ID   MDM34_NEUCR             Reviewed;         615 AA.
AC   Q7RZK9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   25-MAY-2022, entry version 82.
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=NCU00357, NCU20066;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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       mmm-1 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 mmm-1, 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; CM002238; EAA28592.3; -; Genomic_DNA.
DR   RefSeq; XP_957828.3; XM_952735.3.
DR   AlphaFoldDB; Q7RZK9; -.
DR   STRING; 5141.EFNCRP00000000211; -.
DR   EnsemblFungi; EAA28592; EAA28592; NCU00357.
DR   GeneID; 3873878; -.
DR   KEGG; ncr:NCU00357; -.
DR   VEuPathDB; FungiDB:NCU00357; -.
DR   HOGENOM; CLU_036502_1_0_1; -.
DR   InParanoid; Q7RZK9; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
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:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR   GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
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..615
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384351"
FT   DOMAIN          1..195
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          293..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  67733 MW;  66339DAFC8E6DA50 CRC64;
     MAFNFNWSPL TADAGFYERA RDLLTTALNK SPKPPIIVDD IFVTELNLGS VPPDLEILEI
     GDLAEDRFRG IFKMCYSGDA FLTLATRVQA NPLNTYISAK PSFTSPEPLT ASSSLTIPLQ
     ITLSEIKLSA FIILVFSKQK GLTIVFRNDP LESLKVSSTF DSIQFVRDYL QKTIEMKLRD
     LIMDELPAII HRLSLQLWCP DQVPKEDEEA KEESDAAINP LATPPLDAVD AHGHRLDPAE
     ISSLSLDGGP ETQSLFSQKN LEKMDALASA HRTSSLLTPN ILEVVFRAWA GQSDKPDATA
     TPASTPNLHR TSSYQGSVHT YTFSDNSSQA SGHALSRPTL VSMGSATTGL SLGSGRHSKA
     GRKKKMRVVN LRSKTAVSEP VSEIGSTSSQ AGDSHTEAST RTPMSEPVIP TTIREVPEDD
     LAASQSKVRF RPPTDATTSA RASESSGPRA AVPSVPVTAQ PSRATSSQEH VYTRQPSMFP
     SSPAPQTSAQ EMPPSYSSRV SEKAESTASI YADAKGQQQQ FQQQQQQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQQQQQWGR AGPQPDMSSV ILEQAWITKI AGEIARRVYD EKNRNPAFWE
     DSHQHDIPPP AYEPR