MDM38_YEAST
ID MDM38_YEAST Reviewed; 573 AA.
AC Q08179; D6W238;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitochondrial distribution and morphology protein 38 {ECO:0000303|PubMed:11907266};
DE Flags: Precursor;
GN Name=MDM38 {ECO:0000303|PubMed:11907266}; OrderedLocusNames=YOL027C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
RA Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W.,
RA Westermann B.;
RT "Genetic basis of mitochondrial function and morphology in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:847-853(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15138253; DOI=10.1074/jbc.m403607200;
RA Nowikovsky K., Froschauer E.M., Zsurka G., Samaj J., Reipert S.,
RA Kolisek M., Wiesenberger G., Schweyen R.J.;
RT "The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+
RT homeostasis with a potential role in the Wolf-Hirschhorn syndrome.";
RL J. Biol. Chem. 279:30307-30315(2004).
RN [8]
RP BINDING TO MITORIBOSOMES, INTERACTION WITH MBA1, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=20427570; DOI=10.1091/mbc.e10-02-0101;
RA Bauerschmitt H., Mick D.U., Deckers M., Vollmer C., Funes S., Kehrein K.,
RA Ott M., Rehling P., Herrmann J.M.;
RT "Ribosome-binding proteins Mdm38 and Mba1 display overlapping functions for
RT regulation of mitochondrial translation.";
RL Mol. Biol. Cell 21:1937-1944(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 160-408, DOMAIN, AND BINDING TO
RP MITORIBOSOMES.
RX PubMed=21718401; DOI=10.1111/j.1600-0854.2011.01239.x;
RA Lupo D., Vollmer C., Deckers M., Mick D.U., Tews I., Sinning I.,
RA Rehling P.;
RT "Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis
RT machinery at the inner mitochondrial membrane.";
RL Traffic 12:1457-1466(2011).
CC -!- FUNCTION: Involved in mitochondrial potassium homeostasis through the
CC mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266,
CC PubMed:15138253). With MBA1, plays a role in ribosomal translation and
CC protein insertion into the inner membrane (PubMed:20427570).
CC {ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:15138253,
CC ECO:0000269|PubMed:20427570}.
CC -!- SUBUNIT: Interacts with MBA1. Binds to mitoribosomes in order to
CC recruit them to the mitochondrial inner membrane.
CC {ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:21718401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:15138253}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The matrix-exposed C-terminus contains a 14-3-3-like domain
CC which is necessary and sufficient for interaction with mitochondrial
CC ribosomes. {ECO:0000269|PubMed:21718401}.
CC -!- DISRUPTION PHENOTYPE: Leads to the absence of respiratory complexes III
CC and IV in mitochondrial inner membrane when MBA1 is also missing.
CC {ECO:0000269|PubMed:20427570}.
CC -!- MISCELLANEOUS: Present with 7390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74769; CAA99027.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10754.1; -; Genomic_DNA.
DR PIR; S66710; S66710.
DR RefSeq; NP_014615.1; NM_001183281.1.
DR PDB; 3SKQ; X-ray; 2.10 A; A=160-408.
DR PDBsum; 3SKQ; -.
DR AlphaFoldDB; Q08179; -.
DR SMR; Q08179; -.
DR BioGRID; 34373; 284.
DR IntAct; Q08179; 2.
DR STRING; 4932.YOL027C; -.
DR TCDB; 2.A.97.1.2; the mitochondrial inner membrane k(+)/h(+) and ca(2+)/h(+) exchanger (letm1) family.
DR iPTMnet; Q08179; -.
DR MaxQB; Q08179; -.
DR PaxDb; Q08179; -.
DR PRIDE; Q08179; -.
DR TopDownProteomics; Q08179; -.
DR EnsemblFungi; YOL027C_mRNA; YOL027C; YOL027C.
DR GeneID; 854130; -.
DR KEGG; sce:YOL027C; -.
DR SGD; S000005387; MDM38.
DR VEuPathDB; FungiDB:YOL027C; -.
DR eggNOG; KOG1043; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_008958_5_1_1; -.
DR InParanoid; Q08179; -.
DR OMA; HEVKHYV; -.
DR BioCyc; YEAST:G3O-33443-MON; -.
DR PRO; PR:Q08179; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08179; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:SGD.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:SGD.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IGI:SGD.
DR GO; GO:0006813; P:potassium ion transport; IMP:SGD.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IGI:SGD.
DR InterPro; IPR011685; LETM1-like.
DR InterPro; IPR044202; LETM1/MDM38-like.
DR InterPro; IPR033122; LETM1_RBD.
DR PANTHER; PTHR14009; PTHR14009; 2.
DR Pfam; PF07766; LETM1; 1.
DR PROSITE; PS51758; LETM1_RBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..573
FT /note="Mitochondrial distribution and morphology protein
FT 38"
FT /id="PRO_0000017697"
FT TOPO_DOM 57..138
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..573
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 182..404
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT REGION 417..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..440
FT /evidence="ECO:0000255"
FT COILED 503..541
FT /evidence="ECO:0000255"
FT COMPBIAS 418..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:3SKQ"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 277..301
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3SKQ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3SKQ"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:3SKQ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3SKQ"
FT HELIX 383..401
FT /evidence="ECO:0007829|PDB:3SKQ"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:3SKQ"
SQ 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
