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FLRT3_MOUSE
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   03-AUG-2022, entry version 173.
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|Ensembl:ENSMUSP00000053399,
RC   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};
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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.ENSMUSP00000053399; -.
DR   GlyGen; Q8BGT1; 1 site.
DR   iPTMnet; Q8BGT1; -.
DR   PhosphoSitePlus; Q8BGT1; -.
DR   MaxQB; Q8BGT1; -.
DR   PaxDb; Q8BGT1; -.
DR   PRIDE; Q8BGT1; -.
DR   ProteomicsDB; 273004; -.
DR   ABCD; Q8BGT1; 1 sequenced antibody.
DR   Antibodypedia; 24361; 114 antibodies from 24 providers.
DR   DNASU; 71436; -.
DR   Ensembl; ENSMUST00000056760; ENSMUSP00000053399; ENSMUSG00000051379.
DR   Ensembl; ENSMUST00000110057; ENSMUSP00000105684; ENSMUSG00000051379.
DR   GeneID; 71436; -.
DR   KEGG; mmu:71436; -.
DR   UCSC; uc012cfb.1; mouse.
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; LIWTKIG; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q8BGT1; -.
DR   TreeFam; TF331598; -.
DR   Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR   BioGRID-ORCS; 71436; 0 hits in 73 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 255 other 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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISS: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; -; 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   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
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
 
 
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