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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.

Accession Number:Q9LI83
Protein Name:Phospholipid-transporting ATPase 10
Length:1202
Molecular Weight:136279.00
Species:Arabidopsis thaliana (Mouse-ear cress) [3702]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
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