ID FLRT3_MOUSE Reviewed; 649 AA.
AC Q8BGT1; Q6ZPQ1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT3 {ECO:0000305};
DE AltName: Full=Fibronectin leucine rich transmembrane protein 3 {ECO:0000312|EMBL:AAH52043.1};
DE Flags: Precursor;
GN Name=Flrt3 {ECO:0000312|MGI:MGI:1918686};
GN Synonyms=Kiaa1469 {ECO:0000312|EMBL:BAC98179.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAR92203.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FGFR1, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, AND INDUCTION BY FGF2.
RC STRAIN=C57BL/6 X CBA {ECO:0000312|EMBL:AAR92203.1};
RX PubMed=16872596; DOI=10.1016/j.ydbio.2006.04.004;
RA Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.;
RT "Regulated expression of FLRT genes implies a functional role in the
RT regulation of FGF signalling during mouse development.";
RL Dev. Biol. 297:14-25(2006).
RN [2] {ECO:0000312|EMBL:BAC98179.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAC98179.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18448090; DOI=10.1016/j.ydbio.2008.03.021;
RA Maretto S., Mueller P.S., Aricescu A.R., Cho K.W., Bikoff E.K.,
RA Robertson E.J.;
RT "Ventral closure, headfold fusion and definitive endoderm migration defects
RT in mouse embryos lacking the fibronectin leucine-rich transmembrane protein
RT FLRT3.";
RL Dev. Biol. 318:184-193(2008).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19056886; DOI=10.1101/gad.486708;
RA Egea J., Erlacher C., Montanez E., Burtscher I., Yamagishi S., Hess M.,
RA Hampel F., Sanchez R., Rodriguez-Manzaneque M.T., Boesl M.R., Faessler R.,
RA Lickert H., Klein R.;
RT "Genetic ablation of FLRT3 reveals a novel morphogenetic function for the
RT anterior visceral endoderm in suppressing mesoderm differentiation.";
RL Genes Dev. 22:3349-3362(2008).
RN [9]
RP INTERACTION WITH UNC5B AND UNC5D.
RX PubMed=19492039; DOI=10.1371/journal.pone.0005742;
RA Karaulanov E., Boettcher R.T., Stannek P., Wu W., Rau M., Ogata S.,
RA Cho K.W.Y., Niehrs C.;
RT "Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus
RT embryos.";
RL PLoS ONE 4:E5742-E5742(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=21350012; DOI=10.1242/dev.059386;
RA Mueller P.S., Schulz R., Maretto S., Costello I., Srinivas S., Bikoff E.,
RA Robertson E.;
RT "The fibronectin leucine-rich repeat transmembrane protein Flrt2 is
RT required in the epicardium to promote heart morphogenesis.";
RL Development 138:1297-1308(2011).
RN [12]
RP FUNCTION, INTERACTION WITH UNC5B, SUBCELLULAR LOCATION, PROTEOLYTIC
RP CLEAVAGE, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=21673655; DOI=10.1038/emboj.2011.189;
RA Yamagishi S., Hampel F., Hata K., Del Toro D., Schwark M., Kvachnina E.,
RA Bastmeyer M., Yamashita T., Tarabykin V., Klein R., Egea J.;
RT "FLRT2 and FLRT3 act as repulsive guidance cues for Unc5-positive
RT neurons.";
RL EMBO J. 30:2920-2933(2011).
RN [13]
RP FUNCTION, INTERACTION WITH UNC5A; UNC5B; UNC5C; ADGRL1; LPHN2 AND ADGRL3,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
RN [14]
RP FUNCTION, INTERACTION WITH ROBO1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24560577; DOI=10.1016/j.cub.2014.01.042;
RA Leyva-Diaz E., del Toro D., Menal M.J., Cambray S., Susin R.,
RA Tessier-Lavigne M., Klein R., Egea J., Lopez-Bendito G.;
RT "FLRT3 is a Robo1-interacting protein that determines Netrin-1 attraction
RT in developing axons.";
RL Curr. Biol. 24:494-508(2014).
RN [15]
RP INTERACTION WITH ADGRL3.
RX PubMed=24739570; DOI=10.1186/1749-8104-9-7;
RA O'Sullivan M.L., Martini F., von Daake S., Comoletti D., Ghosh A.;
RT "LPHN3, a presynaptic adhesion-GPCR implicated in ADHD, regulates the
RT strength of neocortical layer 2/3 synaptic input to layer 5.";
RL Neural Dev. 9:7-7(2014).
RN [16] {ECO:0007744|PDB:4V2E}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-359, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, INTERACTION WITH UNC5B, DISULFIDE BONDS, MUTAGENESIS OF
RP HIS-165; ARG-181 AND ASP-183, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=25374360; DOI=10.1016/j.neuron.2014.10.008;
RA Seiradake E., del Toro D., Nagel D., Cop F., Haertl R., Ruff T.,
RA Seyit-Bremer G., Harlos K., Border E.C., Acker-Palmer A., Jones E.Y.,
RA Klein R.;
RT "FLRT structure: balancing repulsion and cell adhesion in cortical and
RT vascular development.";
RL Neuron 84:370-385(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 29-386 IN COMPLEX WITH ADGRL3,
RP INTERACTION WITH ADGRL3, MUTAGENESIS OF PHE-160, AND DOMAIN.
RX PubMed=26235031; DOI=10.1016/j.str.2015.06.022;
RA Ranaivoson F.M., Liu Q., Martini F., Bergami F., von Daake S., Li S.,
RA Lee D., Demeler B., Hendrickson W.A., Comoletti D.;
RT "Structural and mechanistic insights into the latrophilin3-FLRT3 complex
RT that mediates glutamatergic synapse development.";
RL Structure 23:1665-1677(2015).
CC -!- FUNCTION: Functions in cell-cell adhesion, cell migration and axon
CC guidance, exerting an attractive or repulsive role depending on its
CC interaction partners (PubMed:19056886, PubMed:25374360). Plays a role
CC in the spatial organization of brain neurons (PubMed:25374360). Plays a
CC role in vascular development in the retina (PubMed:25374360). Plays a
CC role in cell-cell adhesion via its interaction with ADGRL3 and probably
CC also other latrophilins that are expressed at the surface of adjacent
CC cells (PubMed:22405201, PubMed:25374360). Interaction with the
CC intracellular domain of ROBO1 mediates axon attraction towards cells
CC expressing NTN1 (PubMed:24560577). Mediates axon growth cone collapse
CC and plays a repulsive role in neuron guidance via its interaction with
CC UNC5B, and possibly also other UNC-5 family members (PubMed:21673655,
CC PubMed:25374360). Promotes neurite outgrowth (in vitro) (By
CC similarity). Mediates cell-cell contacts that promote an increase both
CC in neurite number and in neurite length (By similarity). Plays a role
CC in the regulation of the density of glutamaergic synapses
CC (PubMed:22405201). Plays a role in fibroblast growth factor-mediated
CC signaling cascades (PubMed:16872596). Required for normal morphogenesis
CC during embryonic development, but not for normal embryonic patterning
CC (PubMed:19056886). Required for normal ventral closure, headfold fusion
CC and definitive endoderm migration during embryonic development
CC (PubMed:18448090). Required for the formation of a normal basement
CC membrane and the maintenance of a normal anterior visceral endoderm
CC during embryonic development (PubMed:19056886).
CC {ECO:0000250|UniProtKB:B1H234, ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:18448090, ECO:0000269|PubMed:19056886,
CC ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Self-associates (via
CC leucine-rich repeats), giving rise to homooligomers (PubMed:25374360).
CC Interacts with FGFR1 (PubMed:16872596). Interacts (via extracellular
CC domain) with ADGRL1/LPHN1 and LPHN2 (via olfactomedin-like domain)
CC (PubMed:22405201). Interacts (via extracellular domain) with ADGRL3
CC (via olfactomedin-like domain) (PubMed:24739570, PubMed:22405201,
CC PubMed:26235031). Interacts (via extracellular domain) with UNC5B (via
CC Ig domain) (PubMed:19492039, PubMed:21673655, PubMed:22405201,
CC PubMed:25374360). May also interact (via extracellular domain) with
CC UNC5A and UNC5C (PubMed:22405201). Interacts (via extracellular domain)
CC with UNC5D (via extracellular domain) (PubMed:19492039). Identified in
CC complexes composed of FLRT3, ADGRL3 and UNC5B, respectively FLRT3,
CC ADGRL3 and UNC5D (By similarity). Interacts (via cytoplasmic domain)
CC with ROBO1 (PubMed:24560577). {ECO:0000250|UniProtKB:Q9NZU0,
CC ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655,
CC ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577,
CC ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25374360,
CC ECO:0000269|PubMed:26235031}.
CC -!- INTERACTION:
CC Q8BGT1; Q80TS3: Adgrl3; NbExp=6; IntAct=EBI-16166902, EBI-770665;
CC Q8BGT1; P12023: App; NbExp=2; IntAct=EBI-16166902, EBI-78814;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360}; Single-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16872596}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}.
CC Cell projection, axon {ECO:0000269|PubMed:24560577}. Cell projection,
CC growth cone membrane {ECO:0000269|PubMed:24560577}. Note=Detected on
CC dendritic punctae that colocalize in part with glutamaergic synapses,
CC but not with GABAergic synapses. Proteolytic cleavage in the
CC juxtamembrane region gives rise to a shedded ectodomain
CC (PubMed:21673655). {ECO:0000250|UniProtKB:B1H234,
CC ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:24560577}.
CC -!- TISSUE SPECIFICITY: Detected in adult brain (PubMed:21350012). Detected
CC in embryonic rostral thalamus neurons (at protein level)
CC (PubMed:24560577). Detected in embryonic rostral thalamus neurons
CC (PubMed:24560577). Detected in neonate eye, in the inner plexiform
CC layer and the outer nuclear layer (PubMed:25374360).
CC {ECO:0000269|PubMed:21350012, ECO:0000269|PubMed:24560577}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic brain at 13 dpc. Levels in
CC brain decrease gradually after 15 dpc, but expression continues after
CC birth (PubMed:21673655). Detected in embryonic myocardium, body wall
CC and pro-epicardial organ at 9.5 dpc. Detected throughout the myocardium
CC at 10.5 dpc, but levels in the epicardial cell layer are strongly
CC decreased. Almost exclusively detected in the neural tube at 14.5 dpc
CC (at protein level) (PubMed:21350012). Detected in the chorion and
CC visceral endoderm between 6 and 8 dpc (PubMed:19056886). Detected in
CC the visceral endoderm at 7 dpc, with a gradient from high expression in
CC the anterior part to low expression at the posterior part
CC (PubMed:19056886). At 8 dpc, detected in definitve endoderm, parts of
CC the neuroectoderm, the headfold and posterior mesoderm
CC (PubMed:19056886). Detected in the developing brain, the proepicardial
CC organ and in somites at 8.5 dpc (PubMed:16872596, PubMed:18448090). At
CC 9.5 and 10.5 dpc, detected in telencephalic vesicles, at the midbrain
CC boundaries with forebrain and hindbrain, the hypothalamic region, in
CC the apical ectodermal ridge, pharyngeal arches, the developing eye, the
CC epithelial structures surrounding the lower region of the developing
CC heart, limb buds and somites (PubMed:16872596, PubMed:18448090). At
CC 10.5 dpc, detected at interlimb somites with loss of expression at limb
CC somites and anterior trunk somites. At 11 dpc, detected in mesoderm in
CC head and branchial arches, migrating germ cells and limbs
CC (PubMed:16872596). {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:18448090, ECO:0000269|PubMed:19056886,
CC ECO:0000269|PubMed:21673655}.
CC -!- INDUCTION: Up-regulated by FGF2. {ECO:0000269|PubMed:16872596}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:21673655}.
CC -!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a
CC soluble ectodomain. Cleavage is probably effected by a metalloprotease.
CC {ECO:0000269|PubMed:21673655}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous mice are viable and fertile, but
CC homozygous mice display nearly complete embryonic lethality. Most
CC embryos die at about 10.5 dpc (PubMed:18448090, PubMed:19056886). A
CC majority present disruption of the basement membrane and ruptures of
CC the anterior visceral endoderm (PubMed:19056886). About one third
CC display a pronounced defect in the fusion of the lateral edges of the
CC body wall, resulting in cardia bifida. Mutant mice display also a
CC defect in proepicardial cell migration. About one third of the mutants
CC display abnormal morphogenesis of the neuroepithelium and headfold
CC fusion defects. Besides, mutant embryos display defects in definitive
CC endoderm migration, resulting in anterior axis truncations. Each of
CC these phenotypes has partial penetrance, and many mutant embryos
CC present a spectrum of defects. About 3% of the mutants develop into
CC viable and fertile adults (PubMed:18448090, PubMed:19056886).
CC {ECO:0000269|PubMed:18448090, ECO:0000269|PubMed:19056886}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98179.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY495670; AAR92203.1; -; mRNA.
DR EMBL; AK129369; BAC98179.1; ALT_INIT; mRNA.
DR EMBL; AK028252; BAC25843.1; -; mRNA.
DR EMBL; AK031464; BAC27417.1; -; mRNA.
DR EMBL; AL928700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28416.1; -; Genomic_DNA.
DR EMBL; BC052043; AAH52043.1; -; mRNA.
DR CCDS; CCDS16806.1; -.
DR RefSeq; NP_001165631.1; NM_001172160.1.
DR RefSeq; NP_848469.1; NM_178382.4.
DR PDB; 4V2E; X-ray; 2.50 A; A/B=29-359.
DR PDB; 4YEB; X-ray; 3.19 A; B=29-386.
DR PDBsum; 4V2E; -.
DR PDBsum; 4YEB; -.
DR AlphaFoldDB; Q8BGT1; -.
DR SMR; Q8BGT1; -.
DR DIP; DIP-61803N; -.
DR IntAct; Q8BGT1; 2.
DR STRING; 10090.ENSMUSP00000105684; -.
DR GlyCosmos; Q8BGT1; 1 site, No reported glycans.
DR GlyGen; Q8BGT1; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8BGT1; -.
DR PhosphoSitePlus; Q8BGT1; -.
DR MaxQB; Q8BGT1; -.
DR PaxDb; 10090-ENSMUSP00000053399; -.
DR ProteomicsDB; 273004; -.
DR ABCD; Q8BGT1; 1 sequenced antibody.
DR Antibodypedia; 24361; 125 antibodies from 24 providers.
DR DNASU; 71436; -.
DR Ensembl; ENSMUST00000056760.4; ENSMUSP00000053399.4; ENSMUSG00000051379.13.
DR Ensembl; ENSMUST00000110057.3; ENSMUSP00000105684.3; ENSMUSG00000051379.13.
DR GeneID; 71436; -.
DR KEGG; mmu:71436; -.
DR UCSC; uc012cfb.1; mouse.
DR AGR; MGI:1918686; -.
DR CTD; 23767; -.
DR MGI; MGI:1918686; Flrt3.
DR VEuPathDB; HostDB:ENSMUSG00000051379; -.
DR eggNOG; ENOG502QQBZ; Eukaryota.
DR GeneTree; ENSGT00940000159704; -.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; Q8BGT1; -.
DR OMA; DAIHISW; -.
DR OrthoDB; 2916435at2759; -.
DR PhylomeDB; Q8BGT1; -.
DR TreeFam; TF331598; -.
DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR BioGRID-ORCS; 71436; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Flrt3; mouse.
DR PRO; PR:Q8BGT1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BGT1; Protein.
DR Bgee; ENSMUSG00000051379; Expressed in undifferentiated genital tubercle and 258 other cell types or tissues.
DR Genevisible; Q8BGT1; MM.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0060322; P:head development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; IMP:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR45712:SF28; AGAP007037-PA; 1.
DR PANTHER; PTHR45712; AGAP008170-PA; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..649
FT /note="Leucine-rich repeat transmembrane protein FLRT3"
FT /id="PRO_0000434517"
FT TOPO_DOM 29..528
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..62
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 58..82
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 83..105
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 107..126
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 127..152
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 153..176
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 178..197
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 198..223
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 224..246
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 247..269
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 270..293
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 305..356
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 405..504
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 38..67
FT /note="Interaction with ADGRL3"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT REGION 629..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..37
FT /evidence="ECO:0007744|PDB:4V2E"
FT DISULFID 35..44
FT /evidence="ECO:0007744|PDB:4V2E"
FT DISULFID 309..334
FT /evidence="ECO:0007744|PDB:4V2E"
FT MUTAGEN 160
FT /note="F->A,N: Abolishes interaction with ADGRL3."
FT /evidence="ECO:0000269|PubMed:26235031"
FT MUTAGEN 165
FT /note="H->N: Abolishes interaction with UNC5B."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 181
FT /note="R->N: Abolishes homooligomerization and FLRT3-
FT mediated cell-cell adhesion; when associated with T-183."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 183
FT /note="D->N: Abolishes homooligomerization and FLRT3-
FT mediated cell-cell adhesion; when associated with N-181."
FT /evidence="ECO:0000269|PubMed:25374360"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4V2E"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4YEB"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4YEB"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4YEB"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4V2E"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4V2E"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:4V2E"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:4V2E"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4V2E"
SQ SEQUENCE 649 AA; 72879 MW; 736AC23C5E5BAA41 CRC64;
MISPAWSLFL IGTKIGLFFQ VAPLSVVAKS CPSVCRCDAG FIYCNDRSLT SIPVGIPEDA
TTLYLQNNQI NNVGIPSDLK NLLKVQRIYL YHNSLDEFPT NLPKYVKELH LQENNIRTIT
YDSLSKIPYL EELHLDDNSV SAVSIEEGAF RDSNYLRLLF LSRNHLSTIP GGLPRTIEEL
RLDDNRISTI SSPSLHGLTS LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA
PVNLPGTSLR KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL
ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLSA ELFDCKDSGI
VSTIQITTAI PNTAYPAQGQ WPAPVTKQPD IKNPKLIKDQ RTTGSPSRKT ILITVKSVTP
DTIHISWRLA LPMTALRLSW LKLGHSPAFG SITETIVTGE RSEYLVTALE PESPYRVCMV
PMETSNLYLF DETPVCIETQ TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV
SIALLALVCW YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS
NEPISKEEFV IHTIFPPNGM NLYKNNLSES SSNRSYRDSG IPDSDHSHS
//
