ID   MDM34_PICST             Reviewed;         523 AA.
AC   A3GFQ7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 65.
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=PICST_28329;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63393.2; -; Genomic_DNA.
DR   RefSeq; XP_001387416.2; XM_001387379.1.
DR   AlphaFoldDB; A3GFQ7; -.
DR   STRING; 4924.XP_001387416.2; -.
DR   PRIDE; A3GFQ7; -.
DR   EnsemblFungi; EAZ63393; EAZ63393; PICST_28329.
DR   GeneID; 4851106; -.
DR   KEGG; pic:PICST_28329; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_476594_0_0_1; -.
DR   InParanoid; A3GFQ7; -.
DR   OMA; PGCLERQ; -.
DR   OrthoDB; 999167at2759; -.
DR   Proteomes; UP000002258; 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..523
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384359"
FT   DOMAIN          1..200
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          489..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59731 MW;  01FD10B75C7EC90D CRC64;
     MSFKVNWKSL ETDSLTSWTK DLLTSALNSG KSPNILASSI SIKDLNFGKI APNFEILEIG
     ELGRDRFRGI FKINYEGDFH LTLHTNVQAN PLNIYYSNSM EKEIDSQFVT PNFLLSNEQF
     ALPLDLKLSD IKISGIGIIV FSKSKGLTLV FRNDPLDSIK VSSTFDTVQV LANFLQKQIE
     TQIRDLFRET LPTLIHQFSL KYLSLDNNSD DLHAHFASSS RTHSSALDPD NEFNNFTYSS
     KNLQKNLQLF NTRETLDLHI PKFKGIIQRS HLEKFTQNYP SLLNSLYLNL HEIDMKSYNT
     YNNNTGSNGI PIDLLINDKN FNRTNRVLKE ISDIQSNSFY KQSNNNKDTT VKPKRRRIKY
     STRKKAASPT STLINDDFHM ASLHSSVASS MPMSMSSSLS DSEERPQLLA QPRPMRISPD
     FYQAFLKSTP EQCWYQCKRV GLGTNYFNFA TSQPISTSPI KKDPARDFIK EKKSINYIDI
     NKVNNKLKEL SMDRSGKRKQ RNYGSATYES ENPIVAPPPP YSH