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MDM31_YEAST
ID   MDM31_YEAST             Reviewed;         579 AA.
AC   P38880; D3DLE2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Mitochondrial distribution and morphology protein 31;
DE   Flags: Precursor;
GN   Name=MDM31; OrderedLocusNames=YHR194W;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MDM32.
RX   PubMed=15631992; DOI=10.1083/jcb.200410030;
RA   Dimmer K.S., Jakobs S., Vogel F., Altmann K., Westermann B.;
RT   "Mdm31 and Mdm32 are inner membrane proteins required for maintenance of
RT   mitochondrial shape and stability of mitochondrial DNA nucleoids in
RT   yeast.";
RL   J. Cell Biol. 168:103-115(2005).
RN   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC   -!- FUNCTION: Involved in the organization of the mitochondrial membranes
CC       and the global structure of the mitochondria. Also required for
CC       mitochondrial distribution and mobility as well as for the maintenance
CC       of mitochondrial DNA nucleoids structures.
CC       {ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:15631992}.
CC   -!- SUBUNIT: Interacts with MDM32. Participates in a complex of about 600
CC       kDa. {ECO:0000269|PubMed:15631992}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15631992}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15631992}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MDM31/MDM32 family. {ECO:0000305}.
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DR   EMBL; U00030; AAB68358.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06886.1; -; Genomic_DNA.
DR   PIR; S46680; S46680.
DR   RefSeq; NP_012064.1; NM_001179325.1.
DR   AlphaFoldDB; P38880; -.
DR   BioGRID; 36628; 110.
DR   DIP; DIP-2828N; -.
DR   IntAct; P38880; 2.
DR   MINT; P38880; -.
DR   STRING; 4932.YHR194W; -.
DR   PaxDb; P38880; -.
DR   PRIDE; P38880; -.
DR   EnsemblFungi; YHR194W_mRNA; YHR194W; YHR194W.
DR   GeneID; 856601; -.
DR   KEGG; sce:YHR194W; -.
DR   SGD; S000001237; MDM31.
DR   VEuPathDB; FungiDB:YHR194W; -.
DR   eggNOG; ENOG502QQJG; Eukaryota.
DR   GeneTree; ENSGT00940000176498; -.
DR   HOGENOM; CLU_016236_2_1_1; -.
DR   InParanoid; P38880; -.
DR   OMA; IYSCELP; -.
DR   BioCyc; YEAST:G3O-31222-MON; -.
DR   PRO; PR:P38880; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38880; 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:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR   GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR   GO; GO:1900208; P:regulation of cardiolipin metabolic process; IGI:SGD.
DR   InterPro; IPR012571; Mdm31/Mdm32.
DR   PANTHER; PTHR31068; PTHR31068; 1.
DR   Pfam; PF08118; MDM31_MDM32; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..579
FT                   /note="Mitochondrial distribution and morphology protein
FT                   31"
FT                   /id="PRO_0000021664"
FT   TOPO_DOM        48..114
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..558
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        559..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        579
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   579 AA;  66703 MW;  4BB155D6D88BB826 CRC64;
     MSLFTRPFLR SPRQFSVARY VYWARSPALR SNLRIPSIAA ASLRAYSNES KTGRDAPPDK
     KSKKLSNLKY ITERDSLLVQ TNNIFTKLKI NIRWFLKKST RPFNSDDISA FISWILVSNI
     FIFIFWTTTF VSLILYLINT VFAQEYLASK IGKFITKNES LSIVFESAIV PDWSSGKISF
     QKVFVSRRPK VSRGFTKGSQ QDALQRAKLA LSERILVNQQ DFDNGNYTQF DLTIDQVDIS
     LNFRKWINGK GILDEVTING LRGVIDRTHV VWKKDDDPKN YLNVYQPGDF EISKFTMNDV
     LCTLYQPNGF RPFQVSIFNC DLPQLRKHWL FYDILNANNI NGTYDNSMFT IHKKFRTDDQ
     HQDPTLLWKQ MTRFRVDNLD IDHLNAGIEG PFGWINEGRV NMIGDVLLPD DDAASDSLQL
     TEILTEIGDR LIKKAKRYTS SLPLVGPGFS PAVDEIDPND YFIMDFSLRL YNVKAEVPLF
     TSGLTYINSA LIRPIVGYIN SHRTYIPIKC RIVKKKSDFE GSWTIYDSYL MRDLSAEAYD
     AFADYVADDE KRTLRLRRVG FWSLQLILQV ILMSLGAIA
 
 
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