum:i937199B072336C9E
GO
Isoform 2 (identifier: Q80TR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: Missing.

Note: No experimental confirmation available.

Show »
Length:1,295
Mass (Da):142,775
Checksum:i23B2CAE4C15B72E4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 171171Missing in isoform 2. 1 PublicationVSP_022137Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52613.1. [Q80TR1-1]
RefSeqiNP_851382.2. NM_181039.2. [Q80TR1-1]
XP_006531189.1. XM_006531126.2. [Q80TR1-2]
XP_006531190.1. XM_006531127.2. [Q80TR1-2]
XP_006531191.1. XM_006531128.2. [Q80TR1-2]
UniGeneiMm.260733.

Genome annotation databases

EnsembliENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
GeneIDi330814.
KEGGimmu:330814.
UCSCiuc009mlh.2. mouse. [Q80TR1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52613.1. [Q80TR1-1]
RefSeqiNP_851382.2. NM_181039.2. [Q80TR1-1]
XP_006531189.1. XM_006531126.2. [Q80TR1-2]
XP_006531190.1. XM_006531127.2. [Q80TR1-2]
XP_006531191.1. XM_006531128.2. [Q80TR1-2]
UniGeneiMm.260733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JX9NMR-A29-131[»]
2JXANMR-A29-131[»]
ProteinModelPortaliQ80TR1.
SMRiQ80TR1. Positions 29-131, 469-832, 855-1094.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80TR1. 1 interaction.
STRINGi10090.ENSMUSP00000115295.

Protein family/group databases

MEROPSiS63.013.
GPCRDBiSearch...

PTM databases

PhosphoSiteiQ80TR1.

Proteomic databases

MaxQBiQ80TR1.
PaxDbiQ80TR1.
PRIDEiQ80TR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
GeneIDi330814.
KEGGimmu:330814.
UCSCiuc009mlh.2. mouse. [Q80TR1-1]

Organism-specific databases

CTDi22859.
MGIiMGI:1929461. Lphn1.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG253931.
GeneTreeiENSGT00760000118787.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiQ80TR1.
KOiK04592.
OrthoDBiEOG76DTRK.
PhylomeDBiQ80TR1.
TreeFamiTF351999.

Miscellaneous databases

ChiTaRSiLphn1. mouse.
EvolutionaryTraceiQ80TR1.
NextBioi399562.
PROiQ80TR1.
SOURCEiSearch...

Gene expression databases

BgeeiQ80TR1.
CleanExiMM_LPHN1.
ExpressionAtlasiQ80TR1. baseline and differential.
GenevestigatoriQ80TR1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-978.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-1466.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain."
    Vakonakis I., Langenhan T., Promel S., Russ A., Campbell I.D.
    Structure 16:944-953(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 29-132 IN COMPLEX WITH D-GALACTOSE AND L-RHAMNOSE, GLYCOSYLATION AT ASN-98, MUTAGENESIS OF GLU-42 AND LYS-120, DISULFIDE BONDS.

Entry informationi

Entry nameiLPHN1_MOUSE
AccessioniPrimary (citable) accession number: Q80TR1
Secondary accession number(s): Q3UH90, Q7TNE5, Q80T49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 9, 2007
Last modified: April 29, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.