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).
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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+) |
---|
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