MIDUO_HUMAN
ID MIDUO_HUMAN Reviewed; 70 AA.
AC L0R8F8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=MIEF1 upstream open reading frame protein {ECO:0000305};
DE AltName: Full=Alternative MIEF1 protein {ECO:0000303|PubMed:29083303, ECO:0000305};
DE Short=AltMIEF1 {ECO:0000303|PubMed:29083303};
DE AltName: Full=MIEF1 microprotein {ECO:0000303|PubMed:30215512};
DE Short=MIEF1-MP {ECO:0000303|PubMed:30215512};
GN Name=MIEF1 {ECO:0000312|HGNC:HGNC:25979};
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 [GENOMIC DNA], AND ALTERNATIVE INITIATION (ISOFORM 2).
RX PubMed=23950983; DOI=10.1371/journal.pone.0070698;
RA Vanderperre B., Lucier J.-F., Motard J., Tremblay G., Vanderperre S.,
RA Wisztorski M., Salzet M., Boisvert F.-M., Roucou X.;
RT "Direct detection of alternative open reading frames translation products
RT in human significantly expands the proteome.";
RL PLoS ONE 8:E70698-E70698(2013).
RN [2]
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 [3]
RP ALTERNATIVE INITIATION (ISOFORM 2).
RX PubMed=25621764; DOI=10.7554/elife.03971;
RA Andreev D.E., O'Connor P.B., Fahey C., Kenny E.M., Terenin I.M.,
RA Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V.;
RT "Translation of 5' leaders is pervasive in genes resistant to eIF2
RT repression.";
RL Elife 4:E03971-E03971(2015).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 12-LEU--ARG-14.
RX PubMed=29083303; DOI=10.7554/elife.27860;
RA Samandi S., Roy A.V., Delcourt V., Lucier J.F., Gagnon J., Beaudoin M.C.,
RA Vanderperre B., Breton M.A., Motard J., Jacques J.F., Brunelle M.,
RA Gagnon-Arsenault I., Fournier I., Ouangraoua A., Hunting D.J., Cohen A.A.,
RA Landry C.R., Scott M.S., Roucou X.;
RT "Deep transcriptome annotation enables the discovery and functional
RT characterization of cryptic small proteins.";
RL Elife 6:0-0(2017).
RN [5]
RP FUNCTION, INTERACTION WITH MRPL4; MRPS27 AND NDUFAB1, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF 12-LEU--ARG-14 AND PHE-39.
RX PubMed=30215512; DOI=10.1021/acs.biochem.8b00726;
RA Rathore A., Chu Q., Tan D., Martinez T.F., Donaldson C.J., Diedrich J.K.,
RA Yates J.R. III, Saghatelian A.;
RT "MIEF1 microprotein regulates mitochondrial translation.";
RL Biochemistry 57:5564-5575(2018).
RN [6] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- FUNCTION: Involved in the regulation of mitochondrial fission mediated
CC by DNM1L (PubMed:29083303). Positively regulates mitochondrial
CC translation (PubMed:30215512). May play a role in ribosome biogenesis
CC by preventing premature association of the 28S and 39S ribosomal
CC subunits (Probable). {ECO:0000269|PubMed:29083303,
CC ECO:0000269|PubMed:30215512, ECO:0000305|PubMed:28892042}.
CC -!- SUBUNIT: Identified in a complex composed of MALSU1, MIEF1 upstream
CC open reading frame protein and NDUFAB1; within the trimeric complex,
CC MIEF1 upstream open reading frame protein functions as a bridging
CC scaffold that interacts with MALSU1 on one side, and with NDUFAB1 on
CC the other side (PubMed:28892042, PubMed:30215512). Within the complex,
CC MALSU1 mediates interaction with the mitochondrial large ribosomal
CC subunit (PubMed:28892042). Interacts with ribosomal proteins MRPL4 and
CC MRPS27 (PubMed:30215512). {ECO:0000269|PubMed:28892042,
CC ECO:0000269|PubMed:30215512}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:28892042, ECO:0000269|PubMed:29083303,
CC ECO:0000269|PubMed:30215512}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=3; Synonyms=uORF {ECO:0000303|PubMed:25621764}, AltMIEF1
CC {ECO:0000303|PubMed:29083303};
CC IsoId=L0R8F8-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9NQG6-1; Sequence=External;
CC Name=2;
CC IsoId=Q9NQG6-2; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform 3]: Product of the upstream open reading frame
CC of this bicistronic gene. {ECO:0000305|PubMed:25621764}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. {ECO:0000305}.
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DR EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HF548110; CCO13821.1; -; Genomic_DNA.
DR PDB; 5OOL; EM; 3.06 A; v=1-70.
DR PDB; 5OOM; EM; 3.03 A; v=1-70.
DR PDB; 7A5H; EM; 3.30 A; v=1-70.
DR PDB; 7A5J; EM; 3.10 A; v=1-70.
DR PDB; 7O9K; EM; 3.10 A; v=1-70.
DR PDB; 7O9M; EM; 2.50 A; v=1-70.
DR PDB; 7ODR; EM; 2.90 A; v=1-70.
DR PDB; 7ODS; EM; 3.10 A; v=1-70.
DR PDB; 7ODT; EM; 3.10 A; v=1-70.
DR PDB; 7OF0; EM; 2.20 A; v=1-70.
DR PDB; 7OF2; EM; 2.70 A; v=1-70.
DR PDB; 7OF3; EM; 2.70 A; v=1-70.
DR PDB; 7OF5; EM; 2.90 A; v=1-70.
DR PDB; 7OF7; EM; 2.50 A; v=1-70.
DR PDB; 7OI6; EM; 5.70 A; v=1-70.
DR PDB; 7OI7; EM; 3.50 A; v=1-70.
DR PDB; 7OI8; EM; 3.50 A; v=1-70.
DR PDB; 7OI9; EM; 3.30 A; v=1-70.
DR PDB; 7OIC; EM; 3.10 A; v=1-70.
DR PDB; 7OID; EM; 3.70 A; v=1-70.
DR PDB; 7OIE; EM; 3.50 A; v=1-70.
DR PDB; 7PD3; EM; 3.40 A; v=1-70.
DR PDB; 7QH6; EM; 3.08 A; v=1-70.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; L0R8F8; -.
DR SMR; L0R8F8; -.
DR IntAct; L0R8F8; 1.
DR BioMuta; MIEF1; -.
DR EPD; L0R8F8; -.
DR jPOST; L0R8F8; -.
DR MassIVE; L0R8F8; -.
DR PeptideAtlas; L0R8F8; -.
DR PRIDE; L0R8F8; -.
DR Antibodypedia; 82186; 1 antibodies from 1 providers.
DR GeneCards; MIEF1; -.
DR HGNC; HGNC:25979; MIEF1.
DR HPA; ENSG00000285025; Tissue enhanced (brain, choroid plexus, skeletal muscle).
DR neXtProt; NX_L0R8F8; -.
DR VEuPathDB; HostDB:ENSG00000285025; -.
DR GeneTree; ENSGT01030000234887; -.
DR OMA; KYGNHLK; -.
DR PathwayCommons; L0R8F8; -.
DR SignaLink; L0R8F8; -.
DR ChiTaRS; MIEF1; human.
DR Pharos; L0R8F8; Tbio.
DR Proteomes; UP000005640; Chromosome 22.
DR Bgee; ENSG00000100335; Expressed in sperm and 204 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd20272; Complex1_LYR_MIEF1-MP; 1.
DR InterPro; IPR008011; Complex1_LYR_dom.
DR InterPro; IPR045300; Complex1_LYR_MIEF1-MP.
DR Pfam; PF05347; Complex1_LYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Mitochondrion;
KW Reference proteome; Ribosome biogenesis; Translation regulation.
FT CHAIN 1..70
FT /note="MIEF1 upstream open reading frame protein"
FT /id="PRO_0000439344"
FT MUTAGEN 12..14
FT /note="LYR->AAA: Inhibits mitochondrial fission. Unable to
FT convert the mitochondrial morphology from tubular to
FT fragmented. Abolishes interaction with NDUFAB1; when
FT associated with A-39."
FT /evidence="ECO:0000269|PubMed:29083303,
FT ECO:0000269|PubMed:30215512"
FT MUTAGEN 39
FT /note="F->A: Abolishes interaction with NDUFAB1; when
FT associated with 12-A--A-14."
FT /evidence="ECO:0000269|PubMed:30215512"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 70 AA; 8445 MW; 4910AF3BF93D0CD2 CRC64;
MAPWSREAVL SLYRALLRQG RQLRYTDRDF YFASIRREFR KNQKLEDAEA RERQLEKGLV
FLNGKLGRII
