MDM34_BOTFB
ID MDM34_BOTFB Reviewed; 563 AA.
AC A6S9E2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=BC1G_09322;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476900; EDN29825.1; -; Genomic_DNA.
DR RefSeq; XP_001552158.1; XM_001552108.1.
DR AlphaFoldDB; A6S9E2; -.
DR SMR; A6S9E2; -.
DR GeneID; 5432678; -.
DR KEGG; bfu:BCIN_07g05250; -.
DR VEuPathDB; FungiDB:Bcin07g05250; -.
DR OMA; FKMSYAG; -.
DR OrthoDB; 1120952at2759; -.
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; Transmembrane; Transmembrane beta strand;
KW Transport.
FT CHAIN 1..563
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384331"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 298..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 61775 MW; 80A94BAB8E342FD3 CRC64;
MAFNFNWSPL TADAEFYQRA QEMLTAALNK SPKPPIIKDD ILVNELNLGS VPPDLEILEI
GDLAEDRFRG IFKMCYSGDA FLTLKTRVQA NPLNNHLFSK PSFTSPQPLA ADAGLTIPLQ
ITLSDIKLSA FIIVVFSKSK GLTLVFRNDP LESLKVSSTF DSIPFIKDYL QKEIEQQLRT
LMMDELPAII HRLSLRLWCP EYRAKEDQEM AEAAKKTKDE VAVDPFASPP QDAVDARGNV
LDATEISNLS LDGGSEIHSL FSQKNLLRLA ALTNSHRTLS LFTPSIRDAV FRAWAPSERG
DSAGTTTPAT PSLQRPQSSL GSQSTTYTFS NRSSDDGHGG IPSRPSLVNM NSATTGLSLG
ANRGSRSHPT RKKKNRVVNL RKPKTTESSE SGESETASTT AVSEPTVPSR IPEEPEDLPV
TPPSGKVRFN SIDLGDSPKK LPPSRSMTPE QVKMDQIPSL TVQPSTPINT QEQKRPAYNQ
SASTSYTPEK SAITPPHTPF SYPHGLHFST TESPSGILEQ AWIMKMASEL ARRQHDDKTA
RQGFWSTSSN GDDAPPAYEP KAL
