MCUB_MOUSE
ID MCUB_MOUSE Reviewed; 345 AA.
AC Q810S1; Q3U4A9; Q9CSE7; Q9D345;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calcium uniporter regulatory subunit MCUb, mitochondrial {ECO:0000305};
DE Short=MCUb {ECO:0000303|PubMed:23900286};
DE AltName: Full=Coiled-coil domain-containing protein 109B {ECO:0000305};
DE Flags: Precursor;
GN Name=Mcub {ECO:0000303|PubMed:23900286, ECO:0000312|MGI:MGI:1914065};
GN Synonyms=Ccdc109b {ECO:0000312|MGI:MGI:1914065};
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
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].
RC TISSUE=Brain;
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 FUNCTION, SUBUNIT, INTERACTION WITH MCU, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23900286; DOI=10.1038/emboj.2013.157;
RA Raffaello A., De Stefani D., Sabbadin D., Teardo E., Merli G., Picard A.,
RA Checchetto V., Moro S., Szabo I., Rizzuto R.;
RT "The mitochondrial calcium uniporter is a multimer that can include a
RT dominant-negative pore-forming subunit.";
RL EMBO J. 32:2362-2376(2013).
CC -!- FUNCTION: Negatively regulates the activity of MCU, the mitochondrial
CC inner membrane calcium uniporter, and thereby modulates calcium uptake
CC into the mitochondrion. Does not form functional calcium channels by
CC itself. Mitochondrial calcium homeostasis plays key roles in cellular
CC physiology and regulates cell bioenergetics, cytoplasmic calcium
CC signals and activation of cell death pathways.
CC {ECO:0000269|PubMed:23900286}.
CC -!- SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB,
CC MICU1, MICU2 and EMRE/SMDT1 (By similarity). Heterooligomer with MCU;
CC this reduces MCU channel activity. Homooligomer.
CC {ECO:0000250|UniProtKB:Q9NWR8, ECO:0000269|PubMed:23900286}.
CC -!- INTERACTION:
CC Q810S1; Q3UMR5: Mcu; NbExp=3; IntAct=EBI-8847756, EBI-776370;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:23900286}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23900286}.
CC -!- TISSUE SPECIFICITY: Detected in lung, brain and heart, and at lower
CC levels in white fat, skeletal muscle and spleen. Detected at very low
CC levels in kidney and liver. {ECO:0000269|PubMed:23900286}.
CC -!- SIMILARITY: Belongs to the MCU (TC 1.A.77) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK013032; BAB28611.1; -; mRNA.
DR EMBL; AK018492; BAB31237.1; ALT_INIT; mRNA.
DR EMBL; AK150724; BAE29802.1; -; mRNA.
DR EMBL; AK150995; BAE30019.1; -; mRNA.
DR EMBL; AK151201; BAE30198.1; -; mRNA.
DR EMBL; AK151915; BAE30794.1; -; mRNA.
DR EMBL; AK154338; BAE32524.1; -; mRNA.
DR EMBL; BC049571; AAH49571.1; -; mRNA.
DR RefSeq; NP_001280573.1; NM_001293644.1.
DR RefSeq; NP_080055.2; NM_025779.3.
DR AlphaFoldDB; Q810S1; -.
DR SMR; Q810S1; -.
DR BioGRID; 211736; 2.
DR IntAct; Q810S1; 2.
DR MINT; Q810S1; -.
DR STRING; 10090.ENSMUSP00000029624; -.
DR PhosphoSitePlus; Q810S1; -.
DR EPD; Q810S1; -.
DR MaxQB; Q810S1; -.
DR PaxDb; Q810S1; -.
DR PeptideAtlas; Q810S1; -.
DR PRIDE; Q810S1; -.
DR ProteomicsDB; 292282; -.
DR Antibodypedia; 62656; 83 antibodies from 18 providers.
DR DNASU; 66815; -.
DR Ensembl; ENSMUST00000029624; ENSMUSP00000029624; ENSMUSG00000027994.
DR GeneID; 66815; -.
DR KEGG; mmu:66815; -.
DR UCSC; uc008rir.2; mouse.
DR CTD; 55013; -.
DR MGI; MGI:1914065; Mcub.
DR VEuPathDB; HostDB:ENSMUSG00000027994; -.
DR eggNOG; KOG2966; Eukaryota.
DR GeneTree; ENSGT00940000158059; -.
DR HOGENOM; CLU_056554_0_1_1; -.
DR InParanoid; Q810S1; -.
DR OMA; HAMELED; -.
DR OrthoDB; 1076768at2759; -.
DR PhylomeDB; Q810S1; -.
DR TreeFam; TF314435; -.
DR Reactome; R-MMU-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 66815; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mcub; mouse.
DR PRO; PR:Q810S1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q810S1; protein.
DR Bgee; ENSMUSG00000027994; Expressed in lumbar dorsal root ganglion and 133 other tissues.
DR ExpressionAtlas; Q810S1; baseline and differential.
DR Genevisible; Q810S1; MM.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990246; C:uniplex complex; ISS:UniProtKB.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IBA:GO_Central.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
DR InterPro; IPR006769; MCU_C.
DR InterPro; IPR039055; MCU_fam.
DR PANTHER; PTHR13462; PTHR13462; 1.
DR Pfam; PF04678; MCU; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium transport; Coiled coil; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..345
FT /note="Calcium uniporter regulatory subunit MCUb,
FT mitochondrial"
FT /id="PRO_0000282981"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 188..221
FT /evidence="ECO:0000255"
FT COILED 306..334
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="L -> R (in Ref. 1; BAE32524)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="Q -> R (in Ref. 1; BAE32524)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> G (in Ref. 1; BAE32524)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="R -> Q (in Ref. 1; BAE32524)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="E -> G (in Ref. 1; BAE32524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39799 MW; 17E51A0B855FC996 CRC64;
MPGALSGRRM LPSGLCLGRW QLLRTIRARG RGDPRELPST PQVLCMKLYG NPKYHQALHY
GTVEPQDEIT VTYKHGLPLV TLTLPSRKER CQFVVKPMLS TVGSFLQDLQ NEDKGIKTAA
IITADGSEIP ASTLMDTLLM TDFKLIINKL RYDIRCHKKE EPSGEHMTEL ENTKSLVHRL
FTILHLEEIQ KRRERHLMAK IDHLQEQLRP LEQVKAAIEA RSEANTSGLL WAGLALLSVQ
GGALAWLTWW VYSWDIMEPV TFFLSFANSI VFFAYFIITR QNYTYSSLRS RQFLQFFHKK
SQRRCFDVEQ YNKLKEDLAE ATESLESVRR SLRLRIQGEE ASEKN
