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1.A.87.1.1
Plant Ca2+ channel protein, Mid1 complementary activity 1, MCA1 (Iida et al. 2013).  MCA1 and MCA2 each forms a homotetramer and exhibit Ca2+-permeable mechanosensitive channel activity.  Both are single-pass type I transmembrane proteins with their N-termini located extracellularly and their C-termini located intracellularly. An EF hand-like motif, coiled-coil motif, and Plac8 motif may all be in the cytoplasm, suggesting that the activities of both channels can be regulated by intracellular Ca2+ and protein interactions (Kamano et al. 2015). However, hydropathy plots suggest that the Plac8 domain may be transmembrane with 3 TMSs.  mca1 but not mca2 mutants show defects in root entry into hard agar, whereas mca2 but not mca1 mutants are defective in Ca2+ uptake in A. thaliana roots (Hamilton et al. 2015). Root growth reduction in response to mechanical stress involves MCA1 tgether with WDL5 (Q94C48) subject to ethylene-mediated regulation) and the co-receptor BAK1 (Q94F62) (Okamoto et al. 2021).  

Accession Number:Q8L7E9
Protein Name:Protein MID1-COMPLEMENTING ACTIVITY 1
Length:421
Molecular Weight:48037.00
Species:Arabidopsis thaliana (Mouse-ear cress) [3702]
Location1 / Topology2 / Orientation3: Cell membrane1 / Single-pass membrane protein2
Substrate calcium(2+)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSHSWDGLGE IASVAQLTGL DAVKLIGLIV KAANTAWMHK KNCRQFAQHL KLIGNLLEQL 
61:	KISEMKKYPE TREPLEGLED ALRRSYLLVN SCRDRSYLYL LAMGWNIVYQ FRKHQDEIDR 
121:	FLKIIPLITL VDNARIRERF EYIDRDQREY TLDEEDRHVQ DVILKQESTR EAASVLKKTL 
181:	SCSYPNLRFC EALKTENEKL QIELQRSQEH YDVAQCEVIQ RLIGVTQAAA AVEPDSEKEL 
241:	TKKASKKSER SSSMKTEYSY DEDSPKKSST RAASRSTSNV SSGHDLLSRR ASQAQHHEEW 
301:	HTDLLACCSE PSLCFKTFFF PCGTLAKIAT AASNRHISSA EACNELMAYS LILSCCCYTC 
361:	CVRRKLRKTL NITGGFIDDF LSHVMCCCCA LVQELREVEI RGAYGTEKTK ISPPSSQFME 
421:	H