ID   MDM34_KOMPG             Reviewed;         489 AA.
AC   C4QYM9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   OrderedLocusNames=PAS_chr1-4_0499;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392319; CAY68353.1; -; Genomic_DNA.
DR   RefSeq; XP_002490633.1; XM_002490588.1.
DR   AlphaFoldDB; C4QYM9; -.
DR   SMR; C4QYM9; -.
DR   STRING; 644223.C4QYM9; -.
DR   EnsemblFungi; CAY68353; CAY68353; PAS_chr1-4_0499.
DR   GeneID; 8197085; -.
DR   KEGG; ppa:PAS_chr1-4_0499; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_043692_0_0_1; -.
DR   InParanoid; C4QYM9; -.
DR   OMA; FRGIFKF; -.
DR   Proteomes; UP000000314; Chromosome 1.
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..489
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384358"
FT   DOMAIN          1..205
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
SQ   SEQUENCE   489 AA;  55869 MW;  BDF71A1917DB41BF CRC64;
     MSFNINWDSI QKESLSAWTA ELLNDALNSG KRPNVLCTDI QIEDLSFGTI PPDFEILEIG
     DLSSDSFRGI FKFNYDGDAS ITLRTKVQAN PLKIYEDNLL DQFEDDQREL GEFIKPRFVM
     ATDILEIPLN LKLSQIKLSS IIIIVFSRSK GLTLVFKNDP LESISVSSTF DRIKPLARFL
     QNKIETQISE LFKEFLPSVL YKFSQKYTTE NFADFHRELL HTQHPERNTE NRVTLQDIDP
     EAPLIISPGS LMRLTTLSSS RQTLTLGGKI SADKLNPDII TKNYFNELIP KTYNKFQLKA
     DKVADIAQNI HSIKNLQSRI FWKNSKNNDK PHRRVVCLGD KDKSKEKCKQ VESESLYRRS
     VYSQGSIFND GASDVSTLTE STEVEQEAPN TEFPKLQAVD LKPDMSVETI IQNSSQEKHR
     KVKPIDDIGL IGRRKERLRE LLKYDVVDFS MPPMPGSPTK FFNTNIFHDS NHINNGNLPI
     RVAPPPYQC