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Mitochondrial distribution and morphology protein 38

 MDM38_YEAST             Reviewed;         573 AA.
Q08179; D6W238;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 128.
RecName: Full=Mitochondrial distribution and morphology protein 38 {ECO:0000303|PubMed:11907266};
Flags: Precursor;
Name=MDM38 {ECO:0000303|PubMed:11907266}; OrderedLocusNames=YOL027C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N.,
Neupert W., Westermann B.;
"Genetic basis of mitochondrial function and morphology in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:847-853(2002).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15138253; DOI=10.1074/jbc.M403607200;
Nowikovsky K., Froschauer E.M., Zsurka G., Samaj J., Reipert S.,
Kolisek M., Wiesenberger G., Schweyen R.J.;
"The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+
homeostasis with a potential role in the Wolf-Hirschhorn syndrome.";
J. Biol. Chem. 279:30307-30315(2004).
[8]
BINDING TO MITORIBOSOMES, INTERACTION WITH MBA1, DISRUPTION PHENOTYPE,
AND FUNCTION.
PubMed=20427570; DOI=10.1091/mbc.E10-02-0101;
Bauerschmitt H., Mick D.U., Deckers M., Vollmer C., Funes S.,
Kehrein K., Ott M., Rehling P., Herrmann J.M.;
"Ribosome-binding proteins Mdm38 and Mba1 display overlapping
functions for regulation of mitochondrial translation.";
Mol. Biol. Cell 21:1937-1944(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 160-408, DOMAIN, AND BINDING
TO MITORIBOSOMES.
PubMed=21718401; DOI=10.1111/j.1600-0854.2011.01239.x;
Lupo D., Vollmer C., Deckers M., Mick D.U., Tews I., Sinning I.,
Rehling P.;
"Mdm38 is a 14-3-3-like receptor and associates with the protein
synthesis machinery at the inner mitochondrial membrane.";
Traffic 12:1457-1466(2011).
-!- FUNCTION: Involved in mitochondrial potassium homeostasis through
the mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266,
PubMed:15138253). With MBA1, plays a role in ribosomal translation
and protein insertion into the inner membrane (PubMed:20427570).
{ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:15138253,
ECO:0000269|PubMed:20427570}.
-!- SUBUNIT: Interacts with MBA1. Binds to mitoribosomes in order to
recruit them to the mitochondrial inner membrane.
{ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:21718401}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:15138253}; Single-pass membrane protein
{ECO:0000255}.
-!- DOMAIN: The matrix-exposed C-terminus contains a 14-3-3-like
domain which is necessary and sufficient for interaction with
mitochondrial ribosomes. {ECO:0000269|PubMed:21718401}.
-!- DISRUPTION PHENOTYPE: Leads to the absence of respiratory
complexes III and IV in mitochondrial inner membrane when MBA1 is
also missing. {ECO:0000269|PubMed:20427570}.
-!- MISCELLANEOUS: Present with 7390 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Z74769; CAA99027.1; -; Genomic_DNA.
EMBL; BK006948; DAA10754.1; -; Genomic_DNA.
PIR; S66710; S66710.
RefSeq; NP_014615.1; NM_001183281.1.
PDB; 3SKQ; X-ray; 2.10 A; A=160-408.
PDBsum; 3SKQ; -.
ProteinModelPortal; Q08179; -.
SMR; Q08179; -.
BioGrid; 34373; 277.
IntAct; Q08179; 2.
STRING; 4932.YOL027C; -.
TCDB; 2.A.97.1.2; the mitochondrial inner membrane k(+)/h(+) and ca(2+)/h(+) exchanger (letm1) family.
iPTMnet; Q08179; -.
MaxQB; Q08179; -.
PaxDb; Q08179; -.
PRIDE; Q08179; -.
TopDownProteomics; Q08179; -.
EnsemblFungi; YOL027C; YOL027C; YOL027C.
GeneID; 854130; -.
KEGG; sce:YOL027C; -.
EuPathDB; FungiDB:YOL027C; -.
SGD; S000005387; MDM38.
GeneTree; ENSGT00390000011225; -.
HOGENOM; HOG000195427; -.
InParanoid; Q08179; -.
KO; K17800; -.
OMA; MFKNDTV; -.
OrthoDB; EOG092C2EMR; -.
BioCyc; YEAST:G3O-33443-MONOMER; -.
PRO; PR:Q08179; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0043022; F:ribosome binding; IDA:SGD.
GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:SGD.
GO; GO:0070131; P:positive regulation of mitochondrial translation; IGI:SGD.
GO; GO:0006813; P:potassium ion transport; IMP:SGD.
GO; GO:0051204; P:protein insertion into mitochondrial membrane; IMP:SGD.
GO; GO:1902600; P:proton transmembrane transport; IGI:SGD.
InterPro; IPR011685; LETM1.
InterPro; IPR033122; LETM1_RBD.
Pfam; PF07766; LETM1; 1.
PROSITE; PS51758; LETM1_RBD; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Membrane; Mitochondrion;
Mitochondrion inner membrane; Reference proteome; Transit peptide;
Transmembrane; Transmembrane helix.
TRANSIT 1 56 Mitochondrion. {ECO:0000255}.
CHAIN 57 573 Mitochondrial distribution and morphology
protein 38.
/FTId=PRO_0000017697.
TOPO_DOM 57 138 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 573 Mitochondrial matrix. {ECO:0000255}.
DOMAIN 182 404 Letm1 RBD. {ECO:0000255|PROSITE-
ProRule:PRU01094}.
COILED 408 440 {ECO:0000255}.
COILED 503 541 {ECO:0000255}.
COMPBIAS 423 552 Glu-rich.
HELIX 183 198 {ECO:0000244|PDB:3SKQ}.
HELIX 206 208 {ECO:0000244|PDB:3SKQ}.
HELIX 212 226 {ECO:0000244|PDB:3SKQ}.
STRAND 234 237 {ECO:0000244|PDB:3SKQ}.
HELIX 238 245 {ECO:0000244|PDB:3SKQ}.
HELIX 250 256 {ECO:0000244|PDB:3SKQ}.
HELIX 259 268 {ECO:0000244|PDB:3SKQ}.
HELIX 277 301 {ECO:0000244|PDB:3SKQ}.
HELIX 303 305 {ECO:0000244|PDB:3SKQ}.
HELIX 308 317 {ECO:0000244|PDB:3SKQ}.
HELIX 327 342 {ECO:0000244|PDB:3SKQ}.
HELIX 348 355 {ECO:0000244|PDB:3SKQ}.
HELIX 356 358 {ECO:0000244|PDB:3SKQ}.
STRAND 359 361 {ECO:0000244|PDB:3SKQ}.
STRAND 368 371 {ECO:0000244|PDB:3SKQ}.
HELIX 373 376 {ECO:0000244|PDB:3SKQ}.
STRAND 378 380 {ECO:0000244|PDB:3SKQ}.
HELIX 383 401 {ECO:0000244|PDB:3SKQ}.
TURN 405 407 {ECO:0000244|PDB:3SKQ}.
SEQUENCE 573 AA; 65005 MW; 5F34453EC009F311 CRC64;
MLNFASRASC VTRRQASLYF VKNQGPRLIA STIPSCHWPL RAQGVQPNYP LSLRFYSTDK
SKSVTKPVAP TSTDAPAKPK ETLMVKVKHA LKHYANGTKL LGYEIKVSTK LLIKFAQGYE
LSRRERNQLR RTMGDVFRLI PFSAFLIIPF AELFLPFALK LFPNLLPSTY ESGKDKQAKR
NKLIEIRKKT SEFLHETLEE SNLITYNTIE NAEKKQKFLN FFRKLYSAKE GKIMTFQHDE
ISAIAQMFKN DSVLDNLSRP QLAAMSKFMS LRPFGNDNML RYQIRSKLKD IMNDDKTIDY
EGVESLSQEE LYQACVSRGM KAYGVSKEDL VDNLKVWLEL RLRQKIPSVL MVLSSTFTFG
GLPKENYSKA FSPLAEKKET KSKYDDLLDL YYDGILQVLS SIPDPVYNVA KLDVSESKSS
AAETEAEKQV AEKKIKTEEK PEETAIPKEE ATAKESVIAT TASAVTPKLV VVNEKAETAK
TEEISQEKEN AEPTDSAEAT EAEEKKTSDD NEFKLNVLKE QEELIKKEEE EAKQRASREH
VPDDINLDEE EEAKSVPPIP ADQAAKTFVI KKD


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