Leucine-rich repeat transmembrane protein FLRT3

UniProt data

UniProt name: FLRT3_HUMAN (Q9NZU0)

Gene name: FLRT3; Synonyms=KIAA1469; ORFNames=UNQ856/PRO1865

Organism: Homo sapiens (Human).

Function: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:26235030). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity). Promotes neurite outgrowth (in vitro) (PubMed:14706654). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length. Plays a role in the regulation of the density of glutamaergic synapses. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning. Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development. Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (By similarity). {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:14706654, ECO:0000269|PubMed:26235030}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:14706654, ECO:0000269|PubMed:26235030}; Single-pass membrane protein {ECO:0000269|PubMed:14706654, ECO:0000305}. 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 on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Detected on axons and at axon termini. Detected at neuronal growth cones. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1}.

Transmembrane domains:

  1. 529-549, 21 AA, Helical. {ECO:0000255}.

Sequence: 649 AA

10 20 30 40 50 60 MISAAWSIFL IGTKIGLFLQ VAPLSVMAKS CPSVCRCDAG FIYCNDRFLT SIPTGIPEDA 70 80 90 100 110 120 TTLYLQNNQI NNAGIPSDLK NLLKVERIYL YHNSLDEFPT NLPKYVKELH LQENNIRTIT 130 140 150 160 170 180 YDSLSKIPYL EELHLDDNSV SAVSIEEGAF RDSNYLRLLF LSRNHLSTIP WGLPRTIEEL 190 200 210 220 230 240 RLDDNRISTI SSPSLQGLTS LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA 250 260 270 280 290 300 PVNLPGTNLR KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL 310 320 330 340 350 360 ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLNA ELFDCKDSGI 370 380 390 400 410 420 VSTIQITTAI PNTVYPAQGQ WPAPVTKQPD IKNPKLTKDH QTTGSPSRKT ITITVKSVTS 430 440 450 460 470 480 DTIHISWKLA LPMTALRLSW LKLGHSPAFG SITETIVTGE RSEYLVTALE PDSPYKVCMV 490 500 510 520 530 540 PMETSNLYLF DETPVCIETE TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV 550 560 570 580 590 600 TIALLALVCW YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS 610 620 630 640 NEPISKEEFV IHTIFPPNGM NLYKNNHSES SSNRSYRDSG IPDSDHSHS

CATM prediction

The sequence of FLRT3_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
      530       540       550
    |    +    |    +    |  		 (Å) (°) (Å) (°)  
Model 1 NLALAAIIGGAVALVTIALLALVCWYV 6.4 -48.7° 1.8 45.2 -35.9
Model 2 NLALAAIIGGAVALVTIALLALVCWYV 6.8 -47.7° 1.1 36.2 -31.5
Prolines* NLPLAAIIGGAVALVTIALLALVCWYV          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 531, ALA, HA A, 530, ALA, O 2.69Å
B, 534, GLY, HA1 A, 531, ALA, O 2.36Å
B, 535, GLY, HA2 A, 534, GLY, O 2.91Å
A, 531, ALA, HA B, 530, ALA, O 2.69Å
A, 534, GLY, HA1 B, 531, ALA, O 2.36Å
A, 535, GLY, HA2 B, 534, GLY, O 2.91Å