MICU1_XENTR
ID MICU1_XENTR Reviewed; 473 AA.
AC B1H2N3; Q28CG4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 69.
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; ORFNames=TGas034p18.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-473 (ISOFORM 1).
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that
CC senses calcium level via its EF-hand domains. micu1 and micu2 form a
CC disulfide-linked heterodimer that stimulates and inhibits mcu activity,
CC depending on the concentration of calcium. Micu1 acts both as an
CC activator or inhibitor of mitochondrial calcium uptake. Acts as a
CC gatekeeper of mcu at low concentration of calcium, preventing channel
CC opening. Enhances mcu opening at high calcium concentration, allowing a
CC rapid response of mitochondria to calcium signals generated in the
CC cytoplasm. {ECO:0000250|UniProtKB:Q9BPX6}.
CC -!- SUBUNIT: Homohexamer; in absence of calcium. Forms a homohexamer in
CC absence of calcium and rearranges into a heterodimer in presence of
CC calcium. Heterodimer; disulfide-linked; heterodimerizes with MICU2. The
CC heterodimer formed with MICU2 associates with MCU at low calcium
CC concentration and dissociates from MCU at high calcium level. Component
CC of the uniplex complex. {ECO:0000250|UniProtKB:Q9BPX6}.
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=2;
CC Name=1;
CC IsoId=B1H2N3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1H2N3-2; Sequence=VSP_039908;
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 -!- SIMILARITY: Belongs to the MICU1 family. MICU1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI61065.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC161065; AAI61065.1; ALT_FRAME; mRNA.
DR EMBL; CR926402; CAJ83562.1; -; mRNA.
DR RefSeq; NP_001106411.2; NM_001112940.2. [B1H2N3-1]
DR RefSeq; XP_017950727.1; XM_018095238.1. [B1H2N3-1]
DR AlphaFoldDB; B1H2N3; -.
DR SMR; B1H2N3; -.
DR STRING; 8364.ENSXETP00000016304; -.
DR DNASU; 100127574; -.
DR Ensembl; ENSXETT00000016304; ENSXETP00000016304; ENSXETG00000007480.
DR GeneID; 100127574; -.
DR KEGG; xtr:100127574; -.
DR CTD; 10367; -.
DR Xenbase; XB-GENE-953464; micu1.
DR eggNOG; KOG2643; Eukaryota.
DR InParanoid; B1H2N3; -.
DR OrthoDB; 707988at2759; -.
DR Reactome; R-XTR-8949215; Mitochondrial calcium ion transport.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007480; Expressed in skeletal muscle tissue and 13 other tissues.
DR ExpressionAtlas; B1H2N3; differential.
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:1990246; C:uniplex complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IBA:GO_Central.
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 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; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript 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:0000250|UniProtKB:Q9BPX6, ECO:0000255"
FT CHAIN 34..473
FT /note="Calcium uptake protein 1, mitochondrial"
FT /id="PRO_0000399809"
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..473
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT DOMAIN 215..250
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 405..440
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 61..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..107
FT /note="Polybasic region"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT REGION 452..462
FT /note="C-helix region"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 DISULFID 460
FT /note="Interchain (with C-413 in micu2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BPX6"
FT VAR_SEQ 176
FT /note="K -> KTE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039908"
SQ SEQUENCE 473 AA; 54249 MW; 254CA9E9EFF77201 CRC64;
MFRLRFIPAV AGLAAVSRRY HGVANHARSR RRLMMAAFVG ATAVSASAGL LWKRANAEAQ
SSVKHSMREE TSEKEKEDAD QAVESSDEDQ PQEGKKKKAR VGFRDRKVME YENRIRAYST
PDKIFRYFAT LKVIHESGES EVFMTPQDFV RSITPNEKQP ENLGLDQFII KRYDGKKISQ
EREKFADEDS IFYSLGECGL ISFSDYIFLT TVLSTPQRNF EIAFKMFDLN GDGEVDMEEF
EQVQSIIRSQ TSMGMRHRDR STTGNTLKTG FSSALTTYFF GADLKGKLTI KNFLEFQRKL
QHDVLKLEFE RHDPVDGHIT ERQFGSMLLA YSGVQSKKLT HMLKQLKKRF KDAEGLTFEE
VENFFTFLKN INDVDTALSF YHMAGASLDK VTMQQVARTV AKVELSDHVC DVVFALFDCD
GNGELSNKEF IAIMKQRLMR GLEKPKDMGF TRLMRAMWKC AQETAWDFAM PKQ
