Flrt1
entrez
396184
canonical
uniprot
Q6RKD8
canonical
ensembl
ENSMUSG00000047787
resolver
ensp
ENSMUSP00000109010
resolver
ensp
ENSMUSP00000310179
resolver
genesymbol
Flrt1
resolver
uniprot
A0A452J8F8
resolver
uniprot
Q14DT7
resolver
uniprot
Q6RKD9
resolver
uniprot_entry
FLRT1_MOUSE
resolver
uniprot_sec
A0A452J8F8
resolver
uniprot_sec
Q14DT7
resolver
uniprot_sec
Q6RKD9
resolver
amino_acid_sequence
MVVAHSAATATTTPAATVTATVVMTTATMDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKVQVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNHLSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLPSAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAAVVNVRGLMCQGPEKVRGMAIKDITSEMDECFEAGSQGGAANAAAKTTVSNHASATTPQGSLFTLKAKRPGLRLPDSNIDYPMATGDGAKTLVIQVKPLTADSIRITWKAMLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMVTMETGNTYVADETPVCAKAETADSYGPTTTLNQEQNAGPMAGLPLAGIIGGAVALVFLFLVLGAICWYVHRAGELLTRERVYNRGSRRKDDYMESGTKKDNSILEIRGPGLQMLPINPYRSKEEYVVHTIFPSNGSSLCKGAHTIGYGTTRGYREAGIPDVDYSYT
uniprot
proteins
function
FUNCTION: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases (PubMed:16872596, PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length (PubMed:20421966). May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000305|PubMed:22405201}.
uniprot
proteins
mass_dalton
74151
uniprot
proteins
mutagenesis
MUTAGEN 600; /note="Y->F: Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-633 and F-671."; /evidence="ECO:0000269|PubMed:20421966"; MUTAGEN 633; /note="Y->F: Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-600 and F-671."; /evidence="ECO:0000269|PubMed:20421966"; MUTAGEN 671; /note="Y->F: Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-600 and F-633."; /evidence="ECO:0000269|PubMed:20421966
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in response to FGFR1 signaling, but is not a direct substrate of FGFR1 or SRC. A mutant where the Tyr phosphorylation sites have been replaced by Phe displays constitutive FGFR1-dependent activation of downstream MAP kinases. {ECO:0000269|PubMed:20421966}.; PTM: N-glycosylated. {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. {ECO:0000269|PubMed:21673655}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16872596
uniprot
proteins
pubmed
18448090
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20421966
uniprot
proteins
pubmed
21673655
uniprot
proteins
pubmed
22405201
uniprot
proteins
sequence_length
674
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, neuron projection {ECO:0000269|PubMed:20421966}. Cell junction {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along neurites and at contacts between neurite termini and other cells (PubMed:20421966). Proteolytic cleavage gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}.
uniprot
proteins
transmembrane_region
TRANSMEM 553..573; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins