MCAC1_ARATH
ID MCAC1_ARATH Reviewed; 421 AA.
AC Q8L7E9; O65629; Q9ASR5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein MID1-COMPLEMENTING ACTIVITY 1;
GN Name=MCA1; OrderedLocusNames=At4g35920; ORFNames=T19K4.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17360695; DOI=10.1073/pnas.0607703104;
RA Nakagawa Y., Katagiri T., Shinozaki K., Qi Z., Tatsumi H., Furuichi T.,
RA Kishigami A., Sokabe M., Kojima I., Sato S., Kato T., Tabata S., Iida K.,
RA Terashima A., Nakano M., Ikeda M., Yamanaka T., Iida H.;
RT "Arabidopsis plasma membrane protein crucial for Ca2+ influx and touch
RT sensing in roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3639-3644(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20097794; DOI=10.1104/pp.109.147371;
RA Yamanaka T., Nakagawa Y., Mori K., Nakano M., Imamura T., Kataoka H.,
RA Terashima A., Iida K., Kojima I., Katagiri T., Shinozaki K., Iida H.;
RT "MCA1 and MCA2 that mediate Ca2+ uptake have distinct and overlapping roles
RT in Arabidopsis.";
RL Plant Physiol. 152:1284-1296(2010).
CC -!- FUNCTION: Calcium-permeable stretch-activated channel component.
CC Involved in mechano-stimulated calcium uptake mechanism and in
CC mechanosensing in the primary root. {ECO:0000269|PubMed:17360695,
CC ECO:0000269|PubMed:20097794}.
CC -!- ACTIVITY REGULATION: Inhibited by GdCl(3), but not by verapamil.
CC {ECO:0000269|PubMed:17360695}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360695};
CC Single-pass membrane protein {ECO:0000269|PubMed:17360695}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L7E9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L7E9-2; Sequence=VSP_040964;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Expressed in vascular tissues of cotyledons, leaves and
CC primary root, in the promeristem and adjacent elongation zone of the
CC primary root and in the shoot apical meristem. Detected in the stele
CC and endodermis, but not in the cortex, epidermis or root cap, including
CC the columella. Not expressed in root hairs or in mesophyll cells of
CC leaves and cotyledons. {ECO:0000269|PubMed:17360695,
CC ECO:0000269|PubMed:20097794}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions; due to partial redundancy with MCA2. The roots are unable
CC to sense a change in the hardness of the growth medium. Mca1 and mca2
CC double mutant shows a strong growth defect.
CC {ECO:0000269|PubMed:17360695, ECO:0000269|PubMed:20097794}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18486.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA21478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB196960; BAF46389.1; -; mRNA.
DR EMBL; AL022373; CAA18486.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031986; CAA21478.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81501.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86589.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86590.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86591.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67921.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67922.1; -; Genomic_DNA.
DR EMBL; AY136293; AAM96959.1; -; mRNA.
DR EMBL; BT003430; AAO30093.1; -; mRNA.
DR EMBL; AF367322; AAK32909.1; -; mRNA.
DR EMBL; AY133604; AAM91434.1; -; mRNA.
DR EMBL; AK316845; BAH19557.1; -; mRNA.
DR PIR; T04702; T04702.
DR RefSeq; NP_001329715.1; NM_001342380.1. [Q8L7E9-1]
DR RefSeq; NP_001329716.1; NM_001342381.1. [Q8L7E9-1]
DR RefSeq; NP_195317.2; NM_119759.4. [Q8L7E9-1]
DR RefSeq; NP_849503.1; NM_179172.3. [Q8L7E9-1]
DR RefSeq; NP_849504.2; NM_179173.4. [Q8L7E9-1]
DR AlphaFoldDB; Q8L7E9; -.
DR SMR; Q8L7E9; -.
DR STRING; 3702.AT4G35920.1; -.
DR TCDB; 1.A.87.1.1; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; Q8L7E9; -.
DR PaxDb; Q8L7E9; -.
DR PRIDE; Q8L7E9; -.
DR ProteomicsDB; 238820; -. [Q8L7E9-1]
DR EnsemblPlants; AT4G35920.1; AT4G35920.1; AT4G35920. [Q8L7E9-1]
DR EnsemblPlants; AT4G35920.2; AT4G35920.2; AT4G35920. [Q8L7E9-1]
DR EnsemblPlants; AT4G35920.3; AT4G35920.3; AT4G35920. [Q8L7E9-1]
DR EnsemblPlants; AT4G35920.4; AT4G35920.4; AT4G35920. [Q8L7E9-1]
DR EnsemblPlants; AT4G35920.5; AT4G35920.5; AT4G35920. [Q8L7E9-1]
DR GeneID; 829747; -.
DR Gramene; AT4G35920.1; AT4G35920.1; AT4G35920. [Q8L7E9-1]
DR Gramene; AT4G35920.2; AT4G35920.2; AT4G35920. [Q8L7E9-1]
DR Gramene; AT4G35920.3; AT4G35920.3; AT4G35920. [Q8L7E9-1]
DR Gramene; AT4G35920.4; AT4G35920.4; AT4G35920. [Q8L7E9-1]
DR Gramene; AT4G35920.5; AT4G35920.5; AT4G35920. [Q8L7E9-1]
DR KEGG; ath:AT4G35920; -.
DR Araport; AT4G35920; -.
DR TAIR; locus:2125369; AT4G35920.
DR eggNOG; ENOG502QQIG; Eukaryota.
DR HOGENOM; CLU_738527_0_0_1; -.
DR InParanoid; Q8L7E9; -.
DR OMA; HEEWNTD; -.
DR PhylomeDB; Q8L7E9; -.
DR PRO; PR:Q8L7E9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7E9; baseline and differential.
DR Genevisible; Q8L7E9; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:TAIR.
DR GO; GO:0005262; F:calcium channel activity; IDA:TAIR.
DR GO; GO:0006816; P:calcium ion transport; IMP:TAIR.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:TAIR.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
DR Gene3D; 1.20.930.20; -; 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR045766; MCAfunc.
DR InterPro; IPR006461; PLAC_motif_containing.
DR Pfam; PF19584; MCAfunc; 1.
DR Pfam; PF04749; PLAC8; 1.
DR TIGRFAMs; TIGR01571; A_thal_Cys_rich; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Protein MID1-COMPLEMENTING ACTIVITY 1"
FT /id="PRO_0000407741"
FT TRANSMEM 346..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 233..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..218
FT /evidence="ECO:0000255"
FT COMPBIAS 235..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 405..421
FT /note="GTEKTKISPPSSQFMEH -> DLCRYGEDENKPAFVAVHGTLKSSIIQKVNK
FT NNDLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040964"
SQ SEQUENCE 421 AA; 48037 MW; F03E0ADF1786EF9F CRC64;
MSHSWDGLGE IASVAQLTGL DAVKLIGLIV KAANTAWMHK KNCRQFAQHL KLIGNLLEQL
KISEMKKYPE TREPLEGLED ALRRSYLLVN SCRDRSYLYL LAMGWNIVYQ FRKHQDEIDR
FLKIIPLITL VDNARIRERF EYIDRDQREY TLDEEDRHVQ DVILKQESTR EAASVLKKTL
SCSYPNLRFC EALKTENEKL QIELQRSQEH YDVAQCEVIQ RLIGVTQAAA AVEPDSEKEL
TKKASKKSER SSSMKTEYSY DEDSPKKSST RAASRSTSNV SSGHDLLSRR ASQAQHHEEW
HTDLLACCSE PSLCFKTFFF PCGTLAKIAT AASNRHISSA EACNELMAYS LILSCCCYTC
CVRRKLRKTL NITGGFIDDF LSHVMCCCCA LVQELREVEI RGAYGTEKTK ISPPSSQFME
H
