ID MICU_ARATH Reviewed; 498 AA.
AC Q9SZ45; A8MRL1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Calcium uptake protein, mitochondrial {ECO:0000250|UniProtKB:Q9BPX6};
DE AltName: Full=Mitochondrial calcium uniporter {ECO:0000303|PubMed:26530087};
DE Flags: Precursor;
GN Name=MICU {ECO:0000303|PubMed:26530087};
GN OrderedLocusNames=At4g32060 {ECO:0000312|Araport:AT4G32060};
GN ORFNames=F10N7.140 {ECO:0000312|EMBL:CAA16584.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26530087; DOI=10.1105/tpc.15.00509;
RA Wagner S., Behera S., De Bortoli S., Logan D.C., Fuchs P., Carraretto L.,
RA Teardo E., Cendron L., Nietzel T., Fuessl M., Doccula F.G., Navazio L.,
RA Fricker M.D., Van Aken O., Finkemeier I., Meyer A.J., Szabo I., Costa A.,
RA Schwarzlaender M.;
RT "The EF-hand Ca2+ binding protein MICU choreographs mitochondrial Ca2+
RT dynamics in Arabidopsis.";
RL Plant Cell 27:3190-3212(2015).
CC -!- FUNCTION: Calcium-binding protein maintaining matrix calcium levels at
CC low concentration. Regulates mitochondrial calcium dynamics in planta
CC by restricting influx. {ECO:0000269|PubMed:26530087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:26530087}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:26530087}. Note=Located at the inner mitochondrial
CC membrane and/or in the intermembrane space.
CC {ECO:0000269|PubMed:26530087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SZ45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZ45-2; Sequence=VSP_058723, VSP_058724;
CC -!- TISSUE SPECIFICITY: Expressed in both green and non-green tissues,
CC including roots, shoots, floral buds and pollen.
CC {ECO:0000269|PubMed:26530087}.
CC -!- DOMAIN: The EF-hand domains have high affinity for calcium.
CC {ECO:0000269|PubMed:26530087}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:26530087}.
CC -!- SIMILARITY: Belongs to the MICU1 family. MICU1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL021636; CAA16584.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79924.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85999.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86000.1; -; Genomic_DNA.
DR EMBL; AY072163; AAL59985.1; -; mRNA.
DR EMBL; AY122982; AAM67515.1; -; mRNA.
DR PIR; T04640; T04640.
DR RefSeq; NP_001078476.1; NM_001085007.1. [Q9SZ45-2]
DR RefSeq; NP_194934.1; NM_119358.4. [Q9SZ45-1]
DR AlphaFoldDB; Q9SZ45; -.
DR SMR; Q9SZ45; -.
DR STRING; 3702.Q9SZ45; -.
DR PaxDb; 3702-AT4G32060-1; -.
DR ProteomicsDB; 250931; -. [Q9SZ45-1]
DR EnsemblPlants; AT4G32060.1; AT4G32060.1; AT4G32060. [Q9SZ45-1]
DR EnsemblPlants; AT4G32060.2; AT4G32060.2; AT4G32060. [Q9SZ45-2]
DR GeneID; 829337; -.
DR Gramene; AT4G32060.1; AT4G32060.1; AT4G32060. [Q9SZ45-1]
DR Gramene; AT4G32060.2; AT4G32060.2; AT4G32060. [Q9SZ45-2]
DR KEGG; ath:AT4G32060; -.
DR Araport; AT4G32060; -.
DR TAIR; AT4G32060; MICU.
DR eggNOG; KOG2643; Eukaryota.
DR HOGENOM; CLU_027103_2_0_1; -.
DR InParanoid; Q9SZ45; -.
DR OMA; GGPMYMT; -.
DR OrthoDB; 1020411at2759; -.
DR PhylomeDB; Q9SZ45; -.
DR PRO; PR:Q9SZ45; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ45; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0006816; P:calcium ion transport; IDA:TAIR.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IEA:InterPro.
DR GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
DR CDD; cd15900; EFh_MICU; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039800; MICU1/2/3.
DR PANTHER; PTHR12294:SF23; CALCIUM UPTAKE PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12294; EF HAND DOMAIN FAMILY A1,A2-RELATED; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium transport; Ion transport; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..498
FT /note="Calcium uptake protein, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438705"
FT DOMAIN 216..241
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 243..278
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 329..364
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 437..472
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 432..454
FT /note="VCGITLSDNVIEIAFHVFDSNQD -> REGRGTANCKRIVSVLLRWMEGF
FT (in isoform 2)"
FT /id="VSP_058723"
FT VAR_SEQ 455..498
FT /note="Missing (in isoform 2)"
FT /id="VSP_058724"
SQ SEQUENCE 498 AA; 55415 MW; D6B1CDA90380A16C CRC64;
MPALSHYRSV SSLPSVDRSF LLIQRLRIHG SSSSFPESSP SASILSGADP LKCTVSGGSL
AKWITGISAG SALGFLYWSS GSSDSISGLF GGSNLLSFAD SSTPSVCGVK VGDLKPRSFI
PKLSLPGYSS GFIFGDAYRR KIFFNYEKRL RLQSPPEKVF EYFASVRTDK GEILMKPADL
MRAIVPVFPP SESHLVREGY LTGERNPGEL RCSPSEFFML FDVDNDGLIS FKEYIFFVTL
LSIPESSFAV AFKMFDTDNN GEIDKEEFKT VMSLMRSQHR QGVGHRDGLR TGLHMTGSVE
DGGLVEYFFG KDGSQKLKHD KFTKFMKDLT EEMLRLEFAH YDYKRRGSIS AKDFALSMVA
AADASHLSKL LDRVESLSEH PHLRDMRISL KEFKQFDELR SKLGPFSLAL FAYGKANGLL
TMKDFKRAAS QVCGITLSDN VIEIAFHVFD SNQDGNLSVD EFLRVLHRRE RDVAQPIAKG
LSRYFSDGWK GSKNCSSS
//
