FLRT3_XENTR
ID FLRT3_XENTR Reviewed; 648 AA.
AC B1H134;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT3;
DE AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 3;
DE Flags: Precursor;
GN Name=flrt3 {ECO:0000312|Xenbase:XB-GENE-490901};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAI60452.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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).
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 (By similarity). Modulates cadherin-dependent
CC cell-cell adhesion and cell sorting (By similarity). Plays a role in
CC the spatial organization of brain neurons. Plays a role in vascular
CC development. Plays a role in cell-cell adhesion via its interaction
CC with latrophilins that are expressed at the surface of adjacent cells.
CC Mediates axon attraction towards cells expressing ntn1. mediates axon
CC growth cone collapse and plays a repulsive role in neuron guidance via
CC its interaction with unc-5 family members. Plays a role in the
CC regulation of the density of glutamaergic synapses (By similarity).
CC Plays a role in signaling cascades downstream of fgfr1, and possibly
CC also other fgfr family members (By similarity). Plays a role in
CC embryonic morphogenesis, but not in embryonic patterning
CC (PubMed:19492039). {ECO:0000250|UniProtKB:Q70AK3,
CC ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:19492039}.
CC -!- SUBUNIT: Interacts with fgfr1 and fgfr4. Interacts with rnd1, cdh1 and
CC pcdh8. Interacts (via extracellular domain) with unc5b and unc5d (via
CC extracellular domain) (By similarity). {ECO:0000250|UniProtKB:Q70AK3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BGT1};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted
CC {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, growth cone membrane
CC {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that
CC colocalize in part with glutamaergic synapses, but not with GABAergic
CC synapses. Proteolytic cleavage in the juxtamembrane region gives rise
CC to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234,
CC ECO:0000250|UniProtKB:Q8BGT1}.
CC -!- DEVELOPMENTAL STAGE: Detected in blastula and gastrula, in dorsal
CC mesoderm. {ECO:0000269|PubMed:19492039}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.
CC -!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a
CC soluble ectodomain. Cleavage is probably effected by a metalloprotease.
CC {ECO:0000250|UniProtKB:Q8BGT1}.
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DR EMBL; AAMC01004255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC160452; AAI60452.1; -; mRNA.
DR RefSeq; NP_001116922.1; NM_001123450.1.
DR RefSeq; XP_012818149.1; XM_012962695.2.
DR AlphaFoldDB; B1H134; -.
DR SMR; B1H134; -.
DR STRING; 8364.ENSXETP00000019062; -.
DR PaxDb; B1H134; -.
DR GeneID; 100144692; -.
DR KEGG; xtr:100144692; -.
DR CTD; 23767; -.
DR Xenbase; XB-GENE-490901; flrt3.
DR eggNOG; ENOG502QQBZ; Eukaryota.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; B1H134; -.
DR OMA; MAAQCKN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; B1H134; -.
DR TreeFam; TF331598; -.
DR Reactome; R-XTR-5654687; Downstream signaling of activated FGFR1.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000008706; Expressed in embryo and 9 other tissues.
DR ExpressionAtlas; B1H134; baseline.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060322; P:head development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
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; 2.
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.
DR PROSITE; PS51450; LRR; 8.
PE 2: Evidence at transcript level;
KW 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..648
FT /note="Leucine-rich repeat transmembrane protein FLRT3"
FT /id="PRO_0000434520"
FT TOPO_DOM 29..527
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..648
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 154..179
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 181..197
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 198..223
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 225..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 409..503
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 624..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..37
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 35..44
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 309..334
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
SQ 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
