MDM34_TALSN
ID MDM34_TALSN Reviewed; 564 AA.
AC B8MKT9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
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}; ORFNames=TSTA_044050;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962657; EED14938.1; -; Genomic_DNA.
DR RefSeq; XP_002484891.1; XM_002484846.1.
DR AlphaFoldDB; B8MKT9; -.
DR STRING; 441959.B8MKT9; -.
DR EnsemblFungi; EED14938; EED14938; TSTA_044050.
DR GeneID; 8097913; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR InParanoid; B8MKT9; -.
DR OrthoDB; 1120952at2759; -.
DR Proteomes; UP000001745; 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..564
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384365"
FT DOMAIN 1..208
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 208..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 61863 MW; 60FE2F47A4D43B98 CRC64;
MAFNFNWSPL MADAGFYTRA QDLLTAALNK SPKPPIIVDD IKVTELNLGS IPPDLEILEV
GDLAEDRFRG IFKMSYNGDA FLTLKTRVQA NPLNTFLVTR PSFASPKPLA AAAGLTIPLQ
ITLSEFRLSG FVVLVFSKQK GITVVFRNDP LESLKVSSTF DSISFVRDYL QKAIEGQLRA
LFMDELPAII HRLSLRLWVP EYRDRESESV NTLDQSSGPG QDPLASPPQD PVDASGNALN
PSEVASLSLD SGVEIHSLFS QKNLLRLAAL TDSQRTLSLF TPSIKDVVYR AWTASTELGD
SNTLTSPASP VLSRAQSHIG SLHSFVDNAS TISMQSGGSS NFSGHGLNLR SGRHPRPHGK
KRKKRVVDLR RPKTTDDMES VSGESVFSSE NATSAPTIFS SPAQFSEEKN DDPVTPPLAP
QNDLHLPTIH ERRRISQGEH TLTRRSVPSM SEVAQPSSSR NSAAMIADTW PDPDATPRNS
IRLPSSDRAN NPLTTAHLPS SAIQYPPPIP DNNDPRQQAW LSKMAAELAR RIQEEKVGPS
GSRPFPDFWD DHSREEIPPP AYGH
