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Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin-like domain-containing leucine-rich transmembrane protein 3)

 FLRT3_XENTR             Reviewed;         648 AA.
B1H134;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 1.
10-OCT-2018, entry version 84.
RecName: Full=Leucine-rich repeat transmembrane protein FLRT3;
AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 3;
Flags: Precursor;
Name=flrt3 {ECO:0000312|Xenbase:XB-GENE-490901};
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Silurana.
NCBI_TaxID=8364;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=20431018; DOI=10.1126/science.1183670;
Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L.,
Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E.,
Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T.,
Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M.,
Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N.,
Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D.,
Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B.,
Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M.,
Rokhsar D.S.;
"The genome of the Western clawed frog Xenopus tropicalis.";
Science 328:633-636(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo {ECO:0000312|EMBL:AAI60452.1};
NIH - Xenopus Gene Collection (XGC) project;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19492039; DOI=10.1371/journal.pone.0005742;
Karaulanov E., Boettcher R.T., Stannek P., Wu W., Rau M., Ogata S.,
Cho K.W.Y., Niehrs C.;
"Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in
Xenopus embryos.";
PLoS ONE 4:E5742-E5742(2009).
-!- FUNCTION: Functions in cell-cell adhesion, cell migration and axon
guidance, exerting an attractive or repulsive role depending on
its interaction partners (By similarity). Modulates cadherin-
dependent cell-cell adhesion and cell sorting (By similarity).
Plays a role in the spatial organization of brain neurons. Plays a
role in vascular development. Plays a role in cell-cell adhesion
via its interaction with latrophilins that are expressed at the
surface of adjacent cells. Mediates axon attraction towards cells
expressing ntn1. mediates axon growth cone collapse and plays a
repulsive role in neuron guidance via its interaction with unc-5
family members. Plays a role in the regulation of the density of
glutamaergic synapses (By similarity). Plays a role in signaling
cascades downstream of fgfr1, and possibly also other fgfr family
members (By similarity). Plays a role in embryonic morphogenesis,
but not in embryonic patterning (PubMed:19492039).
{ECO:0000250|UniProtKB:Q70AK3, ECO:0000250|UniProtKB:Q8BGT1,
ECO:0000269|PubMed:19492039}.
-!- SUBUNIT: Interacts with fgfr1 and fgfr4. Interacts with rnd1, cdh1
and pcdh8. Interacts (via extracellular domain) with unc5b and
unc5d (via extracellular domain) (By similarity).
{ECO:0000250|UniProtKB:Q70AK3}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q70AK3}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:Q8BGT1}. Secreted
{ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon
{ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected at neuronal growth
cones. Proteolytic cleavage in the juxtamembrane region gives rise
to a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BGT1}.
-!- DEVELOPMENTAL STAGE: Detected in blastula and gastrula, in dorsal
mesoderm. {ECO:0000269|PubMed:19492039}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.
-!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise
to a soluble ectodomain. Cleavage is probably effected by a
metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}.
-----------------------------------------------------------------------
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EMBL; AAMC01004255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC160452; AAI60452.1; -; mRNA.
RefSeq; NP_001116922.1; NM_001123450.1.
RefSeq; XP_012818149.1; XM_012962695.2.
UniGene; Str.51730; -.
ProteinModelPortal; B1H134; -.
SMR; B1H134; -.
STRING; 8364.ENSXETP00000019062; -.
PaxDb; B1H134; -.
Ensembl; ENSXETT00000019062; ENSXETP00000019062; ENSXETG00000008706.
GeneID; 100144692; -.
KEGG; xtr:100144692; -.
CTD; 23767; -.
Xenbase; XB-GENE-490901; flrt3.
eggNOG; ENOG410IIEA; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000148996; -.
HOGENOM; HOG000290188; -.
HOVERGEN; HBG051629; -.
InParanoid; B1H134; -.
KO; K16362; -.
OrthoDB; EOG091G05YU; -.
TreeFam; TF331598; -.
Reactome; R-XTR-5654687; Downstream signaling of activated FGFR1.
Proteomes; UP000008143; Unassembled WGS sequence.
Bgee; ENSXETG00000008706; Expressed in 13 organ(s), highest expression level in embryo.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060322; P:head development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS51450; LRR; 8.
2: Evidence at transcript level;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Complete proteome; Developmental protein; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Leucine-rich repeat; Membrane;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 648 Leucine-rich repeat transmembrane protein
FLRT3.
/FTId=PRO_0000434520.
TOPO_DOM 29 527 Extracellular. {ECO:0000305}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 648 Cytoplasmic. {ECO:0000305}.
DOMAIN 30 62 LRRNT. {ECO:0000255}.
REPEAT 58 82 LRR 1. {ECO:0000255}.
REPEAT 83 105 LRR 2. {ECO:0000255}.
REPEAT 107 126 LRR 3. {ECO:0000255}.
REPEAT 127 152 LRR 4. {ECO:0000255}.
REPEAT 154 179 LRR 5. {ECO:0000255}.
REPEAT 181 197 LRR 6. {ECO:0000255}.
REPEAT 198 223 LRR 7. {ECO:0000255}.
REPEAT 225 246 LRR 8. {ECO:0000255}.
REPEAT 247 269 LRR 9. {ECO:0000255}.
REPEAT 270 293 LRR 10. {ECO:0000255}.
DOMAIN 305 356 LRRCT. {ECO:0000255}.
DOMAIN 409 503 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 31 37 {ECO:0000250|UniProtKB:Q8BGT1}.
DISULFID 35 44 {ECO:0000250|UniProtKB:Q8BGT1}.
DISULFID 309 334 {ECO:0000250|UniProtKB:Q8BGT1}.
SEQUENCE 648 AA; 73325 MW; 2087374908A934CC CRC64;
MSTETWNLFV AWAQLLLLFR ISPQYVNAKP CPSVCRCDGG FIYCNDRDLT SIPSGIPDDA
TTLYLQNNQI NNAGIPSDLR GLDKVERIYL YRNSLDEFPI NLPKNVKELH LQENNIRTIT
YDALSQIPSI EELHLDDNSV SAVSIEDGAF RDNIFLRLLF LSRNHLSTIP WGLPRTIEEL
RLDDNRISTI AEISLQDLTN LKRLVLDGNL LNNNGLGERV FMNLINLTEL SLVRNSLTSP
PANLPGTNLR KLYLQENHMN YVPPNAFADL TQLYRLDMSN NNITALPQGI FDDLDNLTQL
FLRNNPWYCG CKMKWVRDWL QSLPSKVNVR GLMCQAPERV RGMTIKDLNK ELFDCKDRIG
SNTIHVTTTV LNSLLPAQGQ WPVPVTKQPE IRPPDINKIF RTTPIPVKKI ITIQVKSITT
ETIYISWKVA LPMTALRLSW QLGHSPVFGS ITETIVTGDR TEYLLTALEP ESPYRICMVP
METGNIYLSD ETPVCIETET APLKMYNPTT TLNREQEKEP YKNSSLPLAA IIGGAVALVA
ITLLALVCWY VHRNGSLFSR NCAYSKGRRR KDDYAEAGTK KDNSILEIRE TSFPMIPINS
DPISKEEFII HTIFPPNGVS LYKNSHSESS SNRSYRDSGI PDSDHSHS


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