ID   MDM34_CHAGB             Reviewed;         537 AA.
AC   Q2H9Y1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=CHGG_02973;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC       molecular tether to connect the endoplasmic reticulum (ER) and
CC       mitochondria. Components of this complex are involved in the control of
CC       mitochondrial shape and protein biogenesis, and function in
CC       nonvesicular lipid trafficking between the ER and mitochondria. MDM34
CC       is required for the interaction of the ER-resident membrane protein
CC       MMM1 and the outer mitochondrial membrane-resident beta-barrel protein
CC       MDM10. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC       or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC       {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03105}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03105}. Note=The ERMES/MDM complex localizes to a few discrete
CC       foci (around 10 per single cell), that represent mitochondria-
CC       endoplasmic reticulum junctions. These foci are often found next to
CC       mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting that it
CC       resides in the membrane via beta-sheet conformations similar to those
CC       predicted for other outer membrane proteins and porin.
CC       {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC       various types of glycerophospholipids in its interior and mediate their
CC       transfer between two adjacent bilayers. {ECO:0000255|HAMAP-
CC       Rule:MF_03105}.
CC   -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03105}.
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DR   EMBL; CH408030; EAQ91038.1; -; Genomic_DNA.
DR   RefSeq; XP_001229489.1; XM_001229488.1.
DR   AlphaFoldDB; Q2H9Y1; -.
DR   SMR; Q2H9Y1; -.
DR   STRING; 38033.XP_001229489.1; -.
DR   EnsemblFungi; EAQ91038; EAQ91038; CHGG_02973.
DR   GeneID; 4389743; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_036502_1_0_1; -.
DR   InParanoid; Q2H9Y1; -.
DR   OMA; FKMSYAG; -.
DR   OrthoDB; 1120952at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03105; Mdm34; 1.
DR   InterPro; IPR027536; Mdm34.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR28185; PTHR28185; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Lipid-binding; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   CHAIN           1..537
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384336"
FT   DOMAIN          1..195
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          320..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  59330 MW;  8A613A4CDC44F98F CRC64;
     MAFNFNWSPL TADAGFYKRA RDLLTTALNK SPKPPIIVDD IIVTEFNLGS VPPDLEILEI
     GDLAEDRFRG IFKMCYSGDA FLTLKTRVQA NPLNTCLSAK PDFTSPQPLA AASSLTIPLQ
     ITLSEFKLSA FIILVFSKQK GLTIVFRNDP LESLKVSSTF DSIQFVRDYL QRTIEGKLRD
     LFMDELPAII HRLSLQLWCP DQIAKEDEEP KEADEHGVNP LATPPLDAVD LHGHLLDPAA
     ISELSLDGGP EAQLLFSQKT LLRLSDITNS QVTSSLDTSE TKDVLFRAWA GPDKVDLTNT
     TPLATPSLAR SYSYTSPHTY TFSDNGSQDQ GSLPSRPSLV HLNSATAGLS LGSGRHSKAG
     RKKKTRVVNL RRKAETEANS EEEEDTPETD SIEPPMSEPI MPHPILEESD EELASNKVHF
     GRSPDLQQQP RRPSFRAQAT NAPEVPVPSV ELGKTAVPPL QSSEKQAARF PSQDPAFVDS
     KTGRPRPRSD TSSVILEQAW IMKMAGEIAR RVYDEKNGNP TFWDDQDDTP PPAYEAR