MCUR1_MOUSE
ID MCUR1_MOUSE Reviewed; 340 AA.
AC Q9CXD6; Q14DH8; Q3V3D3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mitochondrial calcium uniporter regulator 1 {ECO:0000250|UniProtKB:Q96AQ8};
DE Short=MCU regulator 1 {ECO:0000250|UniProtKB:Q96AQ8};
DE AltName: Full=Coiled-coil domain-containing protein 90A, mitochondrial {ECO:0000305};
GN Name=Mcur1 {ECO:0000250|UniProtKB:Q96AQ8, ECO:0000312|MGI:MGI:1923387};
GN Synonyms=Ccdc90a {ECO:0000312|MGI:MGI:1923387};
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=Head, and Thymus;
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] (ISOFORM 3).
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, Heart, Kidney, Liver, Lung, and Spleen;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=27184846; DOI=10.1016/j.celrep.2016.04.050;
RA Tomar D., Dong Z., Shanmughapriya S., Koch D.A., Thomas T., Hoffman N.E.,
RA Timbalia S.A., Goldman S.J., Breves S.L., Corbally D.P., Nemani N.,
RA Fairweather J.P., Cutri A.R., Zhang X., Song J., Jana F., Huang J.,
RA Barrero C., Rabinowitz J.E., Luongo T.S., Schumacher S.M., Rockman M.E.,
RA Dietrich A., Merali S., Caplan J., Stathopulos P., Ahima R.S., Cheung J.Y.,
RA Houser S.R., Koch W.J., Patel V., Gohil V.M., Elrod J.W., Rajan S.,
RA Madesh M.;
RT "MCUR1 is a scaffold factor for the MCU complex function and promotes
RT mitochondrial bioenergetics.";
RL Cell Rep. 15:1673-1685(2016).
CC -!- FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU)
CC required for calcium entry into mitochondrion. Plays a direct role in
CC uniporter-mediated calcium uptake via a direct interaction with MCU.
CC Probably involved in the assembly of the membrane components of the
CC uniporter complex (uniplex). {ECO:0000250|UniProtKB:Q96AQ8}.
CC -!- SUBUNIT: Interacts (via coiled coil regions) with MCU; the interaction
CC is direct. Interacts with SMDT1/EMRE; the interaction is direct.
CC Interacts with PPIF. {ECO:0000250|UniProtKB:Q96AQ8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96AQ8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96AQ8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CXD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CXD6-2; Sequence=VSP_027001, VSP_027002;
CC Name=3;
CC IsoId=Q9CXD6-3; Sequence=VSP_027000;
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice lacking Mcur1 in
CC cardiomyocytes and endothelial cells are viable and are born at the
CC expected Mendelian. They however show impaired mitochondrial calcium
CC uptake and mitochondrial calcium uniporter (MCU) current.
CC {ECO:0000269|PubMed:27184846}.
CC -!- SIMILARITY: Belongs to the CCDC90 family. {ECO:0000305}.
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DR EMBL; AK018089; BAB31065.1; -; mRNA.
DR EMBL; AK041849; BAE20607.1; -; mRNA.
DR EMBL; BC113195; AAI13196.1; -; mRNA.
DR CCDS; CCDS36645.1; -. [Q9CXD6-1]
DR RefSeq; NP_001074528.1; NM_001081059.3. [Q9CXD6-1]
DR AlphaFoldDB; Q9CXD6; -.
DR SMR; Q9CXD6; -.
DR BioGRID; 217986; 2.
DR STRING; 10090.ENSMUSP00000021800; -.
DR iPTMnet; Q9CXD6; -.
DR PhosphoSitePlus; Q9CXD6; -.
DR EPD; Q9CXD6; -.
DR jPOST; Q9CXD6; -.
DR MaxQB; Q9CXD6; -.
DR PaxDb; Q9CXD6; -.
DR PeptideAtlas; Q9CXD6; -.
DR PRIDE; Q9CXD6; -.
DR ProteomicsDB; 292283; -. [Q9CXD6-1]
DR ProteomicsDB; 292284; -. [Q9CXD6-2]
DR ProteomicsDB; 292285; -. [Q9CXD6-3]
DR Antibodypedia; 25007; 77 antibodies from 20 providers.
DR Ensembl; ENSMUST00000021800; ENSMUSP00000021800; ENSMUSG00000021371. [Q9CXD6-1]
DR GeneID; 76137; -.
DR KEGG; mmu:76137; -.
DR UCSC; uc007qgf.2; mouse. [Q9CXD6-1]
DR UCSC; uc007qgg.2; mouse. [Q9CXD6-2]
DR CTD; 63933; -.
DR MGI; MGI:1923387; Mcur1.
DR VEuPathDB; HostDB:ENSMUSG00000021371; -.
DR eggNOG; KOG3156; Eukaryota.
DR GeneTree; ENSGT00940000158957; -.
DR HOGENOM; CLU_791208_0_0_1; -.
DR InParanoid; Q9CXD6; -.
DR OMA; MSHITAV; -.
DR OrthoDB; 1252164at2759; -.
DR PhylomeDB; Q9CXD6; -.
DR TreeFam; TF331442; -.
DR BioGRID-ORCS; 76137; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Mcur1; mouse.
DR PRO; PR:Q9CXD6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CXD6; protein.
DR Bgee; ENSMUSG00000021371; Expressed in brown adipose tissue and 214 other tissues.
DR Genevisible; Q9CXD6; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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: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; IPR024461; CCDC90-like.
DR InterPro; IPR012439; MCUR1.
DR PANTHER; PTHR14360; PTHR14360; 1.
DR PANTHER; PTHR14360:SF11; PTHR14360:SF11; 1.
DR Pfam; PF07798; DUF1640; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Calcium transport; Coiled coil;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..340
FT /note="Mitochondrial calcium uniporter regulator 1"
FT /id="PRO_0000295693"
FT TOPO_DOM 1..54
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ8"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..316
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ8"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ8"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..291
FT /evidence="ECO:0000255"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..180
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027000"
FT VAR_SEQ 267..286
FT /note="YSLNEKKMLELRTEIVSLHA -> VCSFIKSKSLIYFFLDWNAC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027001"
FT VAR_SEQ 287..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027002"
FT CONFLICT 52
FT /note="A -> G (in Ref. 1; BAE20607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37849 MW; F9B6B7A8A0CD92DA CRC64;
MDSGSVAAER PRRTPSRQRL PSSGCGVPAR PGVSTLPGGR SWLRPRGRAA RASPLLFLLL
VPSPRLAATA TATAPRRTLA ERSRPGLVLP AAALGAGRNA LGRLRLGARR VAALASSRRE
LSLSAKCHQL EHRKENLPLS VSRQLYFDTH ALVCLLEANG FTIQQAEIIV SALVKITETN
MNIIYKDMVS KMQQEIALQQ VLSKIANVKK DMVILEKSEF SALRAENEKI KLELHQLKQQ
VMDEVTKVRT DTKLNFNLEK SRVKELYSLN EKKMLELRTE IVSLHAQQDR ALTQTDRKIE
TEVAGLKTML EAHKLDTIKY LAGSVFTCLT VALGFYRLWI
