FLRT2_MOUSE
ID FLRT2_MOUSE Reviewed; 660 AA.
AC Q8BLU0; Q6A073;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT2 {ECO:0000305};
DE AltName: Full=Fibronectin leucine rich transmembrane protein 2 {ECO:0000312|EMBL:AAH96471.1};
DE Flags: Precursor;
GN Name=Flrt2 {ECO:0000312|MGI:MGI:3603594};
GN Synonyms=Kiaa0405 {ECO:0000303|PubMed:15368895};
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:AAR92202.1}
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:AAR92202.1};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3] {ECO:0000312|Ensembl:ENSMUSP00000062171, ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000062171,
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary cancer;
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 [6] {ECO:0000312|EMBL:BAD32223.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-660.
RC TISSUE=Brain {ECO:0000312|EMBL:BAD32223.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [7]
RP 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, FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP 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 [9]
RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION, AND INTERACTION WITH UNC5D AND UNC5B.
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 [10]
RP INTERACTION WITH FGFR2.
RX PubMed=21765038; DOI=10.1177/0022034511415272;
RA Wei K., Xu Y., Tse H., Manolson M.F., Gong S.G.;
RT "Mouse FLRT2 interacts with the extracellular and intracellular regions of
RT FGFR2.";
RL J. Dent. Res. 90:1234-1239(2011).
RN [11]
RP INTERACTION WITH ADGRL1 AND ADGRL3, 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 [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FN1.
RX PubMed=24585683; DOI=10.1002/jcp.24597;
RA Flintoff K.A., Arudchelvan Y., Gong S.G.;
RT "FLRT2 interacts with fibronectin in the ATDC5 chondroprogenitor cells.";
RL J. Cell. Physiol. 229:1538-1547(2014).
RN [13]
RP INTERACTION WITH ADGRL3, AND FUNCTION.
RX PubMed=25728924; DOI=10.1016/j.str.2015.01.013;
RA Jackson V.A., del Toro D., Carrasquero M., Roversi P., Harlos K., Klein R.,
RA Seiradake E.;
RT "Structural basis of latrophilin-FLRT interaction.";
RL Structure 23:774-781(2015).
RN [14] {ECO:0007744|PDB:4V2C, ECO:0007744|PDB:4V2D}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 36-361 IN COMPLEX WITH UNC5D,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH UNC5D, DISULFIDE
RP BONDS, DOMAIN, AND MUTAGENESIS OF HIS-170; ARG-186; ASP-188; ASP-248 AND
RP PRO-250.
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).
CC -!- FUNCTION: Functions in cell-cell adhesion, cell migration and axon
CC guidance. Mediates cell-cell adhesion via its interactions with ADGRL3
CC and probably also other latrophilins that are expressed at the surface
CC of adjacent cells (PubMed:21350012, PubMed:25728924 PubMed:25374360).
CC May play a role in the migration of cortical neurons during brain
CC development via its interaction with UNC5D (PubMed:21673655). Mediates
CC axon growth cone collapse and plays a repulsive role in neuron guidance
CC via its interaction with UNC5D, and possibly also other UNC-5 family
CC members (PubMed:21673655, PubMed:25728924). Plays a role in fibroblast
CC growth factor-mediated signaling cascades (PubMed:16872596). Required
CC for normal organization of the cardiac basement membrane during
CC embryogenesis, and for normal embryonic epicardium and heart
CC morphogenesis (PubMed:21350012). {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:21350012, ECO:0000269|PubMed:21673655,
CC ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:25728924}.
CC -!- SUBUNIT: Self-associates (via leucine-rich repeats), giving rise to
CC homooligomers (PubMed:25374360). Interacts with FGFR1
CC (PubMed:16872596). Interacts with FGFR2 (PubMed:21765038). Interacts
CC (via extracellular domain) with ADGRL1/LPHN1 (PubMed:22405201).
CC Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like
CC domain)(PubMed:22405201, PubMed:25728924). Interacts (via extracellular
CC domain) with UNC5D (via the first Ig-like domain) (PubMed:21673655,
CC PubMed:25374360). Can also interact (via extracellular domain) with
CC UNC5B, but with much lower affinity (PubMed:21673655). Interacts (via
CC extracellular domain) with FN1 (PubMed:24585683).
CC {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655,
CC ECO:0000269|PubMed:21765038, ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:24585683, ECO:0000269|PubMed:25374360,
CC ECO:0000269|PubMed:25728924}.
CC -!- INTERACTION:
CC Q8BLU0; Q80TS3: Adgrl3; NbExp=2; IntAct=EBI-16146541, EBI-770665;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24585683,
CC ECO:0000269|PubMed:25374360}; Single-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:24585683}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:24585683}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:D3ZTV3}. Microsome membrane
CC {ECO:0000269|PubMed:24585683}. Secreted {ECO:0000269|PubMed:21673655}.
CC Note=Proteolytic cleavage gives rise to a shedded ectodomain.
CC {ECO:0000269|PubMed:21673655}.
CC -!- TISSUE SPECIFICITY: Detected in adult brain (at protein level).
CC {ECO:0000269|PubMed:21350012}.
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 in the epicardial cell
CC layer and throughout the myocardium at 10.5 dpc. Highly expressed in
CC embryonic and neonate heart, but after that levels decrease strongly,
CC and the protein is barely detectable 3 weeks after birth, with even
CC lower levels after 7 and 15 weeks (at protein level) (PubMed:21350012).
CC Detected in the anterior endoderm at 7.5 dpc. Detected on anterior
CC somites, the allantois and mesenchymal tissue behind the developing
CC heart at 8.5 dpc (PubMed:18448090). Detected in the cephalic mesenchyme
CC and in tissue posterior to the developing heart at 9.5 and 10.5 dpc.
CC Detected in the developing stomach and in a subset of the trunk
CC sclerotome at 10.5 dpc. At 11 dpc, detected also in branchial arches,
CC eyes and limbs (PubMed:16872596, PubMed:18448090).
CC {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:18448090,
CC ECO:0000269|PubMed:21350012, 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 12.5 dpc, probably due to impaired expansion of
CC the ventricular myocardium during development, reduced endocardial
CC volume and heart insufficiency. Contrary to wild-type, the epicardium
CC appears ruffled and presents numerous holes, due to defective formation
CC of cell-cell adhesions. Still, there is a very small percentage of
CC life-born pups that survive at least up to weaning.
CC {ECO:0000269|PubMed:21350012}.
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DR EMBL; AY495669; AAR92202.1; -; mRNA.
DR EMBL; AK041311; BAC30900.1; -; mRNA.
DR EMBL; AK135149; BAE22441.1; -; mRNA.
DR EMBL; AC122430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466549; EDL18942.1; -; Genomic_DNA.
DR EMBL; BC096471; AAH96471.1; -; mRNA.
DR EMBL; BC138297; AAI38298.1; -; mRNA.
DR EMBL; BC138298; AAI38299.1; -; mRNA.
DR EMBL; AK172945; BAD32223.1; -; mRNA.
DR CCDS; CCDS26094.1; -.
DR RefSeq; NP_958926.1; NM_201518.4.
DR RefSeq; XP_006516118.1; XM_006516055.3.
DR RefSeq; XP_011242434.1; XM_011244132.2.
DR PDB; 4V2C; X-ray; 4.00 A; A/C=35-362.
DR PDB; 4V2D; X-ray; 2.50 A; A=36-361.
DR PDB; 5FTT; X-ray; 3.40 A; B/F=35-362.
DR PDB; 5FTU; X-ray; 6.01 A; B/F/J=35-362.
DR PDBsum; 4V2C; -.
DR PDBsum; 4V2D; -.
DR PDBsum; 5FTT; -.
DR PDBsum; 5FTU; -.
DR AlphaFoldDB; Q8BLU0; -.
DR SMR; Q8BLU0; -.
DR DIP; DIP-61401N; -.
DR IntAct; Q8BLU0; 3.
DR MINT; Q8BLU0; -.
DR STRING; 10090.ENSMUSP00000062171; -.
DR GlyGen; Q8BLU0; 1 site.
DR iPTMnet; Q8BLU0; -.
DR PhosphoSitePlus; Q8BLU0; -.
DR MaxQB; Q8BLU0; -.
DR PaxDb; Q8BLU0; -.
DR PRIDE; Q8BLU0; -.
DR ProteomicsDB; 273003; -.
DR Antibodypedia; 55194; 73 antibodies from 16 providers.
DR DNASU; 399558; -.
DR Ensembl; ENSMUST00000057324; ENSMUSP00000062171; ENSMUSG00000047414.
DR Ensembl; ENSMUST00000110117; ENSMUSP00000105744; ENSMUSG00000047414.
DR GeneID; 399558; -.
DR KEGG; mmu:399558; -.
DR UCSC; uc007olc.2; mouse.
DR CTD; 23768; -.
DR MGI; MGI:3603594; Flrt2.
DR VEuPathDB; HostDB:ENSMUSG00000047414; -.
DR eggNOG; ENOG502QSJU; Eukaryota.
DR GeneTree; ENSGT00940000158937; -.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; Q8BLU0; -.
DR OMA; PTVPDWD; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q8BLU0; -.
DR TreeFam; TF315838; -.
DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR BioGRID-ORCS; 399558; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Flrt2; mouse.
DR PRO; PR:Q8BLU0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BLU0; protein.
DR Bgee; ENSMUSG00000047414; Expressed in rostral migratory stream and 238 other tissues.
DR Genevisible; Q8BLU0; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:UniProtKB.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; 3.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; Membrane;
KW Microsome; Reference proteome; Repeat; Secreted; Signal; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..660
FT /note="Leucine-rich repeat transmembrane protein FLRT2"
FT /id="PRO_0000434523"
FT TOPO_DOM 36..540
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 36..63
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 62..87
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 88..108
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 109..131
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 132..157
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 159..181
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 183..202
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 203..228
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 229..251
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 252..274
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 275..298
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 310..362
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 419..517
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 371..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..42
FT /evidence="ECO:0007744|PDB:4V2C, ECO:0007744|PDB:4V2D"
FT DISULFID 40..49
FT /evidence="ECO:0007744|PDB:4V2C, ECO:0007744|PDB:4V2D"
FT DISULFID 314..339
FT /evidence="ECO:0007744|PDB:4V2C, ECO:0007744|PDB:4V2D"
FT DISULFID 316..360
FT /evidence="ECO:0007744|PDB:4V2C, ECO:0007744|PDB:4V2D"
FT MUTAGEN 170
FT /note="H->E,N: Abolishes interaction with UNC5D."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 186
FT /note="R->N: Abolishes homooligomerization and FLRT2-
FT mediated cell-cell adhesion; when associated with T-188."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 188
FT /note="D->T: Abolishes homooligomerization and FLRT2-
FT mediated cell-cell adhesion; when associated with N-186."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 248
FT /note="D->N: No effect on interaction with UNC5D; when
FT associated with T-250."
FT /evidence="ECO:0000269|PubMed:25374360"
FT MUTAGEN 250
FT /note="P->T: No effect on interaction with UNC5D; when
FT associated with N-248."
FT /evidence="ECO:0000269|PubMed:25374360"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4V2D"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 343..347
FT /evidence="ECO:0007829|PDB:4V2D"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4V2D"
FT TURN 355..359
FT /evidence="ECO:0007829|PDB:5FTT"
SQ SEQUENCE 660 AA; 73948 MW; 5C1A9BBA3142C020 CRC64;
MGLQTTKWPG RGAFILKFWL IISLGLYLQV SKLLACPSVC RCDRNFVYCN ERSLTSVPLG
IPEGVTVLYL HNNQINNAGF PAELHNVQSV HTVYLYGNQL DEFPMNLPKN VRVLHLQENN
IQTISRAALA QLLKLEELHL DDNSISTVGV EDGAFREAIS LKLLFLSKNH LSSVPVGLPV
DLQELRVDEN RIAVISDMAF QNLTSLERLI VDGNLLTNKG IAEGTFSHLT KLKEFSIVRN
SLSHPPPDLP GTHLIRLYLQ DNQINHIPLT AFANLRKLER LDISNNQLRM LTQGVFDHLS
NLKQLTARNN PWFCDCSIKW VTEWLKYIPS SLNVRGFMCQ GPEQVRGMAV RELNMNLLSC
PTTTPGLPVF TPAPSTVSPT TQSPTLSVPS PSRGSVPPAP TPSKLPTIPD WDGRERVTPP
ISERIQLSIH FVNDTSIQVS WLSLFTVMAY KLTWVKMGHS LVGGIVQERI VSGEKQHLSL
VNLEPRSTYR ICLVPLDAFN YRTVEDTICS EATTHASYLN NGSNTASSHE QTTSHSMGSP
FLLAGLIGGA VIFVLVVLLS VFCWHMHKKG RYTSQKWKYN RGRRKDDYCE AGTKKDNSIL
EMTETSFQIV SLNNDQLLKG DFRLQPIYTP NGGINYTDCH IPNNMRYCNS SVPDLEHCHT
