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Protein

Leucine-rich repeat transmembrane protein FLRT3

Gene

Flrt3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (PubMed:19056886, PubMed:25374360). Plays a role in the spatial organization of brain neurons (PubMed:25374360). Plays a role in vascular development in the retina (PubMed:25374360). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25374360). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (PubMed:21673655, PubMed:25374360). Promotes neurite outgrowth (in vitro) (By similarity). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length (By similarity). Plays a role in the regulation of the density of glutamaergic synapses (PubMed:22405201). Plays a role in fibroblast growth factor-mediated signaling cascades (PubMed:16872596). Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning (PubMed:19056886). Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development (PubMed:18448090). Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (PubMed:19056886).By similarity7 Publications

GO - Molecular functioni

  • chemorepellent activity Source: MGI
  • fibroblast growth factor receptor binding Source: UniProtKB
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • axon guidance Source: UniProtKB
  • cell-cell adhesion Source: UniProtKB
  • embryonic morphogenesis Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • head development Source: UniProtKB
  • heart development Source: UniProtKB
  • negative chemotaxis Source: GOC
  • neuron projection development Source: UniProtKB
  • neuron projection extension Source: UniProtKB
  • positive regulation of synapse assembly Source: MGI
  • proepicardium cell migration involved in pericardium morphogenesis Source: UniProtKB
  • response to axon injury Source: UniProtKB
  • synapse assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat transmembrane protein FLRT3Curated
Alternative name(s):
Fibronectin leucine rich transmembrane protein 3Imported
Gene namesi
Name:Flrt3Imported
Synonyms:Kiaa1469Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1918686. Flrt3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 528500ExtracellularCuratedAdd
BLAST
Transmembranei529 – 54921HelicalSequence analysisAdd
BLAST
Topological domaini550 – 649100CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • axonal growth cone Source: UniProtKB
  • axon terminus Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular space Source: MGI
  • focal adhesion Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • synaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Heterozygous mice are viable and fertile, but homozygous mice display nearly complete embryonic lethality. Most embryos die at about 10.5 dpc (PubMed:18448090, PubMed:19056886). A majority present disruption of the basement membrane and ruptures of the anterior visceral endoderm (PubMed:19056886). About one third display a pronounced defect in the fusion of the lateral edges of the body wall, resulting in cardia bifida. Mutant mice display also a defect in proepicardial cell migration. About one third of the mutants display abnormal morphogenesis of the neuroepithelium and headfold fusion defects. Besides, mutant embryos display defects in definitive endoderm migration, resulting in anterior axis truncations. Each of these phenotypes has partial penetrance, and many mutant embryos present a spectrum of defects. About 3% of the mutants develop into viable and fertile adults (PubMed:18448090, PubMed:19056886).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi160 – 1601F → A or N: Abolishes interaction with ADGRL3. 1 Publication
Mutagenesisi165 – 1651H → N: Abolishes interaction with UNC5B. 1 Publication
Mutagenesisi181 – 1811R → N: Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with T-183. 1 Publication
Mutagenesisi183 – 1831D → N: Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with N-181. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 649621Leucine-rich repeat transmembrane protein FLRT3PRO_0000434517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 37Combined sources
Disulfide bondi35 ↔ 44Combined sources
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi309 ↔ 334Combined sources

Post-translational modificationi

N-glycosylated.2 Publications
Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BGT1.
PaxDbiQ8BGT1.

PTM databases

PhosphoSiteiQ6ZPQ1.

Expressioni

Tissue specificityi

Detected in adult brain (PubMed:21350012). Detected in embryonic rostral thalamus neurons (at protein level) (PubMed:24560577). Detected in embryonic rostral thalamus neurons (PubMed:24560577). Detected in neonate eye, in the inner plexiform layer and the outer nuclear layer (PubMed:25374360).2 Publications

Developmental stagei

Detected in embryonic brain at 13 dpc. Levels in brain decrease gradually after 15 dpc, but expression continues after birth (PubMed:21673655). Detected in embryonic myocardium, body wall and pro-epicardial organ at 9.5 dpc. Detected throughout the myocardium at 10.5 dpc, but levels in the epicardial cell layer are strongly decreased. Almost exclusively detected in the neural tube at 14.5 dpc (at protein level) (PubMed:21350012). Detected in the chorion and visceral endoderm between 6 and 8 dpc (PubMed:19056886). Detected in the visceral endoderm at 7 dpc, with a gradient from high expression in the anterior part to low expression at the posterior part (PubMed:19056886). At 8 dpc, detected in definitve endoderm, parts of the neuroectoderm, the headfold and posterior mesoderm (PubMed:19056886). Detected in the developing brain, the proepicardial organ and in somites at 8.5 dpc (PubMed:16872596, PubMed:18448090). At 9.5 and 10.5 dpc, detected in telencephalic vesicles, at the midbrain boundaries with forebrain and hindbrain, the hypothalamic region, in the apical ectodermal ridge, pharyngeal arches, the developing eye, the epithelial structures surrounding the lower region of the developing heart, limb buds and somites (PubMed:16872596, PubMed:18448090). At 10.5 dpc, detected at interlimb somites with loss of expression at limb somites and anterior trunk somites. At 11 dpc, detected in mesoderm in head and branchial arches, migrating germ cells and limbs (PubMed:16872596).4 Publications

Inductioni

Up-regulated by FGF2.1 Publication

Gene expression databases

BgeeiQ6ZPQ1.
GenevisibleiQ8BGT1. MM.

Interactioni

Subunit structurei

Monomer and homodimer (By similarity). Self-associates (via leucine-rich repeats), giving rise to homooligomers (PubMed:25374360). Interacts with FGFR1 (PubMed:16872596). Interacts (via extracellular domain) with ADGRL1/LPHN1 and LPHN2 (via olfactomedin-like domain) (PubMed:22405201). Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like domain) (PubMed:24739570, PubMed:22405201, PubMed:26235031). Interacts (via extracellular domain) with UNC5B (via Ig domain) (PubMed:19492039, PubMed:21673655, PubMed:22405201, PubMed:25374360). May also interact (via extracellular domain) with UNC5A and UNC5C (PubMed:22405201). Interacts (via extracellular domain) with UNC5D (via extracellular domain) (PubMed:19492039). Identified in complexes composed of FLRT3, ADGRL3 and UNC5B, respectively FLRT3, ADGRL3 and UNC5D (By similarity). Interacts (via cytoplasmic domain) with ROBO1 (PubMed:24560577).By similarity7 Publications

GO - Molecular functioni

  • fibroblast growth factor receptor binding Source: UniProtKB
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

DIPiDIP-61803N.
STRINGi10090.ENSMUSP00000053399.

Structurei

Secondary structure

1
649
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Beta strandi41 – 433Combined sources
Beta strandi61 – 644Combined sources
Beta strandi71 – 733Combined sources
Helixi77 – 793Combined sources
Beta strandi87 – 893Combined sources
Beta strandi92 – 943Combined sources
Beta strandi96 – 983Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi113 – 1153Combined sources
Helixi121 – 1255Combined sources
Beta strandi131 – 1344Combined sources
Turni142 – 1443Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi179 – 1813Combined sources
Helixi192 – 1943Combined sources
Turni195 – 1973Combined sources
Beta strandi203 – 2053Combined sources
Turni213 – 2153Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi251 – 2533Combined sources
Turni264 – 2663Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi299 – 3013Combined sources
Turni312 – 3143Combined sources
Helixi315 – 3206Combined sources
Beta strandi325 – 3317Combined sources
Beta strandi333 – 3386Combined sources
Turni339 – 3424Combined sources
Turni345 – 3473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V2EX-ray2.50A/B29-359[»]
4YEBX-ray3.19B29-386[»]
ProteinModelPortaliQ8BGT1.
SMRiQ8BGT1. Positions 30-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 6233LRRNTSequence analysisAdd
BLAST
Repeati58 – 8225LRR 1Sequence analysisAdd
BLAST
Repeati83 – 10523LRR 2Sequence analysisAdd
BLAST
Repeati107 – 12620LRR 3Sequence analysisAdd
BLAST
Repeati127 – 15226LRR 4Sequence analysisAdd
BLAST
Repeati153 – 17624LRR 5Sequence analysisAdd
BLAST
Repeati178 – 19720LRR 6Sequence analysisAdd
BLAST
Repeati198 – 22326LRR 7Sequence analysisAdd
BLAST
Repeati224 – 24623LRR 8Sequence analysisAdd
BLAST
Repeati247 – 26923LRR 9Sequence analysisAdd
BLAST
Repeati270 – 29324LRR 10Sequence analysisAdd
BLAST
Domaini305 – 35652LRRCTSequence analysisAdd
BLAST
Domaini405 – 504100Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6730Interaction with ADGRL3By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 10 LRR (leucine-rich) repeats.Sequence analysis2 Publications
Contains 1 LRRCT domain.Sequence analysis
Contains 1 LRRNT domain.Sequence analysis

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIEA. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000290188.
HOVERGENiHBG051629.
KOiK16362.
OMAiSPYRVCM.
OrthoDBiEOG773XFK.
TreeFamiTF331598.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BGT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISPAWSLFL IGTKIGLFFQ VAPLSVVAKS CPSVCRCDAG FIYCNDRSLT
60 70 80 90 100
SIPVGIPEDA TTLYLQNNQI NNVGIPSDLK NLLKVQRIYL YHNSLDEFPT
110 120 130 140 150
NLPKYVKELH LQENNIRTIT YDSLSKIPYL EELHLDDNSV SAVSIEEGAF
160 170 180 190 200
RDSNYLRLLF LSRNHLSTIP GGLPRTIEEL RLDDNRISTI SSPSLHGLTS
210 220 230 240 250
LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA PVNLPGTSLR
260 270 280 290 300
KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL
310 320 330 340 350
ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLSA
360 370 380 390 400
ELFDCKDSGI VSTIQITTAI PNTAYPAQGQ WPAPVTKQPD IKNPKLIKDQ
410 420 430 440 450
RTTGSPSRKT ILITVKSVTP DTIHISWRLA LPMTALRLSW LKLGHSPAFG
460 470 480 490 500
SITETIVTGE RSEYLVTALE PESPYRVCMV PMETSNLYLF DETPVCIETQ
510 520 530 540 550
TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV SIALLALVCW
560 570 580 590 600
YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS
610 620 630 640
NEPISKEEFV IHTIFPPNGM NLYKNNLSES SSNRSYRDSG IPDSDHSHS
Length:649
Mass (Da):72,879
Last modified:March 1, 2003 - v1
Checksum:i736AC23C5E5BAA41
GO

Sequence cautioni

The sequence BAC98179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY495670 mRNA. Translation: AAR92203.1.
AK129369 mRNA. Translation: BAC98179.1. Different initiation.
AK028252 mRNA. Translation: BAC25843.1.
AK031464 mRNA. Translation: BAC27417.1.
AL928700 Genomic DNA. No translation available.
CH466519 Genomic DNA. Translation: EDL28416.1.
BC052043 mRNA. Translation: AAH52043.1.
CCDSiCCDS16806.1.
RefSeqiNP_001165631.1. NM_001172160.1.
NP_848469.1. NM_178382.4.
UniGeneiMm.426781.

Genome annotation databases

EnsembliENSMUST00000056760; ENSMUSP00000053399; ENSMUSG00000051379.
ENSMUST00000110057; ENSMUSP00000105684; ENSMUSG00000051379.
GeneIDi71436.
KEGGimmu:71436.
UCSCiuc012cfb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY495670 mRNA. Translation: AAR92203.1.
AK129369 mRNA. Translation: BAC98179.1. Different initiation.
AK028252 mRNA. Translation: BAC25843.1.
AK031464 mRNA. Translation: BAC27417.1.
AL928700 Genomic DNA. No translation available.
CH466519 Genomic DNA. Translation: EDL28416.1.
BC052043 mRNA. Translation: AAH52043.1.
CCDSiCCDS16806.1.
RefSeqiNP_001165631.1. NM_001172160.1.
NP_848469.1. NM_178382.4.
UniGeneiMm.426781.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V2EX-ray2.50A/B29-359[»]
4YEBX-ray3.19B29-386[»]
ProteinModelPortaliQ8BGT1.
SMRiQ8BGT1. Positions 30-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61803N.
STRINGi10090.ENSMUSP00000053399.

PTM databases

PhosphoSiteiQ6ZPQ1.

Proteomic databases

MaxQBiQ8BGT1.
PaxDbiQ8BGT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056760; ENSMUSP00000053399; ENSMUSG00000051379.
ENSMUST00000110057; ENSMUSP00000105684; ENSMUSG00000051379.
GeneIDi71436.
KEGGimmu:71436.
UCSCiuc012cfb.1. mouse.

Organism-specific databases

CTDi23767.
MGIiMGI:1918686. Flrt3.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IIEA. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000290188.
HOVERGENiHBG051629.
KOiK16362.
OMAiSPYRVCM.
OrthoDBiEOG773XFK.
TreeFamiTF331598.

Miscellaneous databases

NextBioi333779.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZPQ1.
GenevisibleiQ8BGT1. MM.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulated expression of FLRT genes implies a functional role in the regulation of FGF signalling during mouse development."
    Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.
    Dev. Biol. 297:14-25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FGFR1, SUBCELLULAR LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, INDUCTION BY FGF2.
    Strain: C57BL/6 X CBAImported.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Head and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  7. "Ventral closure, headfold fusion and definitive endoderm migration defects in mouse embryos lacking the fibronectin leucine-rich transmembrane protein FLRT3."
    Maretto S., Mueller P.S., Aricescu A.R., Cho K.W., Bikoff E.K., Robertson E.J.
    Dev. Biol. 318:184-193(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE.
  8. "Genetic ablation of FLRT3 reveals a novel morphogenetic function for the anterior visceral endoderm in suppressing mesoderm differentiation."
    Egea J., Erlacher C., Montanez E., Burtscher I., Yamagishi S., Hess M., Hampel F., Sanchez R., Rodriguez-Manzaneque M.T., Boesl M.R., Faessler R., Lickert H., Klein R.
    Genes Dev. 22:3349-3362(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos."
    Karaulanov E., Boettcher R.T., Stannek P., Wu W., Rau M., Ogata S., Cho K.W.Y., Niehrs C.
    PLoS ONE 4:E5742-E5742(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC5B AND UNC5D.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.
  11. "The fibronectin leucine-rich repeat transmembrane protein Flrt2 is required in the epicardium to promote heart morphogenesis."
    Mueller P.S., Schulz R., Maretto S., Costello I., Srinivas S., Bikoff E., Robertson E.
    Development 138:1297-1308(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  12. Cited for: FUNCTION, INTERACTION WITH UNC5B, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, DEVELOPMENTAL STAGE, GLYCOSYLATION.
  13. "FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development."
    O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S., Yates J.R. III, Ghosh A.
    Neuron 73:903-910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UNC5A; UNC5B; UNC5C; ADGRL1; LPHN2 AND ADGRL3, SUBCELLULAR LOCATION.
  14. "FLRT3 is a Robo1-interacting protein that determines Netrin-1 attraction in developing axons."
    Leyva-Diaz E., del Toro D., Menal M.J., Cambray S., Susin R., Tessier-Lavigne M., Klein R., Egea J., Lopez-Bendito G.
    Curr. Biol. 24:494-508(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROBO1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. "LPHN3, a presynaptic adhesion-GPCR implicated in ADHD, regulates the strength of neocortical layer 2/3 synaptic input to layer 5."
    O'Sullivan M.L., Martini F., von Daake S., Comoletti D., Ghosh A.
    Neural Dev. 9:7-7(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADGRL3.
  16. "FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development."
    Seiradake E., del Toro D., Nagel D., Cop F., Haertl R., Ruff T., Seyit-Bremer G., Harlos K., Border E.C., Acker-Palmer A., Jones E.Y., Klein R.
    Neuron 84:370-385(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-359, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH UNC5B, DISULFIDE BONDS, MUTAGENESIS OF HIS-165; ARG-181 AND ASP-183, TISSUE SPECIFICITY, DOMAIN.
  17. "Structural and mechanistic insights into the latrophilin3-FLRT3 complex that mediates glutamatergic synapse development."
    Ranaivoson F.M., Liu Q., Martini F., Bergami F., von Daake S., Li S., Lee D., Demeler B., Hendrickson W.A., Comoletti D.
    Structure 23:1665-1677(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 29-386 IN COMPLEX WITH ADGRL3, INTERACTION WITH ADGRL3, MUTAGENESIS OF PHE-160, DOMAIN.

Entry informationi

Entry nameiFLRT3_MOUSE
AccessioniPrimary (citable) accession number: Q8BGT1
Secondary accession number(s): Q6ZPQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 135 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.