FLRT3_XENLA
ID FLRT3_XENLA Reviewed; 648 AA.
AC Q70AK3; B7ZR53;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
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|EMBL:CAE54086.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:CAE54086.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH FGFR1 AND FGFR4, AND DEVELOPMENTAL STAGE.
RX PubMed=14688794; DOI=10.1038/ncb1082;
RA Bottcher R.T., Pollet N., Delius H., Niehrs C.;
RT "The transmembrane protein XFLRT3 forms a complex with FGF receptors and
RT promotes FGF signalling.";
RL Nat. Cell Biol. 6:38-44(2004).
RN [2] {ECO:0000312|EMBL:AAI70046.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI70046.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH RND1; CDH1 AND PCDH8.
RX PubMed=20027292; DOI=10.1371/journal.pone.0008411;
RA Chen X., Koh E., Yoder M., Gumbiner B.M.;
RT "A protocadherin-cadherin-FLRT3 complex controls cell adhesion and
RT morphogenesis.";
RL PLoS ONE 4:E8411-E8411(2009).
RN [4]
RP FUNCTION, INTERACTION WITH UNC5B AND UNC5D, AND SUBCELLULAR LOCATION.
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 (PubMed:20027292, PubMed:19492039).
CC Plays a role in the spatial organization of brain neurons. Plays a role
CC in vascular development. Plays a role in cell-cell adhesion via its
CC interaction with latrophilins that are expressed at the surface of
CC adjacent cells. Mediates axon attraction towards cells expressing ntn1.
CC Mediates axon growth cone collapse and plays a repulsive role in neuron
CC guidance via its interaction with unc-5 family members. Plays a role in
CC the 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 (PubMed:14688794). Plays a role in
CC embryonic morphogenesis, but not in embryonic patterning
CC (PubMed:19492039). {ECO:0000250|UniProtKB:Q8BGT1,
CC ECO:0000269|PubMed:14688794, ECO:0000269|PubMed:19492039,
CC ECO:0000269|PubMed:20027292}.
CC -!- SUBUNIT: Interacts with fgfr1 and fgfr4 (PubMed:14688794). Interacts
CC with rnd1, cdh1 and pcdh8 (PubMed:20027292). Interacts (via
CC extracellular domain) with unc5b and unc5d (via extracellular domain)
CC (PubMed:19492039). {ECO:0000269|PubMed:14688794,
CC ECO:0000269|PubMed:19492039, ECO:0000269|PubMed:20027292}.
CC -!- INTERACTION:
CC Q70AK3; Q70AK3: flrt3; NbExp=2; IntAct=EBI-8042279, EBI-8042279;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14688794,
CC ECO:0000305|PubMed:19492039}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion
CC {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: First detected at the mid-blastula transition. In
CC gastrula, detected at the marginal zone. In neurula, detected at the
CC boundary between midbrain and hindbrain, and at the anterior neural
CC ridge. In tadpoles, detected in telencephalon, diencephalon, at the
CC boundary between midbrain and hindbrain, in ears and branchial arches.
CC {ECO:0000269|PubMed:14688794}.
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; AJ605776; CAE54086.1; -; mRNA.
DR EMBL; BC170046; AAI70046.1; -; mRNA.
DR EMBL; BC170048; AAI70048.1; -; mRNA.
DR RefSeq; NP_001080928.1; NM_001087459.1.
DR AlphaFoldDB; Q70AK3; -.
DR SMR; Q70AK3; -.
DR IntAct; Q70AK3; 3.
DR MINT; Q70AK3; -.
DR GeneID; 394225; -.
DR KEGG; xla:394225; -.
DR CTD; 394225; -.
DR Xenbase; XB-GENE-17334173; flrt3.S.
DR OMA; MAAQCKN; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 394225; Expressed in gastrula and 13 other tissues.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; IPI:IntAct.
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; 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; 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 1: Evidence at protein 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 /evidence="ECO:0000255"
FT /id="PRO_0000434519"
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 153..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:Q9NZU0"
FT DISULFID 35..44
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT DISULFID 309..334
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT CONFLICT 370
FT /note="M -> T (in Ref. 1; CAE54086)"
SQ SEQUENCE 648 AA; 73376 MW; 6F7EAD7591398549 CRC64;
MSTETWNLFV AWAQFLLLLR MLPQCDSAKP CPSVCRCDAG FIYCNDRDLT SIPSGIPDDA
TTLYLQNNQI NNAGIPSDLK GLDKVERIYL YRNSLDEFPI NLPKNVKELH LQENNIRTIT
YDALLQIPFI EELHLDDNSV SAVSIEDGAF RDNIFLRLLF LSRNHLSTIP WGLPKTIEEL
RLDDNRISTI SEISLQDLTN LKRLVLDGNL LNNNGLGERV FMNLINLTEL SLVRNSLTSP
PANLPGTSLR KLYLQENHMN YVPPNSFADL TQLYRLDMSN NNLTALPQGI FDDLDNLTQL
FLRNNPWYCG CKMKWVRDWL QSLPSKVNVR GLMCQAPERV RGMTIKDLNK ELFDCKDRIG
SNTIHVTTTM LNSLLPAQGQ WPVPVTKQPE IRPPDINKIF RTTPIPVKKI ITIQVKSITT
ETIYISWKVA LPMTALRLSW QLGHSPVFGS ITETIVTGDR AEYLLTALEP ESPYRICMVP
METGNIYLSD ETPVCIETET APLKMYNPTT TLNREQEKEP YKNSSLPLAA IIGGAVALVA
ITLLALVCWY VHRNGSLFSR NCAYNKGRRR KDDYAEAGTK KDNSILEIRE TSFPMIPINS
DPLSKEEFII HTIFPPNGVS LYKNSHSESS SNRSYRDSGI PDSDHSHS
