MDM35_YEAST
ID MDM35_YEAST Reviewed; 86 AA.
AC O60200; D6VXN4; Q6Q599;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial distribution and morphology protein 35;
GN Name=MDM35; OrderedLocusNames=YKL053C-A;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION.
RX PubMed=9392081;
RX DOI=10.1002/(sici)1097-0061(199711)13:14<1363::aid-yea182>3.0.co;2-8;
RA Andrade M.A., Daruvar A., Casari G., Schneider R., Termier M., Sander C.;
RT "Characterization of new proteins found by analysis of short open reading
RT frames from the full yeast genome.";
RL Yeast 13:1363-1374(1997).
RN [6]
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 [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17095012; DOI=10.1016/j.jmb.2006.10.038;
RA Gabriel K., Milenkovic D., Chacinska A., Mueller J., Guiard B., Pfanner N.,
RA Meisinger C.;
RT "Novel mitochondrial intermembrane space proteins as substrates of the MIA
RT import pathway.";
RL J. Mol. Biol. 365:612-620(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UPS1; UPS2 AND UPS3.
RX PubMed=20622808; DOI=10.1038/emboj.2010.149;
RA Tamura Y., Iijima M., Sesaki H.;
RT "Mdm35p imports Ups proteins into the mitochondrial intermembrane space by
RT functional complex formation.";
RL EMBO J. 29:2875-2887(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UPS1 AND UPS2.
RX PubMed=20657548; DOI=10.1038/emboj.2010.169;
RA Potting C., Wilmes C., Engmann T., Osman C., Langer T.;
RT "Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins
RT depends on proteolysis and Mdm35.";
RL EMBO J. 29:2888-2898(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [13]
RP FUNCTION.
RX PubMed=26071602; DOI=10.15252/embr.201540229;
RA Miliara X., Garnett J.A., Tatsuta T., Abid Ali F., Baldie H.,
RA Perez-Dorado I., Simpson P., Yague E., Langer T., Matthews S.;
RT "Structural insight into the TRIAP1/PRELI-like domain family of
RT mitochondrial phospholipid transfer complexes.";
RL EMBO Rep. 16:824-835(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-75 IN COMPLEX WITH UPS1,
RP INTERACTION WITH UPS1, AND DISULFIDE BONDS.
RX PubMed=26071601; DOI=10.15252/embr.201540137;
RA Yu F., He F., Yao H., Wang C., Wang J., Li J., Qi X., Xue H., Ding J.,
RA Zhang P.;
RT "Structural basis of intramitochondrial phosphatidic acid transport
RT mediated by Ups1-Mdm35 complex.";
RL EMBO Rep. 16:813-823(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-81 IN COMPLEX WITH UPS1,
RP INTERACTION WITH UPS1 AND UPS2, DISULFIDE BONDS, AND MUTAGENESIS OF PHE-24;
RP TRP-27; TYR-28 AND PHE-32.
RX PubMed=26235513; DOI=10.1038/ncomms8922;
RA Watanabe Y., Tamura Y., Kawano S., Endo T.;
RT "Structural and mechanistic insights into phospholipid transfer by Ups1-
RT Mdm35 in mitochondria.";
RL Nat. Commun. 6:7922-7922(2015).
CC -!- FUNCTION: Involved in mitochondrial distribution and morphology.
CC Mediates the import of UPS1, UPS2 and UPS3, 3 atypical mitochondrial
CC intermembrane space (IMS) proteins lacking the two major IMS-targeting
CC signals, into the intermembrane space. The UPS1:MDM35 complex mediates
CC the transfer of phosphatidic acid (PA) between liposomes and probably
CC functions as a PA transporter across the mitochondrion intermembrane
CC space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic
CC acid import is required for cardiolipin (CL) synthesis in the
CC mitochondrial inner membrane (PubMed:26071602).
CC {ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:20622808,
CC ECO:0000269|PubMed:20657548, ECO:0000269|PubMed:26071601,
CC ECO:0000269|PubMed:26071602, ECO:0000269|PubMed:26235513}.
CC -!- SUBUNIT: Interacts with UPS1, UPS2 and UPS3.
CC {ECO:0000269|PubMed:20622808, ECO:0000269|PubMed:20657548,
CC ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26235513}.
CC -!- INTERACTION:
CC O60200; Q05776: UPS1; NbExp=5; IntAct=EBI-2080774, EBI-30337;
CC O60200; P35200: UPS2; NbExp=5; IntAct=EBI-2080774, EBI-11337;
CC O60200; Q04006: UPS3; NbExp=3; IntAct=EBI-2080774, EBI-3830982;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:17095012, ECO:0000269|PubMed:20622808,
CC ECO:0000269|PubMed:20657548, ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRIAP1/MDM35 family. {ECO:0000305}.
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DR EMBL; Z28054; CAA81891.1; -; Genomic_DNA.
DR EMBL; Z28052; CAA81889.1; -; Genomic_DNA.
DR EMBL; AY558262; AAS56588.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09104.1; -; Genomic_DNA.
DR RefSeq; NP_012870.1; NM_001184336.1.
DR PDB; 4XHR; X-ray; 2.55 A; M/N=1-86.
DR PDB; 4XIZ; X-ray; 2.00 A; M/N=6-75.
DR PDB; 4YTV; X-ray; 1.45 A; A=1-81.
DR PDB; 4YTW; X-ray; 1.40 A; A/C=1-81.
DR PDB; 4YTX; X-ray; 3.20 A; A/C/E/G/I/K/M/O=1-81.
DR PDB; 5JQL; X-ray; 2.90 A; B/D/F/H/J/L=1-86.
DR PDB; 5JQM; X-ray; 1.50 A; A/B/C=1-86.
DR PDB; 6KYL; X-ray; 3.55 A; A/C=1-86.
DR PDBsum; 4XHR; -.
DR PDBsum; 4XIZ; -.
DR PDBsum; 4YTV; -.
DR PDBsum; 4YTW; -.
DR PDBsum; 4YTX; -.
DR PDBsum; 5JQL; -.
DR PDBsum; 5JQM; -.
DR PDBsum; 6KYL; -.
DR AlphaFoldDB; O60200; -.
DR SMR; O60200; -.
DR BioGRID; 34080; 405.
DR IntAct; O60200; 3.
DR MINT; O60200; -.
DR STRING; 4932.YKL053C-A; -.
DR MaxQB; O60200; -.
DR PaxDb; O60200; -.
DR PRIDE; O60200; -.
DR EnsemblFungi; YKL053C-A_mRNA; YKL053C-A; YKL053C-A.
DR GeneID; 853812; -.
DR KEGG; sce:YKL053C-A; -.
DR SGD; S000007243; MDM35.
DR VEuPathDB; FungiDB:YKL053C-A; -.
DR eggNOG; KOG3481; Eukaryota.
DR GeneTree; ENSGT00940000176689; -.
DR HOGENOM; CLU_101473_2_0_1; -.
DR InParanoid; O60200; -.
DR OMA; KQWYAYT; -.
DR BioCyc; YEAST:G3O-32092-MON; -.
DR Reactome; R-SCE-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR PRO; PR:O60200; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; O60200; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IDA:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:SGD.
DR DisProt; DP02325; -.
DR InterPro; IPR007918; MDM35_apoptosis.
DR PANTHER; PTHR46403; PTHR46403; 1.
DR Pfam; PF05254; UPF0203; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Lipid transport; Mitochondrion;
KW Nucleus; Reference proteome; Transport.
FT CHAIN 1..86
FT /note="Mitochondrial distribution and morphology protein
FT 35"
FT /id="PRO_0000220526"
FT DOMAIN 10..60
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 13..23
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 42..52
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 13..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26235513,
FT ECO:0007744|PDB:4XHR, ECO:0007744|PDB:4XIZ,
FT ECO:0007744|PDB:4YTV, ECO:0007744|PDB:4YTW,
FT ECO:0007744|PDB:4YTX"
FT DISULFID 23..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000269|PubMed:26071601, ECO:0000269|PubMed:26235513,
FT ECO:0007744|PDB:4XHR, ECO:0007744|PDB:4XIZ,
FT ECO:0007744|PDB:4YTV, ECO:0007744|PDB:4YTW,
FT ECO:0007744|PDB:4YTX"
FT MUTAGEN 24
FT /note="F->A: Impairs interaction with UPS1 and UPS2; when
FT associated with A-27 and A-28."
FT /evidence="ECO:0000269|PubMed:26235513"
FT MUTAGEN 27
FT /note="W->A: Impairs interaction with UPS1 and UPS2; when
FT associated with A-24 and A-28."
FT /evidence="ECO:0000269|PubMed:26235513"
FT MUTAGEN 28
FT /note="Y->A: Impairs interaction with UPS1 and UPS2; when
FT associated with A-24 and A-27."
FT /evidence="ECO:0000269|PubMed:26235513"
FT MUTAGEN 32
FT /note="F->A: Impairs interaction with UPS1 and UPS2."
FT /evidence="ECO:0000269|PubMed:26235513"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:4YTV"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4YTW"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:4YTW"
FT TURN 31..35
FT /evidence="ECO:0007829|PDB:4YTW"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:4YTW"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:4YTW"
SQ SEQUENCE 86 AA; 9712 MW; 3DFEA08927BB8D10 CRC64;
MGNIMSASFA PECTDLKTKY DSCFNEWYSE KFLKGKSVEN ECSKQWYAYT TCVNAALVKQ
GIKPALDEAR EEAPFENGGK LKEVDK
