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1.A.17.5.19
OSCA1.2 of 772 aas and 11 TMSs.  It is a dimer containing eleven TMSs per subunit, similar to other TMEM16 proteins. Jojoa Cruz et al. 2018 located the ion permeation pathway within each subunit by demonstrating that a conserved acidic residue is a determinant of channel conductance. Molecular dynamics simulations revealed membrane interactions, suggesting a role of lipids in gating.  The high resolution structure of this hyperosmolality-gated calcium-permeable channel has been determined (Liu et al. 2018). It contains 11 TMSs and forms a homodimer. The pore-lining residues were clearly identified. Its cytosolic domain contains an RNA recognition motif and two unique long helices. The linker between these two helices forms an anchor in the lipid bilayer and may be essential to osmosensing.

Accession Number:Q9XEA1
Protein Name:Protein OSCA1
Length:772
Molecular Weight:87607.00
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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FASTA formatted sequence
1:	MATLKDIGVS AGINILTAFI FFIIFAFLRL QPFNDRVYFS KWYLRGLRSS PASGGGFAGR 
61:	FVNLELRSYL KFLHWMPEAL KMPERELIDH AGLDSVVYLR IYWLGLKIFA PIAMLAWAVL 
121:	VPVNWTNNEL ELAKHFKNVT SSDIDKLTIS NIPEGSNRFW AHIIMAYAFT IWTCYMLMKE 
181:	YETVANMRLQ FLASEGRRPD QFTVLVRNVP PDPDETVSEL VEHFFLVNHP DNYLTHQVVC 
241:	NANKLADLVS KKTKLQNWLD YYQLKYTRNN SQIRPITKLG CLGLCGQKVD AIEHYIAEVD 
301:	KTSKEIAEER ENVVNDQKSV MPASFVSFKT RWAAAVCAQT TQTRNPTEWL TEWAAEPRDI 
361:	YWPNLAIPYV SLTVRRLVMN VAFFFLTFFF IIPIAFVQSL ATIEGIEKVA PFLKVIIEKD 
421:	FIKSLIQGLL AGIALKLFLI FLPAILMTMS KFEGFTSVSF LERRSASRYY IFNLVNVFLG 
481:	SVIAGAAFEQ LNSFLNQSPN QIPKTIGMAI PMKATFFITY IMVDGWAGVA GEILMLKPLI 
541:	IYHLKNAFLV KTEKDREEAM NPGSIGFNTG EPQIQLYFLL GLVYAPVTPM LLPFILVFFA 
601:	LAYVVYRHQI INVYNQEYES AAAFWPDVHG RVITALIISQ LLLMGLLGTK HAASAAPFLI 
661:	ALPVITIGFH RFCKGRFEPA FVRYPLQEAM MKDTLERARE PNLNLKGYLQ DAYIHPVFKG 
721:	GDNDDDGDMI GKLENEVIIV PTKRQSRRNT PAPSRISGES SPSLAVINGK EV