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3.A.1.105.5
AbcG homologue, Snustorr, sioform A, Snu, of 808 aas and 6 TMSs in a 1 + 5 TMS arrangement at the C-terminal part of the protein.  The N-terminal domain is the ATPase domain.  The protein therefore has a C-M domain arrangement.  Lipids in extracellular matrices (ECM) contribute to barrier function and stability of epithelial tissues such as the pulmonary alveoli and the skin. In insects, skin waterproofness depends on the outermost layer of the extracellular cuticle envelope that contains cuticulin, an unidentified water-repellent complex molecule composed of proteins, lipids and catecholamines. Based on live-imaging analyses of fruit fly larvae, Zuber et al. 2018 found that initially, envelope units are assembled within putative vesicles harbouring the ABC transporter Snu and the extracellular protein Snsl. In a second step, the content of these vesicles is distributed to cuticular lipid-transporting nanotubes named pore canals and to the cuticle surface, dependent on Snu function. The surface of snu and snsl mutant larvae is depleted of lipids and cuticulin. Consequently, these animals suffer uncontrolled water loss and penetration of xenobiotics. The data allude to a two-step model of envelope (i.e. barrier) formation. The proposed mechanism in principle parallels the events occurring during differentiation of the lipid-based ECM by keratinocytes in the vertebrate skin, suggesting establishment of analogous mechanisms of skin barrier formation in vertebrates and invertebrates (Zuber et al. 2018).

Accession Number:Q9VAU1
Protein Name:Snustorr, isoform A
Length:808
Molecular Weight:89334.00
Species:Drosophila melanogaster (Fruit fly) [7227]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate lipid

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FASTA formatted sequence
1:	MAPKKEATLS QQQTQQPIMD LERIKRHFSW SDPSAIISTD SAMAATNNDG GTQPNAVAAW 
61:	GAPANGPRNT QAAVSVRHAF KAYGKKKNAN QVLNNLNMTV PKGTIYGLLG ASGCGKTTLL 
121:	SCIVGRRYMD AGEIFVLGGK PGTRGSGVPG KRVGYMPQEI ALYGEFSIQE TMMYFGWIFG 
181:	MDTKEILERL QFLLNFLDLP SEKRLVKNLS GGQQRRVSFA VALMHDPELL ILDEPTVGVD 
241:	PLLRQSIWNH LVHITKAGQK TVIITTHYIE EARQAHTIGL MRSGHLLAEE SPSVLLSIYK 
301:	CISLEEVFLK LSRIQSQKGD VTHVNFSNNI SLHAMAFGSK MDKPSSSQEG GVVGLNFHQS 
361:	KEVLINDSNG SIYTLNQEPY SPPPSRRNNN PNDEESCQDC YSNLCKITSK GKIRALLTKN 
421:	MLRMWRNVGV MLFIFALPVM QVILFCLAIG RDPQGLNLAI VNGEMNDTVR ENCYWEDGCH 
481:	FKNLGCRYLS HLNTSVVKTY YEDLDDAKEA VRKGTAWGAV YISENFTDAF IARANLGRDS 
541:	DDETIDSSEV KVWLDMSNQQ IGVMLNRDIQ LAFRDFAMGL LGQCGSNPKL GDVPIQFRDP 
601:	IYGTMNPSFT DFVAPGVILT IVFFLAVALT SSALIIERTE GLLDRSWVAG VSPFEILFSH 
661:	VITQFVVMCG QTTLVLIFML VVFGVTNNGD LFWVIVLTLL QGMCGMCFGF LISSVCELER 
721:	NAIQLALGSF YPTLLLSGVI WPIEGMPVVL RYISLCLPLT LATSSLRSIL TRGWAILESD 
781:	VYIGYVSTLS WIVGFLVLTL LVLRAKRG