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Mitochondrial distribution and morphology protein 35

 MDM35_YEAST             Reviewed;          86 AA.
O60200; D6VXN4; Q6Q599;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
12-SEP-2018, entry version 138.
RecName: Full=Mitochondrial distribution and morphology protein 35;
Name=MDM35; OrderedLocusNames=YKL053C-A;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091862; DOI=10.1002/yea.320100008;
Rasmussen S.W.;
"Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1
and TOA2 genes, an open reading frame (ORF) similar to a
translationally controlled tumour protein, one ORF containing motifs
also found in plant storage proteins and 13 ORFs with weak or no
homology to known proteins.";
Yeast 10:S63-S68(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
IDENTIFICATION.
PubMed=9392081;
DOI=10.1002/(SICI)1097-0061(199711)13:14<1363::AID-YEA182>3.0.CO;2-8;
Andrade M.A., Daruvar A., Casari G., Schneider R., Termier M.,
Sander C.;
"Characterization of new proteins found by analysis of short open
reading frames from the full yeast genome.";
Yeast 13:1363-1374(1997).
[6]
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).
[7]
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).
[8]
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).
[9]
SUBCELLULAR LOCATION.
PubMed=17095012; DOI=10.1016/j.jmb.2006.10.038;
Gabriel K., Milenkovic D., Chacinska A., Mueller J., Guiard B.,
Pfanner N., Meisinger C.;
"Novel mitochondrial intermembrane space proteins as substrates of the
MIA import pathway.";
J. Mol. Biol. 365:612-620(2007).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UPS1; UPS2 AND
UPS3.
PubMed=20622808; DOI=10.1038/emboj.2010.149;
Tamura Y., Iijima M., Sesaki H.;
"Mdm35p imports Ups proteins into the mitochondrial intermembrane
space by functional complex formation.";
EMBO J. 29:2875-2887(2010).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UPS1 AND UPS2.
PubMed=20657548; DOI=10.1038/emboj.2010.169;
Potting C., Wilmes C., Engmann T., Osman C., Langer T.;
"Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins
depends on proteolysis and Mdm35.";
EMBO J. 29:2888-2898(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=22984289; DOI=10.1074/mcp.M112.021105;
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
"Intermembrane space proteome of yeast mitochondria.";
Mol. Cell. Proteomics 11:1840-1852(2012).
[13]
FUNCTION.
PubMed=26071602; DOI=10.15252/embr.201540229;
Miliara X., Garnett J.A., Tatsuta T., Abid Ali F., Baldie H.,
Perez-Dorado I., Simpson P., Yague E., Langer T., Matthews S.;
"Structural insight into the TRIAP1/PRELI-like domain family of
mitochondrial phospholipid transfer complexes.";
EMBO Rep. 16:824-835(2015).
[14]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-75 IN COMPLEX WITH UPS1,
INTERACTION WITH UPS1, AND DISULFIDE BONDS.
PubMed=26071601; DOI=10.15252/embr.201540137;
Yu F., He F., Yao H., Wang C., Wang J., Li J., Qi X., Xue H., Ding J.,
Zhang P.;
"Structural basis of intramitochondrial phosphatidic acid transport
mediated by Ups1-Mdm35 complex.";
EMBO Rep. 16:813-823(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-81 IN COMPLEX WITH UPS1,
INTERACTION WITH UPS1 AND UPS2, DISULFIDE BONDS, AND MUTAGENESIS OF
PHE-24; TRP-27; TYR-28 AND PHE-32.
PubMed=26235513; DOI=10.1038/ncomms8922;
Watanabe Y., Tamura Y., Kawano S., Endo T.;
"Structural and mechanistic insights into phospholipid transfer by
Ups1-Mdm35 in mitochondria.";
Nat. Commun. 6:7922-7922(2015).
-!- FUNCTION: Involved in mitochondrial distribution and morphology.
Mediates the import of UPS1, UPS2 and UPS3, 3 atypical
mitochondrial intermembrane space (IMS) proteins lacking the two
major IMS-targeting signals, into the intermembrane space. The
UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA)
between liposomes and probably functions as a PA transporter
across the mitochondrion intermembrane space (PubMed:26071602,
PubMed:26071601, PubMed:26235513). Phosphatidic acid import is
required for cardiolipin (CL) synthesis in the mitochondrial inner
membrane (PubMed:26071602). {ECO:0000269|PubMed:11907266,
ECO:0000269|PubMed:20622808, ECO:0000269|PubMed:20657548,
ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26071602,
ECO:0000269|PubMed:26235513}.
-!- SUBUNIT: Interacts with UPS1, UPS2 and UPS3.
{ECO:0000269|PubMed:20622808, ECO:0000269|PubMed:20657548,
ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26235513}.
-!- INTERACTION:
Q05776:UPS1; NbExp=5; IntAct=EBI-2080774, EBI-30337;
P35200:UPS2; NbExp=5; IntAct=EBI-2080774, EBI-11337;
Q04006:UPS3; NbExp=3; IntAct=EBI-2080774, EBI-3830982;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane
space {ECO:0000269|PubMed:17095012, ECO:0000269|PubMed:20622808,
ECO:0000269|PubMed:20657548, ECO:0000269|PubMed:22984289}.
-!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TRIAP1/MDM35 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Z28054; CAA81891.1; -; Genomic_DNA.
EMBL; Z28052; CAA81889.1; -; Genomic_DNA.
EMBL; AY558262; AAS56588.1; -; Genomic_DNA.
EMBL; BK006944; DAA09104.1; -; Genomic_DNA.
RefSeq; NP_012870.1; NM_001184336.1.
PDB; 4XHR; X-ray; 2.55 A; M/N=1-86.
PDB; 4XIZ; X-ray; 2.00 A; M/N=6-75.
PDB; 4YTV; X-ray; 1.45 A; A=1-81.
PDB; 4YTW; X-ray; 1.40 A; A/C=1-81.
PDB; 4YTX; X-ray; 3.20 A; A/C/E/G/I/K/M/O=1-81.
PDB; 5JQL; X-ray; 2.90 A; B/D/F/H/J/L=1-86.
PDB; 5JQM; X-ray; 1.50 A; A/B/C=1-86.
PDB; 5JQO; X-ray; 3.55 A; A/C=1-86.
PDBsum; 4XHR; -.
PDBsum; 4XIZ; -.
PDBsum; 4YTV; -.
PDBsum; 4YTW; -.
PDBsum; 4YTX; -.
PDBsum; 5JQL; -.
PDBsum; 5JQM; -.
PDBsum; 5JQO; -.
ProteinModelPortal; O60200; -.
SMR; O60200; -.
BioGrid; 34080; 401.
IntAct; O60200; 3.
MINT; O60200; -.
STRING; 4932.YKL053C-A; -.
MaxQB; O60200; -.
PaxDb; O60200; -.
PRIDE; O60200; -.
EnsemblFungi; YKL053C-A; YKL053C-A; YKL053C-A.
GeneID; 853812; -.
KEGG; sce:YKL053C-A; -.
EuPathDB; FungiDB:YKL053C-A; -.
SGD; S000007243; MDM35.
GeneTree; ENSGT00390000010642; -.
HOGENOM; HOG000230782; -.
InParanoid; O60200; -.
KO; K17968; -.
OMA; ECTPLKR; -.
OrthoDB; EOG092C5W2N; -.
BioCyc; YEAST:G3O-32092-MONOMER; -.
Reactome; R-SCE-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
PRO; PR:O60200; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:0045332; P:phospholipid translocation; IDA:SGD.
GO; GO:0015914; P:phospholipid transport; IDA:SGD.
InterPro; IPR007918; MDM35_apoptosis.
Pfam; PF05254; UPF0203; 1.
PROSITE; PS51808; CHCH; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Disulfide bond;
Lipid transport; Mitochondrion; Nucleus; Reference proteome;
Transport.
CHAIN 1 86 Mitochondrial distribution and morphology
protein 35.
/FTId=PRO_0000220526.
DOMAIN 10 60 CHCH. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
MOTIF 13 23 Cx9C motif 1. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
MOTIF 42 52 Cx9C motif 2. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
DISULFID 13 52 {ECO:0000244|PDB:4XHR,
ECO:0000244|PDB:4XIZ,
ECO:0000244|PDB:4YTV,
ECO:0000244|PDB:4YTW,
ECO:0000244|PDB:4YTX,
ECO:0000255|PROSITE-ProRule:PRU01150,
ECO:0000269|PubMed:26071601,
ECO:0000269|PubMed:26235513}.
DISULFID 23 42 {ECO:0000244|PDB:4XHR,
ECO:0000244|PDB:4XIZ,
ECO:0000244|PDB:4YTV,
ECO:0000244|PDB:4YTW,
ECO:0000244|PDB:4YTX,
ECO:0000255|PROSITE-ProRule:PRU01150,
ECO:0000269|PubMed:26071601,
ECO:0000269|PubMed:26235513}.
MUTAGEN 24 24 F->A: Impairs interaction with UPS1 and
UPS2; when associated with A-27 and A-28.
{ECO:0000269|PubMed:26235513}.
MUTAGEN 27 27 W->A: Impairs interaction with UPS1 and
UPS2; when associated with A-24 and A-28.
{ECO:0000269|PubMed:26235513}.
MUTAGEN 28 28 Y->A: Impairs interaction with UPS1 and
UPS2; when associated with A-24 and A-27.
{ECO:0000269|PubMed:26235513}.
MUTAGEN 32 32 F->A: Impairs interaction with UPS1 and
UPS2. {ECO:0000269|PubMed:26235513}.
HELIX 4 9 {ECO:0000244|PDB:4YTV}.
HELIX 11 13 {ECO:0000244|PDB:4YTW}.
HELIX 14 30 {ECO:0000244|PDB:4YTW}.
TURN 31 35 {ECO:0000244|PDB:4YTW}.
HELIX 43 57 {ECO:0000244|PDB:4YTW}.
HELIX 63 70 {ECO:0000244|PDB:4YTW}.
SEQUENCE 86 AA; 9712 MW; 3DFEA08927BB8D10 CRC64;
MGNIMSASFA PECTDLKTKY DSCFNEWYSE KFLKGKSVEN ECSKQWYAYT TCVNAALVKQ
GIKPALDEAR EEAPFENGGK LKEVDK


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