EMRE_HUMAN
ID EMRE_HUMAN Reviewed; 107 AA.
AC Q9H4I9; B2R5D1; Q8TAB9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Essential MCU regulator, mitochondrial {ECO:0000303|PubMed:24231807};
DE AltName: Full=Single-pass membrane protein with aspartate-rich tail 1, mitochondrial {ECO:0000312|HGNC:HGNC:25055};
DE Flags: Precursor;
GN Name=SMDT1 {ECO:0000312|HGNC:HGNC:25055};
GN Synonyms=C22orf32 {ECO:0000312|HGNC:HGNC:25055},
GN EMRE {ECO:0000303|PubMed:24231807};
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].
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-46.
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 [6]
RP FUNCTION, 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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 101-GLU--ASP-107.
RX PubMed=26774479; DOI=10.1016/j.celrep.2015.12.054;
RA Vais H., Mallilankaraman K., Mak D.O., Hoff H., Payne R., Tanis J.E.,
RA Foskett J.K.;
RT "EMRE is a matrix Ca(2+) sensor that governs gatekeeping of the
RT mitochondrial Ca(2+) uniporter.";
RL Cell Rep. 14:403-410(2016).
RN [9]
RP INTERACTION WITH MCUR1.
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, INTERACTION WITH MCU AND
RP MICU1, AND MUTAGENESIS OF GLY-81 AND SER-85.
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 [11]
RP SUBCELLULAR LOCATION, TOPOLOGY, PROTEOLYTIC PROCESSING, AND INTERACTION
RP WITH MAIP1.
RX PubMed=27642048; DOI=10.1016/j.molcel.2016.08.020;
RA Koenig T., Troeder S.E., Bakka K., Korwitz A., Richter-Dennerlein R.,
RA Lampe P.A., Patron M., Muehlmeister M., Guerrero-Castillo S., Brandt U.,
RA Decker T., Lauria I., Paggio A., Rizzuto R., Rugarli E.I., De Stefani D.,
RA Langer T.;
RT "The m-AAA protease associated with neurodegeneration limits MCU activity
RT in mitochondria.";
RL Mol. Cell 64:148-162(2016).
CC -!- FUNCTION: Essential regulatory subunit of the mitochondrial calcium
CC uniporter complex (uniplex), a complex that mediates calcium uptake
CC into mitochondria (PubMed:24231807, PubMed:26774479, PubMed:27099988).
CC Required to bridge the calcium-sensing proteins MICU1 and MICU2 with
CC the calcium-conducting subunit MCU (PubMed:24231807). Plays a central
CC role in regulating the uniplex complex response to intracellular
CC calcium signaling (PubMed:27099988). Acts by mediating activation of
CC MCU and retention of MICU1 to the MCU pore, in order to ensure tight
CC regulation of the uniplex complex and appropriate responses to
CC intracellular calcium signaling (PubMed:27099988).
CC {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:26774479,
CC ECO:0000269|PubMed:27099988}.
CC -!- SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB,
CC MICU1, MICU2 and EMRE/SMDT1 (PubMed:24231807). Interacts (via the
CC transmembrane region) with MCU (via the first transmembrane region);
CC the interaction is direct (PubMed:27099988). Interacts (via the poly-
CC Asp region) with MICU1 (via polybasic region); the interaction is
CC direct (PubMed:27099988). Interacts (via its C-terminal poly-Asp tail)
CC with MCUR1; the interaction is direct (PubMed:27184846). Unprocessed
CC form interacts (via transit peptide) with MAIP1 (PubMed:27642048).
CC {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:27099988,
CC ECO:0000269|PubMed:27184846, ECO:0000269|PubMed:27642048}.
CC -!- INTERACTION:
CC Q9H4I9; Q8NE86: MCU; NbExp=7; IntAct=EBI-11908005, EBI-6552124;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:26774479,
CC ECO:0000269|PubMed:27099988, ECO:0000269|PubMed:27642048}; Single-pass
CC membrane protein {ECO:0000269|PubMed:24231807,
CC ECO:0000269|PubMed:27099988}. Note=MAIP1 is required to assist sorting
CC of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against
CC protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation
CC by the mitochondrial processing peptidase (PMPCA and PMPCB)
CC (PubMed:27642048). {ECO:0000269|PubMed:27642048}.
CC -!- DOMAIN: The GXXXX[G/A/S] motif at the C-terminal part of the
CC transmembrane region mediates interaction with MCU and is required to
CC activate the calcium-conducting pore in the uniporter complex.
CC {ECO:0000269|PubMed:27099988}.
CC -!- DOMAIN: The poly-Asp region at the C-terminus mediates interaction with
CC the polybasic region of MICU1. {ECO:0000269|PubMed:27099988}.
CC -!- PTM: Undergoes proteolytic degradation in neurons: degraded by AFG3L2
CC before SMDT1/EMRE assembly with the uniporter complex, limiting the
CC availability of SMDT1/EMRE for MCU assembly and promoting efficient
CC assembly of gatekeeper subunits with MCU (PubMed:27642048).
CC {ECO:0000269|PubMed:27642048}.
CC -!- SIMILARITY: Belongs to the SMDT1/EMRE family. {ECO:0000305}.
CC -!- CAUTION: A publication reports an opposite topology (PubMed:26774479).
CC However, 3 different articles, 2 in human and one in mouse, confirm the
CC topology shown in this entry (PubMed:27099988, PubMed:27642048).
CC {ECO:0000269|PubMed:26774479, ECO:0000269|PubMed:27099988,
CC ECO:0000269|PubMed:27642048}.
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DR EMBL; AL449243; CAC15000.1; -; mRNA.
DR EMBL; CR456453; CAG30339.1; -; mRNA.
DR EMBL; AK312142; BAG35078.1; -; mRNA.
DR EMBL; AL021878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60488.1; -; Genomic_DNA.
DR EMBL; BC024237; AAH24237.1; -; mRNA.
DR CCDS; CCDS14031.1; -.
DR RefSeq; NP_201575.3; NM_033318.4.
DR RefSeq; XP_011528811.1; XM_011530509.2.
DR PDB; 6K7X; EM; 3.27 A; E/F/G/H/O/P/Q/R=48-101.
DR PDB; 6K7Y; EM; 3.60 A; E/F/G/H/R/S/T/U=48-101.
DR PDB; 6O58; EM; 3.80 A; B/D/F/H/J/L/N/P=1-107.
DR PDB; 6O5B; EM; 3.60 A; B/D/F/H=1-107.
DR PDB; 6WDN; EM; 3.20 A; D/F/H/J=48-98.
DR PDB; 6WDO; EM; 3.60 A; B/D/F/H/J/L/N/P=48-100.
DR PDB; 6XJV; EM; 4.17 A; B/D/F/H/J/L/N/P=1-107.
DR PDB; 6XJX; EM; 4.60 A; B/D/F/H=1-107.
DR PDBsum; 6K7X; -.
DR PDBsum; 6K7Y; -.
DR PDBsum; 6O58; -.
DR PDBsum; 6O5B; -.
DR PDBsum; 6WDN; -.
DR PDBsum; 6WDO; -.
DR PDBsum; 6XJV; -.
DR PDBsum; 6XJX; -.
DR AlphaFoldDB; Q9H4I9; -.
DR SMR; Q9H4I9; -.
DR BioGRID; 124866; 27.
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; Q9H4I9; -.
DR IntAct; Q9H4I9; 8.
DR STRING; 9606.ENSP00000327467; -.
DR TCDB; 8.A.45.1.1; the essential mcu regulator emre (emre) family.
DR BioMuta; SMDT1; -.
DR DMDM; 74761431; -.
DR EPD; Q9H4I9; -.
DR jPOST; Q9H4I9; -.
DR MassIVE; Q9H4I9; -.
DR MaxQB; Q9H4I9; -.
DR PaxDb; Q9H4I9; -.
DR PeptideAtlas; Q9H4I9; -.
DR PRIDE; Q9H4I9; -.
DR ProteomicsDB; 80848; -.
DR TopDownProteomics; Q9H4I9; -.
DR Antibodypedia; 27229; 20 antibodies from 8 providers.
DR DNASU; 91689; -.
DR Ensembl; ENST00000331479.4; ENSP00000327467.3; ENSG00000183172.9.
DR Ensembl; ENST00000571525.3; ENSP00000459368.1; ENSG00000272901.5.
DR Ensembl; ENST00000607293.3; ENSP00000475471.1; ENSG00000272835.3.
DR Ensembl; ENST00000615504.2; ENSP00000485029.1; ENSG00000274112.2.
DR GeneID; 91689; -.
DR KEGG; hsa:91689; -.
DR MANE-Select; ENST00000331479.4; ENSP00000327467.3; NM_033318.5; NP_201575.3.
DR UCSC; uc003bca.4; human.
DR CTD; 91689; -.
DR DisGeNET; 91689; -.
DR GeneCards; SMDT1; -.
DR HGNC; HGNC:25055; SMDT1.
DR HPA; ENSG00000183172; Low tissue specificity.
DR MIM; 615588; gene.
DR neXtProt; NX_Q9H4I9; -.
DR OpenTargets; ENSG00000183172; -.
DR PharmGKB; PA145149451; -.
DR VEuPathDB; HostDB:ENSG00000183172; -.
DR eggNOG; KOG4542; Eukaryota.
DR GeneTree; ENSGT00390000017489; -.
DR HOGENOM; CLU_172921_1_0_1; -.
DR InParanoid; Q9H4I9; -.
DR OMA; CISKNFA; -.
DR OrthoDB; 1586309at2759; -.
DR PhylomeDB; Q9H4I9; -.
DR TreeFam; TF314649; -.
DR PathwayCommons; Q9H4I9; -.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-HSA-8949664; Processing of SMDT1.
DR SignaLink; Q9H4I9; -.
DR BioGRID-ORCS; 91689; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; SMDT1; human.
DR GenomeRNAi; 91689; -.
DR Pharos; Q9H4I9; Tbio.
DR PRO; PR:Q9H4I9; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9H4I9; protein.
DR Bgee; ENSG00000183172; Expressed in hindlimb stylopod muscle and 103 other tissues.
DR ExpressionAtlas; Q9H4I9; baseline and differential.
DR Genevisible; Q9H4I9; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990246; C:uniplex complex; IDA:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IDA:ComplexPortal.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
DR InterPro; IPR018782; MCU_reg.
DR PANTHER; PTHR33904; PTHR33904; 1.
DR Pfam; PF10161; DDDD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:27642048"
FT CHAIN 53..107
FT /note="Essential MCU regulator, mitochondrial"
FT /id="PRO_0000296320"
FT TOPO_DOM 53..64
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27099988,
FT ECO:0000305|PubMed:27642048"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..107
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27099988,
FT ECO:0000305|PubMed:27642048"
FT REGION 1..52
FT /note="Interaction with MAIP1"
FT /evidence="ECO:0000269|PubMed:27642048"
FT MOTIF 81..85
FT /note="GXXXX[G/A/S]"
FT /evidence="ECO:0000305|PubMed:27099988"
FT VARIANT 46
FT /note="R -> G (in dbSNP:rs17852210)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034628"
FT MUTAGEN 81
FT /note="G->W: Abolishes calcium uptake into mitochondria."
FT /evidence="ECO:0000269|PubMed:27099988"
FT MUTAGEN 85
FT /note="S->W: Abolishes calcium uptake into mitochondria."
FT /evidence="ECO:0000269|PubMed:27099988"
FT MUTAGEN 101..107
FT /note="EDDDDDD->QNNNNNN: Abolishes regulation of calcium
FT uptake into mitochondria."
FT /evidence="ECO:0000269|PubMed:26774479"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6K7X"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:6WDN"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6WDN"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6WDN"
SQ SEQUENCE 107 AA; 11441 MW; 4E00824D322AE99D CRC64;
MASGAARWLV LAPVRSGALR SGPSLRKDGD VSAAWSGSGR SLVPSRSVIV TRSGAILPKP
VKMSFGLLRV FSIVIPFLYV GTLISKNFAA LLEEHDIFVP EDDDDDD
