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Protein

Calcium uptake protein 1, mitochondrial

Gene

Micu1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake. Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening. Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi233 – 244121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi423 – 434122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium uptake protein 1, mitochondrial
Alternative name(s):
Calcium-binding atopy-related autoantigen 1 homolog
Gene namesi
Name:Micu1
Synonyms:Cbara1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi735033. Micu1.

Subcellular locationi

  • Mitochondrion inner membrane By similarity; Single-pass membrane protein Sequence analysis
  • Mitochondrion intermembrane space By similarity

  • Note: The topology is subject to debate.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5219HelicalSequence analysisAdd
BLAST
Topological domaini53 – 477425Mitochondrial intermembraneBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence analysisBy similarityAdd
BLAST
Chaini34 – 477444Calcium uptake protein 1, mitochondrialPRO_0000322993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi465 – 465Interchain (with C-413 in MICU2)By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ6P6Q9.
PRIDEiQ6P6Q9.

PTM databases

PhosphoSiteiQ6P6Q9.

Interactioni

Subunit structurei

Homohexamer; in absence of calcium. Forms a homohexamer in absence of calcium and rearranges into a heterodimer in presence of calcium. Heterodimer; disulfide-linked; heterodimerizes with MICU2. The heterodimer formed with MICU2 associates with MCU at low calcium concentration and dissociates from MCU at high calcium level. Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1. Interacts (via polybasic region) with EMRE/SMDT1; the interaction is direct. Interacts (via polybasic region) with MCU (via coiled coil domains); the interaction is direct and precedes formation of the heterodimer with MICU2. Interacts with SLC25A23. Interacts with CHCHD4/MIA40; which introduces the interchain disulfide bond with MICU2.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060514.

Structurei

3D structure databases

ProteinModelPortaliQ6P6Q9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 25536EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 37635EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini410 – 44536EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni101 – 11212Polybasic regionBy similarityAdd
BLAST
Regioni457 – 46711C-helix regionBy similarityAdd
BLAST

Domaini

The C-helix is required for assembling the Ca2+-free homohexamer. It also plays a key role in mitochondrial calcium uptake, probably by mediating interaction with MICU2.By similarity
The EF-hand domains have high affinity for calcium and act as sensors of calcium levels.By similarity

Sequence similaritiesi

Belongs to the MICU1 family. MICU1 subfamily.Curated
Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2643. Eukaryota.
ENOG410ZSC1. LUCA.
HOVERGENiHBG107586.
InParanoidiQ6P6Q9.
PhylomeDBiQ6P6Q9.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P6Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRLNALSAL AELAVGSRWY HGTSQPTQTK RRLMLVAFLG ASAVTASTGL
60 70 80 90 100
LWKKAHAESP PSVNSKKTDA GDKGKSKDTR EVSSHEGSAA DTAAEPYPEE
110 120 130 140 150
KKKKRSGFRD RKVMEYENRI RAYSTPDKIF RYFATLKVIN EPGETEVFMT
160 170 180 190 200
PQDFVRSITP NEKQPEHLGL DQYIIKRFDG KKIAQEREKF ADEGSIFYTL
210 220 230 240 250
GECGLISFSD YIFLTTVLST PQRNFEIAFK MFDLNGDGEV DMEEFEQVQS
260 270 280 290 300
IIRSQTSMGM RHRDRPTTGN TLKSGLCSAL TTYFFGADLK GKLTIKNFLE
310 320 330 340 350
FQRKLQHDVL KLEFERHDPV DGRISERQFG GMLLAYSGVQ SKKLTAMQRQ
360 370 380 390 400
LKKHFKDGKG LTFQEVENFF TFLKNINDVD TALSFYHMAG ASLDKVTMQQ
410 420 430 440 450
VARTVAKVEL SDHVCDVVFA LFDCDGNGEL SNKEFVSIMK QRLMRGLEKP
460 470
KDMGFTRLMQ AMWKCAQETA WDFALPK
Length:477
Mass (Da):54,195
Last modified:July 5, 2004 - v1
Checksum:i0A5078932C71FC99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062075 mRNA. Translation: AAH62075.1.
RefSeqiNP_955444.1. NM_199412.1.
UniGeneiRn.231604.

Genome annotation databases

GeneIDi365567.
KEGGirno:365567.
UCSCiRGD:735033. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062075 mRNA. Translation: AAH62075.1.
RefSeqiNP_955444.1. NM_199412.1.
UniGeneiRn.231604.

3D structure databases

ProteinModelPortaliQ6P6Q9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060514.

PTM databases

PhosphoSiteiQ6P6Q9.

Proteomic databases

PaxDbiQ6P6Q9.
PRIDEiQ6P6Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi365567.
KEGGirno:365567.
UCSCiRGD:735033. rat.

Organism-specific databases

CTDi10367.
RGDi735033. Micu1.

Phylogenomic databases

eggNOGiKOG2643. Eukaryota.
ENOG410ZSC1. LUCA.
HOVERGENiHBG107586.
InParanoidiQ6P6Q9.
PhylomeDBiQ6P6Q9.

Miscellaneous databases

PROiQ6P6Q9.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMICU1_RAT
AccessioniPrimary (citable) accession number: Q6P6Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.