MICU1_MOUSE
ID MICU1_MOUSE Reviewed; 477 AA.
AC Q8VCX5; Q8BK07; Q8BL84; Q8R1W0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Calcium uptake protein 1, mitochondrial;
DE AltName: Full=Calcium-binding atopy-related autoantigen 1 homolog;
DE Flags: Precursor;
GN Name=Micu1; Synonyms=Cbara1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryo, Liver, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Eye, Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=21685888; DOI=10.1038/nature10230;
RA De Stefani D., Raffaello A., Teardo E., Szabo I., Rizzuto R.;
RT "A forty-kilodalton protein of the inner membrane is the mitochondrial
RT calcium uniporter.";
RL Nature 476:336-340(2011).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH MCU AND MICU2, AND TISSUE SPECIFICITY.
RX PubMed=23409044; DOI=10.1371/journal.pone.0055785;
RA Plovanich M., Bogorad R.L., Sancak Y., Kamer K.J., Strittmatter L.,
RA Li A.A., Girgis H.S., Kuchimanchi S., De Groot J., Speciner L., Taneja N.,
RA Oshea J., Koteliansky V., Mootha V.K.;
RT "MICU2, a paralog of MICU1, resides within the mitochondrial uniporter
RT complex to regulate calcium handling.";
RL PLoS ONE 8:E55785-E55785(2013).
RN [6]
RP FUNCTION, INTERACTION WITH MICU2, DISULFIDE BOND, AND CALCIUM-BINDING
RP MUTAGENESIS OF CYS-62; CYS-203; ASP-233; GLU-244; CYS-277; ASP-423; GLU-434
RP AND CYS-465.
RX PubMed=24560927; DOI=10.1016/j.molcel.2014.01.013;
RA Patron M., Checchetto V., Raffaello A., Teardo E., Vecellio Reane D.,
RA Mantoan M., Granatiero V., Szabo I., De Stefani D., Rizzuto R.;
RT "MICU1 and MICU2 finely tune the mitochondrial Ca(2+) uniporter by exerting
RT opposite effects on MCU activity.";
RL Mol. Cell 53:726-737(2014).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=26956930; DOI=10.1038/ncomms10955;
RA Antony A.N., Paillard M., Moffat C., Juskeviciute E., Correnti J.,
RA Bolon B., Rubin E., Csordas G., Seifert E.L., Hoek J.B., Hajnoczky G.;
RT "MICU1 regulation of mitochondrial Ca(2+) uptake dictates survival and
RT tissue regeneration.";
RL Nat. Commun. 7:10955-10955(2016).
CC -!- FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that
CC senses calcium level via its EF-hand domains (PubMed:24560927). MICU1
CC and MICU2 form a disulfide-linked heterodimer that stimulates and
CC inhibits MCU activity, depending on the concentration of calcium
CC (PubMed:24560927). MICU1 acts both as an activator or inhibitor of
CC mitochondrial calcium uptake (By similarity). Acts as a gatekeeper of
CC MCU at low concentration of calcium, preventing channel opening (By
CC similarity). Enhances MCU opening at high calcium concentration,
CC allowing a rapid response of mitochondria to calcium signals generated
CC in the cytoplasm (PubMed:24560927). Regulates glucose-dependent insulin
CC secretion in pancreatic beta-cells by regulating mitochondrial calcium
CC uptake (By similarity). Induces T-helper 1-mediated autoreactivity,
CC which is accompanied by the release of IFNG (By similarity).
CC {ECO:0000250|UniProtKB:Q9BPX6}.
CC -!- SUBUNIT: Homohexamer; in absence of calcium (By similarity). Forms a
CC homohexamer in absence of calcium and rearranges into a heterodimer in
CC presence of calcium (By similarity). Heterodimer; disulfide-linked;
CC heterodimerizes with MICU2 (PubMed:23409044, PubMed:24560927). The
CC heterodimer formed with MICU2 associates with MCU at low calcium
CC concentration and dissociates from MCU at high calcium level (By
CC similarity). Component of the uniplex complex, composed of MCU, MCUB,
CC MICU1, MICU2 and EMRE/SMDT1 (By similarity). Interacts (via polybasic
CC region) with EMRE/SMDT1; the interaction is direct (By similarity).
CC Interacts (via polybasic region) with MCU (via coiled coil domains);
CC the interaction is direct and precedes formation of the heterodimer
CC with MICU2 (PubMed:23409044). Interacts with SLC25A23 (By similarity).
CC Interacts with CHCHD4/MIA40; which introduces the interchain disulfide
CC bond with MICU2 (By similarity). {ECO:0000250|UniProtKB:Q9BPX6,
CC ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:24560927}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BPX6}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q9BPX6}. Note=The topology is subject to debate.
CC {ECO:0000250|UniProtKB:Q9BPX6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VCX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCX5-2; Sequence=VSP_031982;
CC Name=3;
CC IsoId=Q8VCX5-3; Sequence=VSP_031983;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, kidney, liver,
CC brain, lung, fat and spleen. {ECO:0000269|PubMed:21685888,
CC ECO:0000269|PubMed:23409044}.
CC -!- DOMAIN: The EF-hand domains have high affinity for calcium and act as
CC sensors of mitochondrial matrix calcium levels.
CC {ECO:0000269|PubMed:24560927}.
CC -!- DOMAIN: The C-helix is required for assembling the Ca(2+)-free
CC homohexamer. It also plays a key role in mitochondrial calcium uptake,
CC probably by mediating interaction with MICU2.
CC {ECO:0000250|UniProtKB:Q9BPX6}.
CC -!- DOMAIN: The EF-hand domains have high affinity for calcium and act as
CC sensors of calcium levels. {ECO:0000250|UniProtKB:Q9BPX6}.
CC -!- DISRUPTION PHENOTYPE: Lethality during the first hours after birth:
CC embryos are at the expected Mendelian ratio and death takes place only
CC after birth. {ECO:0000269|PubMed:26956930}.
CC -!- SIMILARITY: Belongs to the MICU1 family. MICU1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK046049; BAC32581.1; -; mRNA.
DR EMBL; AK049521; BAC33792.1; -; mRNA.
DR EMBL; AK050113; BAC34073.1; -; mRNA.
DR EMBL; AK052485; BAC35013.1; -; mRNA.
DR EMBL; AK077605; BAC36895.1; -; mRNA.
DR EMBL; BC018320; AAH18320.1; -; mRNA.
DR EMBL; BC023022; AAH23022.1; -; mRNA.
DR EMBL; BC023042; AAH23042.1; -; mRNA.
DR EMBL; BC026566; AAH26566.1; -; mRNA.
DR CCDS; CCDS35909.1; -. [Q8VCX5-1]
DR CCDS; CCDS78817.1; -. [Q8VCX5-2]
DR CCDS; CCDS78818.1; -. [Q8VCX5-3]
DR RefSeq; NP_001278371.1; NM_001291442.1. [Q8VCX5-2]
DR RefSeq; NP_001278372.1; NM_001291443.1. [Q8VCX5-3]
DR RefSeq; NP_659071.1; NM_144822.3. [Q8VCX5-1]
DR AlphaFoldDB; Q8VCX5; -.
DR SMR; Q8VCX5; -.
DR BioGRID; 229685; 14.
DR STRING; 10090.ENSMUSP00000126597; -.
DR iPTMnet; Q8VCX5; -.
DR PhosphoSitePlus; Q8VCX5; -.
DR SwissPalm; Q8VCX5; -.
DR EPD; Q8VCX5; -.
DR MaxQB; Q8VCX5; -.
DR PaxDb; Q8VCX5; -.
DR PeptideAtlas; Q8VCX5; -.
DR PRIDE; Q8VCX5; -.
DR ProteomicsDB; 252560; -. [Q8VCX5-1]
DR ProteomicsDB; 252561; -. [Q8VCX5-2]
DR ProteomicsDB; 252562; -. [Q8VCX5-3]
DR Antibodypedia; 29257; 189 antibodies from 29 providers.
DR DNASU; 216001; -.
DR Ensembl; ENSMUST00000020311; ENSMUSP00000020311; ENSMUSG00000020111. [Q8VCX5-2]
DR Ensembl; ENSMUST00000092508; ENSMUSP00000090166; ENSMUSG00000020111. [Q8VCX5-3]
DR Ensembl; ENSMUST00000165563; ENSMUSP00000126597; ENSMUSG00000020111. [Q8VCX5-1]
DR Ensembl; ENSMUST00000179709; ENSMUSP00000136567; ENSMUSG00000020111. [Q8VCX5-1]
DR GeneID; 216001; -.
DR KEGG; mmu:216001; -.
DR UCSC; uc007fdx.2; mouse. [Q8VCX5-1]
DR UCSC; uc007fdy.2; mouse. [Q8VCX5-3]
DR CTD; 10367; -.
DR MGI; MGI:2384909; Micu1.
DR VEuPathDB; HostDB:ENSMUSG00000020111; -.
DR eggNOG; KOG2643; Eukaryota.
DR GeneTree; ENSGT00950000183079; -.
DR HOGENOM; CLU_027103_3_1_1; -.
DR InParanoid; Q8VCX5; -.
DR OMA; WKAEFRQ; -.
DR OrthoDB; 707988at2759; -.
DR PhylomeDB; Q8VCX5; -.
DR TreeFam; TF313815; -.
DR Reactome; R-MMU-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 216001; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Micu1; mouse.
DR PRO; PR:Q8VCX5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VCX5; protein.
DR Bgee; ENSMUSG00000020111; Expressed in intestinal villus and 245 other tissues.
DR ExpressionAtlas; Q8VCX5; baseline and differential.
DR Genevisible; Q8VCX5; MM.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:1990246; C:uniplex complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; ISS:UniProtKB.
DR GO; GO:0070509; P:calcium ion import; ISS:UniProtKB.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; ISS:UniProtKB.
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; PTHR12294; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium transport; Disulfide bond;
KW Ion transport; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..477
FT /note="Calcium uptake protein 1, mitochondrial"
FT /id="PRO_0000322992"
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..477
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT DOMAIN 220..255
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 356..376
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 410..445
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 57..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..112
FT /note="Polybasic region"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT REGION 457..467
FT /note="C-helix region"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT COMPBIAS 65..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 ECO:0000269|PubMed:24560927"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24560927"
FT DISULFID 465
FT /note="Interchain (with C-410 in MICU2)"
FT /evidence="ECO:0000269|PubMed:24560927"
FT VAR_SEQ 181
FT /note="K -> KEFWQTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031982"
FT VAR_SEQ 181
FT /note="K -> KEFWQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031983"
FT MUTAGEN 62
FT /note="C->A: No effect."
FT MUTAGEN 203
FT /note="C->A: No effect."
FT MUTAGEN 233
FT /note="D->A: Acts as a dominant negative mutant that
FT reduces the mitochondrial Ca(2+) peaks; when associated
FT with A-244; A-423 and A-434."
FT MUTAGEN 244
FT /note="E->A: Acts as a dominant negative mutant that
FT reduces the mitochondrial Ca(2+) peaks; when associated
FT with A-233; A-423 and A-434."
FT MUTAGEN 277
FT /note="C->A: No effect."
FT MUTAGEN 423
FT /note="D->A: Acts as a dominant negative mutant that
FT reduces the mitochondrial Ca(2+) peaks; when associated
FT with A-233; A-244 and A-434."
FT MUTAGEN 434
FT /note="E->A: Acts as a dominant negative mutant that
FT reduces the mitochondrial Ca(2+) peaks; when associated
FT with A-233; A-244 and A-423."
FT MUTAGEN 465
FT /note="C->A: Abolishes interaction with MICU2."
FT CONFLICT 19
FT /note="W -> C (in Ref. 1; BAC36895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 54353 MW; D4088D7540E70E5D CRC64;
MFRLNTLSAL AELAVGSRWY HGASQPTQTK RRLMLVAFLG ASAVTASTGL LWKKAHAESP
PCVNSKKPDT EDKERNKDSG EVSSREGRAA DAAAEPYPED KKKKRSGFRD RKVMEYENRI
RAYSTPDKIF RYFATLKVIN EPGETEVFMT PQDFVRSITP NEKQPEHLGL DQYIIKRFDG
KKIAQEREKF ADEGSIFYSL GECGLISFSD YIFLTTVLST PQRNFEIAFK MFDLNGDGEV
DMEEFEQVQS IIRSQTSMGM RHRDRPTTGN TLKSGLCSAL TTYFFGADLK GKLTIKNFLE
FQRKLQHDVL KLEFERHDPV DGRISERQFG GMLLAYSGVQ SKKLTAMQRQ LKKHFKDGKG
LTFQEVENFF TFLKNINDVD TALSFYHMAG ASLDKVTMQQ VARTVAKVEL SDHVCDVVFA
LFDCDGNGEL SNKEFVSIMK QRLMRGLEKP KDMGFTRLMQ AMWKCAQETA WDFALPK
