MDM34_TALMQ
ID MDM34_TALMQ Reviewed; 565 AA.
AC B6QIB3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=PMAA_097010;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
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}.
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DR EMBL; DS995902; EEA23108.1; -; Genomic_DNA.
DR RefSeq; XP_002149275.1; XM_002149239.1.
DR AlphaFoldDB; B6QIB3; -.
DR STRING; 441960.B6QIB3; -.
DR EnsemblFungi; EEA23108; EEA23108; PMAA_097010.
DR GeneID; 7026818; -.
DR KEGG; tmf:PMAA_097010; -.
DR VEuPathDB; FungiDB:PMAA_097010; -.
DR HOGENOM; CLU_036502_1_0_1; -.
DR OrthoDB; 1120952at2759; -.
DR PhylomeDB; B6QIB3; -.
DR Proteomes; UP000001294; 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..565
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384356"
FT DOMAIN 1..208
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 209..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 62286 MW; C962DDCA6B933B33 CRC64;
MAFNFNWSPL MADAGFYTRA QDLLTAALNK SPKPPIIVDD IKVTELNLGS IPPDLEILEV
GDLAEDRFRG IFKMSYNGDA FLTLKTRVQA NPLNTFLVTR PSFASPKPLA AASGLTIPLQ
ITLSEFRLSG FVVLVFSKQK GITVVFRNDP LESLKVSSTF DSISFVRDYL QKAIEGQLRA
LFMDELPAII HRLSLRLWVP EYRDRESESV NTLDLSSESG PGQDPLASPP QDPVDASGNA
LNPSEVASLS LDSGVEIHNL FSHKNLLRLA ALTDSQRTLS LFTPSIKDVV YRAWTASAEL
GESNTLTSPT SPVLSRTHSH IGSLHSFVDN ASTISMQSGG SSNFSGFGSY LRPGRHSRSH
TKKRKKRVVD LRRPKTTDDV DSVSGDSVFS SENATSAPTI FSSPAHFSEE KNDDPVTPPL
GPQNDLHLPT IHERRRISQG DQTLRRSNLS MSEAAQPSSS RSAQMIAETW PDPDATPRNT
IRLPSNDRAS NRFTAVSLPS SAIQYTPTVP INNNNPREQV WLSKMAAELA RRMQEQKIDP
SGSRPFPDFW DDHSREEIPP PAYGH
