Leucine-rich repeat transmembrane protein FLRT2

UniProt data

UniProt name: FLRT2_HUMAN (O43155)

Gene name: FLRT2; Synonyms=KIAA0405; ORFNames=UNQ232/PRO265

Organism: Homo sapiens (Human).

Function: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis. {ECO:0000250|UniProtKB:Q8BLU0}.

Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BLU0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BLU0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BLU0}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BLU0}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8BLU0}. Microsome membrane {ECO:0000250|UniProtKB:Q8BLU0}. Secreted {ECO:0000250|UniProtKB:Q8BLU0}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTV3}. Note=Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BLU0}.

Transmembrane domains:

  1. 542-562, 21 AA, Helical. {ECO:0000255}.

Sequence: 660 AA

10 20 30 40 50 60 MGLQTTKWPS HGAFFLKSWL IISLGLYSQV SKLLACPSVC RCDRNFVYCN ERSLTSVPLG 70 80 90 100 110 120 IPEGVTVLYL HNNQINNAGF PAELHNVQSV HTVYLYGNQL DEFPMNLPKN VRVLHLQENN 130 140 150 160 170 180 IQTISRAALA QLLKLEELHL DDNSISTVGV EDGAFREAIS LKLLFLSKNH LSSVPVGLPV 190 200 210 220 230 240 DLQELRVDEN RIAVISDMAF QNLTSLERLI VDGNLLTNKG IAEGTFSHLT KLKEFSIVRN 250 260 270 280 290 300 SLSHPPPDLP GTHLIRLYLQ DNQINHIPLT AFSNLRKLER LDISNNQLRM LTQGVFDNLS 310 320 330 340 350 360 NLKQLTARNN PWFCDCSIKW VTEWLKYIPS SLNVRGFMCQ GPEQVRGMAV RELNMNLLSC 370 380 390 400 410 420 PTTTPGLPLF TPAPSTASPT TQPPTLSIPN PSRSYTPPTP TTSKLPTIPD WDGRERVTPP 430 440 450 460 470 480 ISERIQLSIH FVNDTSIQVS WLSLFTVMAY KLTWVKMGHS LVGGIVQERI VSGEKQHLSL 490 500 510 520 530 540 VNLEPRSTYR ICLVPLDAFN YRAVEDTICS EATTHASYLN NGSNTASSHE QTTSHSMGSP 550 560 570 580 590 600 FLLAGLIGGA VIFVLVVLLS VFCWHMHKKG RYTSQKWKYN RGRRKDDYCE AGTKKDNSIL 610 620 630 640 650 EMTETSFQIV SLNNDQLLKG DFRLQPIYTP NGGINYTDCH IPNNMRYCNS SVPDLEHCHT

CATM prediction

The sequence of FLRT2_HUMAN returned 6 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
   540       550       560   
 |    +    |    +    |    +		 (Å) (°) (Å) (°)  
Model 1 SAFLLAGLIGGAVIFVLVVLLSVFCWH 6.5 -44.1° 1.8 44.9 -29.6
Model 2 SAFLLAGLIGGAVIFVLVVLLSVFCWH 6.7 -49.4° 3.9 38.1 -21.2
Model 3 SAFLLAGLIGGAVIFVLVVLLSVFCWH 7.3 -43.0° 3.0 34.7 -19.4
Model 4 SAFLLAGLIGGAVIFVLVVLLSVFCWH 6.8 -28.0° 6.0 47.0 -18.3
Model 5 SAFLLAGLIGGAVIFVLVVLLSVFCWH 7.3 -55.0° 2.4 47.7 -12.1
Model 6 SAFLLAGLIGGAVIFVLVVLLSVFCWH 7.2 -49.0° 4.5 49.0 -1.7
Prolines* SPFLLAGLIGGAVIFVLVVLLSVFCWH          

* 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, 545, GLY, HA1 A, 542, LEU, O 2.49Å
B, 546, LEU, HA A, 545, GLY, O 2.70Å
A, 545, GLY, HA1 B, 542, LEU, O 2.49Å
A, 546, LEU, HA B, 545, GLY, O 2.70Å