MCU_HUMAN
ID MCU_HUMAN Reviewed; 351 AA.
AC Q8NE86; B2RDF3; B3KXV7; Q96FL3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Calcium uniporter protein, mitochondrial {ECO:0000303|PubMed:21685886};
DE Short=HsMCU {ECO:0000303|PubMed:27135929};
DE AltName: Full=Coiled-coil domain-containing protein 109A {ECO:0000305};
DE Flags: Precursor;
GN Name=MCU {ECO:0000303|PubMed:21685886, ECO:0000312|HGNC:HGNC:23526};
GN Synonyms=C10orf42 {ECO:0000312|HGNC:HGNC:23526},
GN CCDC109A {ECO:0000312|HGNC:HGNC:23526};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION, MUTAGENESIS OF 261-ASP--GLU-264, SUBCELLULAR LOCATION, AND TISSUE
RP 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 [7]
RP FUNCTION, OLIGOMERIZATION, SUBUNIT, INTERACTION WITH MICU1, MUTAGENESIS OF
RP GLU-257; SER-259 AND 261-ASP--GLU-264, AND SUBCELLULAR LOCATION.
RX PubMed=21685886; DOI=10.1038/nature10234;
RA Baughman J.M., Perocchi F., Girgis H.S., Plovanich M., Belcher-Timme C.A.,
RA Sancak Y., Bao X.R., Strittmatter L., Goldberger O., Bogorad R.L.,
RA Koteliansky V., Mootha V.K.;
RT "Integrative genomics identifies MCU as an essential component of the
RT mitochondrial calcium uniporter.";
RL Nature 476:341-345(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH MICU1.
RX PubMed=23101630; DOI=10.1016/j.cell.2012.10.011;
RA Mallilankaraman K., Doonan P., Cardenas C., Chandramoorthy H.C., Muller M.,
RA Miller R., Hoffman N.E., Gandhirajan R.K., Molgo J., Birnbaum M.J.,
RA Rothberg B.S., Mak D.O., Foskett J.K., Madesh M.;
RT "MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+)
RT uptake that regulates cell survival.";
RL Cell 151:630-644(2012).
RN [9]
RP FUNCTION.
RX PubMed=22904319; DOI=10.1074/jbc.m112.392084;
RA Alam M.R., Groschner L.N., Parichatikanond W., Kuo L., Bondarenko A.I.,
RA Rost R., Waldeck-Weiermair M., Malli R., Graier W.F.;
RT "Mitochondrial Ca2+ uptake 1 (MICU1) and mitochondrial ca2+ uniporter (MCU)
RT contribute to metabolism-secretion coupling in clonal pancreatic beta-
RT cells.";
RL J. Biol. Chem. 287:34445-34454(2012).
RN [10]
RP PHOSPHORYLATION AT SER-57 AND SER-92, AND MUTAGENESIS OF SER-57 AND SER-92.
RX PubMed=23051746; DOI=10.1038/nature11444;
RA Joiner M.L., Koval O.M., Li J., He B.J., Allamargot C., Gao Z.,
RA Luczak E.D., Hall D.D., Fink B.D., Chen B., Yang J., Moore S.A.,
RA Scholz T.D., Strack S., Mohler P.J., Sivitz W.I., Song L.S., Anderson M.E.;
RT "CaMKII determines mitochondrial stress responses in heart.";
RL Nature 491:269-273(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH MCUR1 AND MICU1.
RX PubMed=23178883; DOI=10.1038/ncb2622;
RA Mallilankaraman K., Cardenas C., Doonan P.J., Chandramoorthy H.C.,
RA Irrinki K.M., Golenar T., Csordas G., Madireddi P., Yang J., Muller M.,
RA Miller R., Kolesar J.E., Molgo J., Kaufman B., Hajnoczky G., Foskett J.K.,
RA Madesh M.;
RT "MCUR1 is an essential component of mitochondrial Ca(2+) uptake that
RT regulates cellular metabolism.";
RL Nat. Cell Biol. 14:1336-1343(2012).
RN [12]
RP FUNCTION.
RX PubMed=22829870; DOI=10.1371/journal.pone.0039722;
RA Tarasov A.I., Semplici F., Ravier M.A., Bellomo E.A., Pullen T.J.,
RA Gilon P., Sekler I., Rizzuto R., Rutter G.A.;
RT "The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP
RT increases in pancreatic beta-cells.";
RL PLoS ONE 7:E39722-E39722(2012).
RN [13]
RP FUNCTION.
RX PubMed=22822213; DOI=10.1073/pnas.1210718109;
RA Drago I., De Stefani D., Rizzuto R., Pozzan T.;
RT "Mitochondrial Ca2+ uptake contributes to buffering cytoplasmic Ca2+ peaks
RT in cardiomyocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12986-12991(2012).
RN [14]
RP IDENTIFICATION.
RX PubMed=22605770; DOI=10.1126/science.1214977;
RA Bick A.G., Calvo S.E., Mootha V.K.;
RT "Evolutionary diversity of the mitochondrial calcium uniporter.";
RL Science 336:886-886(2012).
RN [15]
RP FUNCTION, AND INTERACTION WITH MICU1.
RX PubMed=24332854; DOI=10.1016/j.celrep.2013.11.026;
RA Hoffman N.E., Chandramoorthy H.C., Shamugapriya S., Zhang X., Rajan S.,
RA Mallilankaraman K., Gandhirajan R.K., Vagnozzi R.J., Ferrer L.M.,
RA Sreekrishnanilayam K., Natarajaseenivasan K., Vallem S., Force T.,
RA Choi E.T., Cheung J.Y., Madesh M.;
RT "MICU1 motifs define mitochondrial calcium uniporter binding and
RT activity.";
RL Cell Rep. 5:1576-1588(2013).
RN [16]
RP INDUCTION.
RX PubMed=23246404; DOI=10.1016/j.cub.2012.11.026;
RA Marchi S., Lupini L., Patergnani S., Rimessi A., Missiroli S., Bonora M.,
RA Bononi A., Corra F., Giorgi C., De Marchi E., Poletti F., Gafa R.,
RA Lanza G., Negrini M., Rizzuto R., Pinton P.;
RT "Downregulation of the mitochondrial calcium uniporter by cancer-related
RT miR-25.";
RL Curr. Biol. 23:58-63(2013).
RN [17]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP SER-259.
RX PubMed=23755363; DOI=10.7554/elife.00704;
RA Chaudhuri D., Sancak Y., Mootha V.K., Clapham D.E.;
RT "MCU encodes the pore conducting mitochondrial calcium currents.";
RL Elife 2:E00704-E00704(2013).
RN [18]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE UNIPLEX COMPLEX.
RX PubMed=24231807; DOI=10.1126/science.1242993;
RA Sancak Y., Markhard A.L., Kitami T., Kovacs-Bogdan E., Kamer K.J.,
RA Udeshi N.D., Carr S.A., Chaudhuri D., Clapham D.E., Li A.A., Calvo S.E.,
RA Goldberger O., Mootha V.K.;
RT "EMRE is an essential component of the mitochondrial calcium uniporter
RT complex.";
RL Science 342:1379-1382(2013).
RN [19]
RP PHOSPHORYLATION.
RX PubMed=24800979; DOI=10.1089/ars.2013.5394;
RA O-Uchi J., Jhun B.S., Xu S., Hurst S., Raffaello A., Liu X., Yi B.,
RA Zhang H., Gross P., Mishra J., Ainbinder A., Kettlewell S., Smith G.L.,
RA Dirksen R.T., Wang W., Rizzuto R., Sheu S.S.;
RT "Adrenergic signaling regulates mitochondrial Ca2+ uptake through Pyk2-
RT dependent tyrosine phosphorylation of the mitochondrial Ca2+ uniporter.";
RL Antioxid. Redox Signal. 21:863-879(2014).
RN [20]
RP INTERACTION WITH SLC25A23.
RX PubMed=24430870; DOI=10.1091/mbc.e13-08-0502;
RA Hoffman N.E., Chandramoorthy H.C., Shanmughapriya S., Zhang X.Q.,
RA Vallem S., Doonan P.J., Malliankaraman K., Guo S., Rajan S., Elrod J.W.,
RA Koch W.J., Cheung J.Y., Madesh M.;
RT "SLC25A23 augments mitochondrial Ca(2+) uptake, interacts with MCU, and
RT induces oxidative stress-mediated cell death.";
RL Mol. Biol. Cell 25:936-947(2014).
RN [21]
RP FUNCTION.
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 [22]
RP COMMENT ON PUBMED:23051746 RESULTS.
RX PubMed=25254480; DOI=10.1038/nature13626;
RA Fieni F., Johnson D.E., Hudmon A., Kirichok Y.;
RT "Mitochondrial Ca2+ uniporter and CaMKII in heart.";
RL Nature 513:E1-E2(2014).
RN [23]
RP COMMENT ON PUBMED:25254480 RESULTS.
RX PubMed=25254481; DOI=10.1038/nature13627;
RA Joiner M.L., Koval O.M., Li J., He B.J., Allamargot C., Gao Z.,
RA Luczak E.D., Hall D.D., Fink B.D., Chen B., Yang J., Moore S.A.,
RA Scholz T.D., Strack S., Mohler P.J., Sivitz W.I., Song L.S., Anderson M.E.;
RT "Joiner et al. reply.";
RL Nature 513:E3-E3(2014).
RN [24]
RP INDUCTION.
RX PubMed=25764156; DOI=10.3390/ijms16035420;
RA Pan L., Huang B.J., Ma X.E., Wang S.Y., Feng J., Lv F., Liu Y., Liu Y.,
RA Li C.M., Liang D.D., Li J., Xu L., Chen Y.H.;
RT "MiR-25 protects cardiomyocytes against oxidative damage by targeting the
RT mitochondrial calcium uniporter.";
RL Int. J. Mol. Sci. 16:5420-5433(2015).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF 261-ASP--GLU-264.
RX PubMed=25603276; DOI=10.1038/ncomms7081;
RA Wu Y., Rasmussen T.P., Koval O.M., Joiner M.L., Hall D.D., Chen B.,
RA Luczak E.D., Wang Q., Rokita A.G., Wehrens X.H., Song L.S., Anderson M.E.;
RT "The mitochondrial uniporter controls fight or flight heart rate
RT increases.";
RL Nat. Commun. 6:6081-6081(2015).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP FUNCTION.
RX PubMed=26903221; DOI=10.1016/j.bbamem.2016.02.022;
RA Matesanz-Isabel J., Arias-Del-Val J., Alvarez-Illera P., Fonteriz R.I.,
RA Montero M., Alvarez J.;
RT "Functional roles of MICU1 and MICU2 in mitochondrial Ca(2+) uptake.";
RL Biochim. Biophys. Acta 1858:1110-1117(2016).
RN [28]
RP INTERACTION WITH MCUR1 AND CCDC90B.
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).
RN [29]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=27099988; DOI=10.7554/elife.15545;
RA Tsai M.F., Phillips C.B., Ranaghan M., Tsai C.W., Wu Y., Willliams C.,
RA Miller C.;
RT "Dual functions of a small regulatory subunit in the mitochondrial calcium
RT uniporter complex.";
RL Elife 5:0-0(2016).
RN [30]
RP MUTAGENESIS OF GLU-257; SER-259; ASP-261 AND GLU-264.
RX PubMed=27135929; DOI=10.1038/nature17656;
RA Oxenoid K., Dong Y., Cao C., Cui T., Sancak Y., Markhard A.L., Grabarek Z.,
RA Kong L., Liu Z., Ouyang B., Cong Y., Mootha V.K., Chou J.J.;
RT "Architecture of the mitochondrial calcium uniporter.";
RL Nature 533:269-273(2016).
RN [31]
RP INTERACTION WITH MCUR1.
RX PubMed=26976564; DOI=10.1073/pnas.1602264113;
RA Chaudhuri D., Artiga D.J., Abiria S.A., Clapham D.E.;
RT "Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium
RT threshold for the mitochondrial permeability transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1872-E1880(2016).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 75-185, FUNCTION, SUBUNIT,
RP INTERACTION WITH MCUR1; MICU1 AND MICU2, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF SER-92 AND LYS-180, AND DOMAIN.
RX PubMed=26341627; DOI=10.15252/embr.201540436;
RA Lee Y., Min C.K., Kim T.G., Song H.K., Lim Y., Kim D., Shin K., Kang M.,
RA Kang J.Y., Youn H.S., Lee J.G., An J.Y., Park K.R., Lim J.J., Kim J.H.,
RA Kim J.H., Park Z.Y., Kim Y.S., Wang J., Kim D.H., Eom S.H.;
RT "Structure and function of the N-terminal domain of the human mitochondrial
RT calcium uniporter.";
RL EMBO Rep. 16:1318-1333(2015).
CC -!- FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates
CC calcium uptake into mitochondria (PubMed:21685888, PubMed:21685886,
CC PubMed:23101630, PubMed:22904319, PubMed:23178883, PubMed:22829870,
CC PubMed:22822213, PubMed:24332854, PubMed:23755363, PubMed:26341627).
CC Constitutes the pore-forming and calcium-conducting subunit of the
CC uniporter complex (uniplex) (PubMed:23755363). Activity is regulated by
CC MICU1 and MICU2. At low Ca(2+) levels MCU activity is down-regulated by
CC MICU1 and MICU2; at higher Ca(2+) levels MICU1 increases MCU activity
CC (PubMed:24560927, PubMed:26903221). Mitochondrial calcium homeostasis
CC plays key roles in cellular physiology and regulates cell
CC bioenergetics, cytoplasmic calcium signals and activation of cell death
CC pathways. Involved in buffering the amplitude of systolic calcium rises
CC in cardiomyocytes (PubMed:22822213). While dispensable for baseline
CC homeostatic cardiac function, acts as a key regulator of short-term
CC mitochondrial calcium loading underlying a 'fight-or-flight' response
CC during acute stress: acts by mediating a rapid increase of
CC mitochondrial calcium in pacemaker cells (PubMed:25603276).
CC participates in mitochondrial permeability transition during ischemia-
CC reperfusion injury (By similarity). Regulates glucose-dependent insulin
CC secretion in pancreatic beta-cells by regulating mitochondrial calcium
CC uptake (PubMed:22904319, PubMed:22829870). Mitochondrial calcium uptake
CC in skeletal muscle cells is involved in muscle size in adults (By
CC similarity). Regulates synaptic vesicle endocytosis kinetics in central
CC nerve terminal (By similarity). Involved in antigen processing and
CC presentation (By similarity). {ECO:0000250|UniProtKB:Q3UMR5,
CC ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888,
CC ECO:0000269|PubMed:22822213, ECO:0000269|PubMed:22829870,
CC ECO:0000269|PubMed:22904319, ECO:0000269|PubMed:23101630,
CC ECO:0000269|PubMed:23178883, ECO:0000269|PubMed:23755363,
CC ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24560927,
CC ECO:0000269|PubMed:25603276, ECO:0000269|PubMed:26341627,
CC ECO:0000269|PubMed:26903221}.
CC -!- ACTIVITY REGULATION: Inhibited by ruthenium red or its derivative
CC Ru360. {ECO:0000269|PubMed:23755363}.
CC -!- SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB,
CC MICU1, MICU2 and EMRE/SMDT1 (PubMed:24231807). Homooligomer
CC (PubMed:21685886, PubMed:26341627). Forms a pentamer (By similarity).
CC Heterooligomer with CCDC109B/MCUB; this inhibits channel activity (By
CC similarity). Interacts with MICU1; MICU1 acts as an essential regulator
CC for MCU (PubMed:21685886, PubMed:23101630, PubMed:23178883,
CC PubMed:24332854, PubMed:26341627). Interacts with MCUR1
CC (PubMed:23178883, PubMed:26341627, PubMed:27184846, PubMed:26976564).
CC Interacts with CCDC90B (PubMed:27184846). Interactions with MICU1 and
CC MCUR1 are mutually exclusive (PubMed:23178883). Interacts with MICU2
CC (PubMed:26341627). Interacts with SLC25A23 (PubMed:24430870).
CC {ECO:0000250|UniProtKB:Q21121, ECO:0000250|UniProtKB:Q3UMR5,
CC ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:23101630,
CC ECO:0000269|PubMed:23178883, ECO:0000269|PubMed:24231807,
CC ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24430870,
CC ECO:0000269|PubMed:26341627, ECO:0000269|PubMed:26976564,
CC ECO:0000269|PubMed:27184846}.
CC -!- INTERACTION:
CC Q8NE86; Q9BPX6: MICU1; NbExp=7; IntAct=EBI-6552124, EBI-2371996;
CC Q8NE86; Q9H4I9: SMDT1; NbExp=7; IntAct=EBI-6552124, EBI-11908005;
CC Q8NE86-1; Q8NE86-1: MCU; NbExp=2; IntAct=EBI-15932889, EBI-15932889;
CC Q8NE86-1; Q96AQ8: MCUR1; NbExp=4; IntAct=EBI-15932889, EBI-14404755;
CC Q8NE86-1; Q9BPX6: MICU1; NbExp=2; IntAct=EBI-15932889, EBI-2371996;
CC Q8NE86-1; Q9BPX6-1: MICU1; NbExp=2; IntAct=EBI-15932889, EBI-5456336;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888,
CC ECO:0000269|PubMed:23755363, ECO:0000269|PubMed:24231807,
CC ECO:0000269|PubMed:27099988, ECO:0000305|PubMed:26341627}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21685886,
CC ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:24231807}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NE86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NE86-2; Sequence=VSP_024263;
CC Name=3;
CC IsoId=Q8NE86-3; Sequence=VSP_041687;
CC -!- INDUCTION: MCU transcripts are down-regulated by microRNA miR-25
CC (PubMed:23246404). Down-regulation by miR-25 may protect cardiomyocytes
CC against oxidative damage in cardiomyocytes (PubMed:25764156).
CC {ECO:0000269|PubMed:23246404, ECO:0000269|PubMed:25764156}.
CC -!- DOMAIN: The N-terminal MCU domain is required for efficient Ca(2+)
CC uptake and for interaction with MCUR1. It is not required for targeting
CC to the mitochondria, oligomerization, interaction with MICU1 and MICU2,
CC or assembly of the uniplex complex. {ECO:0000269|PubMed:26341627}.
CC -!- DOMAIN: Forms a well-packed pentamer with an overall cylindrical shape.
CC The inner core of the pentamer is formed with the second transmembrane
CC region and the second coiled-coil region: while the transmembrane
CC regions pack into a five-helix bundle having a largely polar pore
CC across the membrane, the coiled-coil outside the membrane forms a
CC pentamer with a hydrophobic core. The inner core is wrapped by the
CC first transmembrane region through contacts between the first and the
CC second transmembrane regions. The second transmembrane is followed by
CC the inner juxtamembrane region (IJMH) that orients at a wide angle
CC relative to the second transmembrane. The two core domains are held
CC together on the periphery by the outer juxtamembrane helix (OJMH).
CC {ECO:0000250|UniProtKB:Q21121}.
CC -!- DOMAIN: The critical DXXE motif connecting the transmembrane regions
CC forms a pentameric barrel that constitutes the mouth of the pore.
CC Inside the barrel, two acidic residues are in position to form two
CC carboxylate rings. In absence of SMDT1/EMRE regulator, the calcium ions
CC cannot exit the channel, suggesting that SMDT1/EMRE-binding induces
CC conformational rearrangements to allow calcium to exit.
CC {ECO:0000250|UniProtKB:Q21121}.
CC -!- PTM: Phosphorylation by CaMK2 in heart leads to increased MCU current
CC (PubMed:23051746, PubMed:25254481). The regulation of MCU by CaMK2 is
CC however subject to discussion: another group was unable to reproduce
CC these results (PubMed:25254480). Phosphorylated on tyrosines by
CC PTK2B/PYK2, promoting oligomerization (PubMed:24800979).
CC {ECO:0000269|PubMed:24800979, ECO:0000305|PubMed:23051746,
CC ECO:0000305|PubMed:25254480, ECO:0000305|PubMed:25254481}.
CC -!- SIMILARITY: Belongs to the MCU (TC 1.A.77) family. {ECO:0000305}.
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DR EMBL; AK315519; BAG37900.1; -; mRNA.
DR EMBL; AK128016; BAG54619.1; -; mRNA.
DR EMBL; AC016542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54461.1; -; Genomic_DNA.
DR EMBL; BC010682; AAH10682.1; -; mRNA.
DR EMBL; BC034235; AAH34235.1; -; mRNA.
DR CCDS; CCDS59218.1; -. [Q8NE86-2]
DR CCDS; CCDS59219.1; -. [Q8NE86-3]
DR CCDS; CCDS7317.1; -. [Q8NE86-1]
DR RefSeq; NP_001257608.1; NM_001270679.1. [Q8NE86-2]
DR RefSeq; NP_001257609.1; NM_001270680.1. [Q8NE86-3]
DR RefSeq; NP_612366.1; NM_138357.2. [Q8NE86-1]
DR PDB; 4XSJ; X-ray; 1.80 A; A=75-165.
DR PDB; 4XTB; X-ray; 1.50 A; A=75-185.
DR PDB; 5BZ6; X-ray; 2.75 A; A=75-165.
DR PDB; 5KUE; X-ray; 1.50 A; A=72-189.
DR PDB; 5KUG; X-ray; 1.90 A; A=72-189.
DR PDB; 5KUI; X-ray; 2.70 A; A=72-189.
DR PDB; 5KUJ; X-ray; 1.60 A; A=72-189.
DR PDB; 6JG0; X-ray; 2.50 A; A=75-165.
DR PDB; 6K7X; EM; 3.27 A; A/B/C/D/K/L/M/N=73-348.
DR PDB; 6K7Y; EM; 3.60 A; A/B/C/D/N/O/P/Q=73-348.
DR PDB; 6KVX; X-ray; 2.85 A; A=75-164.
DR PDB; 6O58; EM; 3.80 A; A/C/E/G/I/K/M/O=1-351.
DR PDB; 6O5B; EM; 3.60 A; A/C/E/G/I/J/K/L=1-351.
DR PDB; 6WDN; EM; 3.20 A; C/E/G/I=169-346.
DR PDB; 6WDO; EM; 3.60 A; A/E/G/I/M/O=74-346, C/K=74-341.
DR PDB; 6XJV; EM; 4.17 A; A/C/E/G/I/K/M/O=1-351.
DR PDB; 6XJX; EM; 4.60 A; A/C/E/G=1-351.
DR PDBsum; 4XSJ; -.
DR PDBsum; 4XTB; -.
DR PDBsum; 5BZ6; -.
DR PDBsum; 5KUE; -.
DR PDBsum; 5KUG; -.
DR PDBsum; 5KUI; -.
DR PDBsum; 5KUJ; -.
DR PDBsum; 6JG0; -.
DR PDBsum; 6K7X; -.
DR PDBsum; 6K7Y; -.
DR PDBsum; 6KVX; -.
DR PDBsum; 6O58; -.
DR PDBsum; 6O5B; -.
DR PDBsum; 6WDN; -.
DR PDBsum; 6WDO; -.
DR PDBsum; 6XJV; -.
DR PDBsum; 6XJX; -.
DR AlphaFoldDB; Q8NE86; -.
DR SMR; Q8NE86; -.
DR BioGRID; 124733; 192.
DR ComplexPortal; CPX-5961; Mitochondrial calcium uniporter complex, MICU1-MICU2 variant.
DR ComplexPortal; CPX-5963; Mitochondrial calcium uniporter complex, MICU1 variant.
DR ComplexPortal; CPX-5965; Mitochondrial calcium uniporter complex, MICU1-MICU3 variant.
DR ComplexPortal; CPX-5966; Mitochondrial calcium uniporter complex, MICUB variant.
DR CORUM; Q8NE86; -.
DR DIP; DIP-60468N; -.
DR IntAct; Q8NE86; 32.
DR MINT; Q8NE86; -.
DR STRING; 9606.ENSP00000362144; -.
DR GlyGen; Q8NE86; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NE86; -.
DR MetOSite; Q8NE86; -.
DR PhosphoSitePlus; Q8NE86; -.
DR SwissPalm; Q8NE86; -.
DR BioMuta; MCU; -.
DR DMDM; 74730222; -.
DR EPD; Q8NE86; -.
DR jPOST; Q8NE86; -.
DR MassIVE; Q8NE86; -.
DR MaxQB; Q8NE86; -.
DR PaxDb; Q8NE86; -.
DR PeptideAtlas; Q8NE86; -.
DR PRIDE; Q8NE86; -.
DR ProteomicsDB; 73134; -. [Q8NE86-1]
DR ProteomicsDB; 73135; -. [Q8NE86-2]
DR ProteomicsDB; 73136; -. [Q8NE86-3]
DR TopDownProteomics; Q8NE86-3; -. [Q8NE86-3]
DR Antibodypedia; 3091; 85 antibodies from 21 providers.
DR DNASU; 90550; -.
DR Ensembl; ENST00000357157.10; ENSP00000349680.6; ENSG00000156026.15. [Q8NE86-2]
DR Ensembl; ENST00000373053.8; ENSP00000362144.3; ENSG00000156026.15. [Q8NE86-1]
DR Ensembl; ENST00000536019.5; ENSP00000440913.1; ENSG00000156026.15. [Q8NE86-3]
DR GeneID; 90550; -.
DR KEGG; hsa:90550; -.
DR MANE-Select; ENST00000373053.8; ENSP00000362144.3; NM_138357.3; NP_612366.1.
DR UCSC; uc001jtc.3; human. [Q8NE86-1]
DR CTD; 90550; -.
DR DisGeNET; 90550; -.
DR GeneCards; MCU; -.
DR HGNC; HGNC:23526; MCU.
DR HPA; ENSG00000156026; Tissue enhanced (tongue).
DR MIM; 614197; gene.
DR neXtProt; NX_Q8NE86; -.
DR OpenTargets; ENSG00000156026; -.
DR PharmGKB; PA134888841; -.
DR VEuPathDB; HostDB:ENSG00000156026; -.
DR eggNOG; KOG2966; Eukaryota.
DR GeneTree; ENSGT00940000157528; -.
DR HOGENOM; CLU_056554_0_0_1; -.
DR InParanoid; Q8NE86; -.
DR OMA; DDIYVEY; -.
DR OrthoDB; 1076768at2759; -.
DR PhylomeDB; Q8NE86; -.
DR TreeFam; TF314435; -.
DR PathwayCommons; Q8NE86; -.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-HSA-8949664; Processing of SMDT1.
DR SignaLink; Q8NE86; -.
DR BioGRID-ORCS; 90550; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; MCU; human.
DR GenomeRNAi; 90550; -.
DR Pharos; Q8NE86; Tbio.
DR PRO; PR:Q8NE86; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8NE86; protein.
DR Bgee; ENSG00000156026; Expressed in tibialis anterior and 152 other tissues.
DR ExpressionAtlas; Q8NE86; baseline and differential.
DR Genevisible; Q8NE86; HS.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:1990246; C:uniplex complex; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015292; F:uniporter activity; IDA:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; IMP:CACAO.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IDA:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:CACAO.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:CACAO.
DR GO; GO:0051259; P:protein complex oligomerization; IDA: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 3D-structure; Acetylation; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Coiled coil; Ion channel; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..351
FT /note="Calcium uniporter protein, mitochondrial"
FT /id="PRO_0000282976"
FT TOPO_DOM 51..233
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27099988"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..265
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27099988"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..351
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:23755363,
FT ECO:0000305|PubMed:27099988"
FT REGION 75..165
FT /note="N-terminal MCU domain"
FT /evidence="ECO:0000269|PubMed:26341627"
FT REGION 216..234
FT /note="Outer juxtamembrane helix (OJMH)"
FT /evidence="ECO:0000250|UniProtKB:Q21121"
FT REGION 283..292
FT /note="Inner juxtamembrane helix (IJMH)"
FT /evidence="ECO:0000250|UniProtKB:Q21121"
FT COILED 192..223
FT /evidence="ECO:0000255"
FT COILED 311..339
FT /evidence="ECO:0000255"
FT MOTIF 261..264
FT /note="DXXE"
FT /evidence="ECO:0000250|UniProtKB:Q21121"
FT MOD_RES 57
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000305|PubMed:23051746"
FT MOD_RES 92
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000305|PubMed:23051746"
FT MOD_RES 332
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMR5"
FT VAR_SEQ 1..50
FT /note="MAAAAGRSLLLLLSSRGGGGGGAGGCGALTAGCFPGLGVSRHRQQQHHRT
FT -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041687"
FT VAR_SEQ 166..219
FT /note="DLLSHENAATLNDVKTLVQQLYTTLCIEQHQLNKERELIERLEDLKEQLAPL
FT EK -> VEMGFCHVGQNGFELLTSSYLPASASQSAEIIA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024263"
FT MUTAGEN 57
FT /note="S->A: Decreased MCU current; when associated with A-
FT 92."
FT /evidence="ECO:0000269|PubMed:23051746"
FT MUTAGEN 92
FT /note="S->A: Decreased MCU current; when associated with A-
FT 57."
FT /evidence="ECO:0000269|PubMed:23051746"
FT MUTAGEN 92
FT /note="S->A: Impairs Ca(2+) uptake, but has no effect on
FT oligomerization and interaction with MCU1 and MCU2."
FT /evidence="ECO:0000269|PubMed:26341627"
FT MUTAGEN 180
FT /note="K->A: No effect on Ca(2+) uptake, oligomerization
FT and interaction with MCU1 and MCU2."
FT /evidence="ECO:0000269|PubMed:26341627"
FT MUTAGEN 257
FT /note="E->A: According to a report, inhibits calcium
FT uptake. According to a subsequent report, does not affect
FT greatly calcium uptake."
FT /evidence="ECO:0000269|PubMed:21685886,
FT ECO:0000269|PubMed:27135929"
FT MUTAGEN 257
FT /note="E->S: Does not affect greatly calcium uptake."
FT /evidence="ECO:0000269|PubMed:27135929"
FT MUTAGEN 259
FT /note="S->A: Does not inhibit calcium uptake. Strongly
FT reduced sensitivity to ruthenium red inhibition."
FT /evidence="ECO:0000269|PubMed:21685886,
FT ECO:0000269|PubMed:23755363"
FT MUTAGEN 259
FT /note="S->R: Prevents entrance of calcium into the pore."
FT /evidence="ECO:0000269|PubMed:27135929"
FT MUTAGEN 261..264
FT /note="DIME->AIMA: Dominant negative (DN) mutant; inhibits
FT calcium uptake. Inhibits calcium channel activity.
FT Expression of the dominant negative protein in mice, leads
FT to mice that are incapable of physiological fight or flight
FT heart rate acceleration."
FT /evidence="ECO:0000269|PubMed:21685886,
FT ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:25603276"
FT MUTAGEN 261
FT /note="D->E: Partially functional; does not completely
FT abolish calcium channel activity."
FT /evidence="ECO:0000269|PubMed:27135929"
FT MUTAGEN 264
FT /note="E->D: Abolishes calcium channel activity."
FT /evidence="ECO:0000269|PubMed:27135929"
FT CONFLICT 107
FT /note="S -> P (in Ref. 1; BAG37900)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="D -> Y (in Ref. 1; BAG37900)"
FT /evidence="ECO:0000305"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5KUI"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4XTB"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4XTB"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5KUI"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4XTB"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4XTB"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4XTB"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 221..240
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:6WDN"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6WDN"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6WDN"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:6WDN"
FT TURN 275..279
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 291..310
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6WDN"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6WDN"
SQ SEQUENCE 351 AA; 39867 MW; 50205D01055D66E4 CRC64;
MAAAAGRSLL LLLSSRGGGG GGAGGCGALT AGCFPGLGVS RHRQQQHHRT VHQRIASWQN
LGAVYCSTVV PSDDVTVVYQ NGLPVISVRL PSRRERCQFT LKPISDSVGV FLRQLQEEDR
GIDRVAIYSP DGVRVAASTG IDLLLLDDFK LVINDLTYHV RPPKRDLLSH ENAATLNDVK
TLVQQLYTTL CIEQHQLNKE RELIERLEDL KEQLAPLEKV RIEISRKAEK RTTLVLWGGL
AYMATQFGIL ARLTWWEYSW DIMEPVTYFI TYGSAMAMYA YFVMTRQEYV YPEARDRQYL
LFFHKGAKKS RFDLEKYNQL KDAIAQAEMD LKRLRDPLQV HLPLRQIGEK D
