Flrt3
entrez
71436
canonical
uniprot
Q8BGT1
canonical
ensembl
ENSMUSG00000051379
resolver
ensp
ENSMUSP00000053399
resolver
ensp
ENSMUSP00000105684
resolver
enst
ENSMUST00000056760
resolver
enst
ENSMUST00000110057
resolver
genesymbol
Flrt3
resolver
genesymbol_syn
Kiaa1469
resolver
uniprot
Q6ZPQ1
resolver
uniprot_entry
FLRT3_MOUSE
resolver
uniprot_sec
Q6ZPQ1
resolver
amino_acid_sequence
MISPAWSLFLIGTKIGLFFQVAPLSVVAKSCPSVCRCDAGFIYCNDRSLTSIPVGIPEDATTLYLQNNQINNVGIPSDLKNLLKVQRIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPGGLPRTIEELRLDDNRISTISSPSLHGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTSLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWLQSLPVKVNVRGLMCQAPEKVRGMAIKDLSAELFDCKDSGIVSTIQITTAIPNTAYPAQGQWPAPVTKQPDIKNPKLIKDQRTTGSPSRKTILITVKSVTPDTIHISWRLALPMTALRLSWLKLGHSPAFGSITETIVTGERSEYLVTALEPESPYRVCMVPMETSNLYLFDETPVCIETQTAPLRMYNPTTTLNREQEKEPYKNPNLPLAAIIGGAVALVSIALLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFQMLPISNEPISKEEFVIHTIFPPNGMNLYKNNLSESSSNRSYRDSGIPDSDHSHS
uniprot
proteins
function
FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (PubMed:19056886, PubMed:30792275, 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:30792275, 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). {ECO:0000250|UniProtKB:B1H234, ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:18448090, ECO:0000269|PubMed:19056886, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:30792275}.
uniprot
proteins
mass_dalton
72879
uniprot
proteins
mutagenesis
MUTAGEN 160; /note="F->A,N: Abolishes interaction with ADGRL3."; /evidence="ECO:0000269|PubMed:26235031"; MUTAGEN 165; /note="H->N: Abolishes interaction with UNC5B."; /evidence="ECO:0000269|PubMed:25374360"; MUTAGEN 181; /note="R->N: Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with T-183."; /evidence="ECO:0000269|PubMed:25374360"; MUTAGEN 183; /note="D->N: Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with N-181."; /evidence="ECO:0000269|PubMed:25374360
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000269|PubMed:21673655}.
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16872596
uniprot
proteins
pubmed
18448090
uniprot
proteins
pubmed
19056886
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19492039
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21350012
uniprot
proteins
pubmed
21673655
uniprot
proteins
pubmed
22405201
uniprot
proteins
pubmed
24560577
uniprot
proteins
pubmed
24739570
uniprot
proteins
pubmed
25374360
uniprot
proteins
pubmed
26235031
uniprot
proteins
pubmed
30792275
uniprot
proteins
sequence_length
649
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360}; Single-pass membrane protein {ECO:0000305}. Presynaptic cell membrane {ECO:0000269|PubMed:30792275}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, axon {ECO:0000269|PubMed:24560577}. Cell projection, growth cone membrane {ECO:0000269|PubMed:24560577}. Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000250|UniProtKB:B1H234, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:24560577}.
uniprot
proteins
transmembrane_region
TRANSMEM 529..549; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins