3.A.3.8.24
Broad range phospholipid-transporting ATPase 10, ALA10, of 1202 aas and 10 TMSs. A structural model of ALA10 reveals a cavity delimited by TMSs 3, 4 and 5 at a similar position as the cation-binding region in related cation transporting P-type ATPases. Docking of a phosphatidylcholine headgroup in silico showed that the cavity can accommodate a phospholipid headgroup, likely leaving the fatty acid tails in contact with the hydrophobic portion of the lipid bilayer. Mutagenesis data supported this interpretation and suggested that two residues in TMS 4 (Y374 and F375) are important for coordination of the phospholipid headgroup (Jensen et al. 2017). These results point to a general mechanism of lipid translocation by P4 ATPases, which closely resembles that of cation-transporting pumps, through coordination of the hydrophilic portion of the substrate in a central membrane cavity.
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| Accession Number: | Q9LI83 |
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| Protein Name: | Phospholipid-transporting ATPase 10 |
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| Length: | 1202 |
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| Molecular Weight: | 136279.00 |
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| Species: | Arabidopsis thaliana (Mouse-ear cress) [3702] |
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| Number of TMSs: | 10 |
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| Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
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| Substrate |
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1: MAGPSRRRRR LHLSKIYSYT CGKSSFQEDH SNIGGPGFSR VVYCNEPGSP AAERRNYAGN
61: YVRSTKYTVA SFFPKSLFEQ FRRVANFYFL VTGILSLTDL SPYGAVSALL PLALVISATM
121: VKEGIEDWRR KQQDIEVNNR KVKVHDGNGI FRQEEWRNLR VGDIVRVEKD EFFPADLLLL
181: SSSYEDSVCY VETMNLDGET NLKVKQGLEA TSSLLNQDSD FKDFRGVVRC EDPNVNLYVF
241: VGTLALEEER FPLSIQQILL RDSKLRNTEY VYGAVVFTGH DTKVIQNSTD PPSKRSRIER
301: TMDKIIYLMF GLVFLMSFVG SIIFGVETRE DKVKNGRTER WYLKPDDADI FFDPERAPMA
361: AIYHFFTATM LYSYFIPISL YVSIEIVKVL QSIFINRDIH MYYEETDKPA QARTSNLNEE
421: LGMVDTILSD KTGTLTCNSM EFIKCSIAGK AYGRGITEVE RAMAVRSGGS PLVNEDLDVV
481: VDQSGPKVKG FNFEDERVMN GNWVRQPEAA VLQKFFRLLA VCHTAIPETD EESGNVSYEA
541: ESPDEAAFVV AAREFGFEFF NRTQNGISFR ELDLVSGEKV ERVYRLLNVL EFNSTRKRMS
601: VIVRDDDGKL LLLSKGADNV MFERLAKNGR QFEAKTQEHV NQYADAGLRT LVLAYREVDE
661: NEYIEFNKSF NEAKASVSED REALIDEITD KMERDLILLG ATAVEDKLQN GVPECIDKLA
721: QAGIKIWVLT GDKMETAINI GFASSLLRQE MKQIIINLET PQIKSLEKSG GKDEIELASR
781: ESVVMQLQEG KALLAASGAS SEAFALIIDG KSLTYALEDE IKKMFLDLAT SCASVICCRS
841: SPKQKALVTR LVKSGTGKTT LAIGDGANDV GMLQEADIGV GISGVEGMQA VMSSDIAIAQ
901: FRYLERLLLV HGHWCYSRIA SMICYFFYKN ITFGVTVFLY EAYTSFSGQP AYNDWFLSLF
961: NVFFSSLPVI ALGVFDQDVS ARFCYKFPLL YQEGVQNILF SWKRIIGWMF NGFISALAIF
1021: FLCKESLKHQ LFDPDGKTAG REILGGTMYT CVVWVVNLQM ALSISYFTWV QHIVIWGSIA
1081: FWYIFLMIYG AMTPSFSTDA YMVFLEALAP APSYWLTTLF VMIFALIPYF VYKSVQMRFF
1141: PKYHQMIQWI RYEGHSNDPE FVEMVRQRSI RPTTVGYTAR RAASVRRSAR FHDQIYKDLV
1201: GV