FLRT3_PONAB
ID FLRT3_PONAB Reviewed; 649 AA.
AC Q5R6T0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in the spatial organization of brain
CC neurons. Plays a role in vascular development in the retina (By
CC similarity). Plays a role in cell-cell adhesion via its interaction
CC with ADGRL3 and probably also other latrophilins that are expressed at
CC the surface of adjacent cells (By similarity). Interaction with the
CC intracellular domain of ROBO1 mediates axon attraction towards cells
CC expressing NTN1. Mediates axon growth cone collapse and plays a
CC repulsive role in neuron guidance via its interaction with UNC5B, and
CC possibly also other UNC-5 family members (By similarity). Promotes
CC neurite outgrowth (in vitro). Mediates cell-cell contacts that promote
CC an increase both in neurite number and in neurite length. Plays a role
CC in the regulation of the density of glutamaergic synapses. Plays a role
CC in fibroblast growth factor-mediated signaling cascades. Required for
CC normal morphogenesis during embryonic development, but not for normal
CC embryonic patterning. Required for normal ventral closure, headfold
CC fusion and definitive endoderm migration during embryonic development.
CC Required for the formation of a normal basement membrane and the
CC maintenance of a normal anterior visceral endoderm during embryonic
CC development (By similarity). {ECO:0000250|UniProtKB:B1H234,
CC ECO:0000250|UniProtKB:Q8BGT1, ECO:0000250|UniProtKB:Q9NZU0}.
CC -!- SUBUNIT: Monomer and homodimer. Self-associates (via leucine-rich
CC repeats), giving rise to homooligomers (By similarity). Interacts with
CC FGFR1. Interacts (via extracellular domain) with ADGRL1/LPHN1 and LPHN2
CC (via olfactomedin-like domain) (By similarity). Interacts (via
CC extracellular domain) with ADGRL3 (via olfactomedin-like domain); the
CC interaction is direct. Interacts (via extracellular domain) with UNC5B
CC and UNC5D (via extracellular domain); the interaction is direct.
CC Identified in complexes composed of FLRT3, ADGRL3 and UNC5B,
CC respectively FLRT3, ADGRL3 and UNC5D (By similarity). May also interact
CC (via extracellular domain) with UNC5A and UNC5C. Interacts (via
CC cytoplasmic domain) with ROBO1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BGT1, ECO:0000250|UniProtKB:Q9NZU0}.
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 -!- 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; CR860404; CAH92530.1; -; mRNA.
DR RefSeq; NP_001127561.1; NM_001134089.2.
DR AlphaFoldDB; Q5R6T0; -.
DR SMR; Q5R6T0; -.
DR STRING; 9601.ENSPPYP00000011984; -.
DR GeneID; 100174639; -.
DR KEGG; pon:100174639; -.
DR CTD; 23767; -.
DR eggNOG; ENOG502QQBZ; Eukaryota.
DR InParanoid; Q5R6T0; -.
DR Proteomes; UP000001595; Unplaced.
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: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..649
FT /note="Leucine-rich repeat transmembrane protein FLRT3"
FT /id="PRO_0000352674"
FT TOPO_DOM 29..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..58
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 59..80
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 84..104
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 105..126
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 129..150
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 155..176
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 177..197
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 200..220
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 226..247
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 248..269
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 272..293
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 305..357
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 409..504
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 38..67
FT /note="Interaction with ADGRL3"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 649 AA; 73131 MW; B7775F241C0C0F52 CRC64;
MISPAWSIFL IGTKIGLFLQ VAPLSVMAKS CPSVCRCDAG FIYCNDRFLT SIPTGIPEDA
TTLYLQNNQI NNAGIPSDLK NLLKVERIYL YHNSLDEFPT NLPKYVKELH LQENNIRTIT
YDSLSKIPYL EELRLDDNSV SAVSIEEGAF RDSNYLRLLF LSRNHLSTIP WGLPRTIEEL
RLDDNRIPTI SSPSLQGLTS LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA
PVNLPGTNLR KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL
ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLNA ELFDCKDSGI
VSTIQITTAI PNTVYPAQEQ WPAPVTKQPD IKNPKLTKDH QTTGSPSRKT ITITVKSVTS
DTIHISWKLA LPMTALRLSW LKLGHSPAFG SITETIVTGE RSEYLVTALE PDSPYKVCMV
PMETSNLYLF DETPVCIETE TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV
TIALLALVCW YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS
NEPISKEEFV IHTIFPPNGM NLYKNNHSES SSNRSYRDSG IPDSDHSHS
