MDM34_CANDC
ID MDM34_CANDC Reviewed; 622 AA.
AC B9W824;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=CD36_05840;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992688; CAX44849.1; -; Genomic_DNA.
DR RefSeq; XP_002417248.1; XM_002417203.1.
DR AlphaFoldDB; B9W824; -.
DR SMR; B9W824; -.
DR STRING; 42374.XP_002417248.1; -.
DR EnsemblFungi; CAX44849; CAX44849; CD36_05840.
DR GeneID; 8044787; -.
DR KEGG; cdu:CD36_05840; -.
DR CGD; CAL0000169650; Cd36_05840.
DR VEuPathDB; FungiDB:CD36_05840; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_476594_0_0_1; -.
DR OrthoDB; 999167at2759; -.
DR Proteomes; UP000002605; 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; Transmembrane; Transmembrane beta strand;
KW Transport.
FT CHAIN 1..622
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384334"
FT DOMAIN 1..204
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 362..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 70418 MW; 9C7F7019F153A9B4 CRC64;
MSFKVNWNSL ETEPLTNWTK ELLTSALNSG KSPNILASNI TIKDLNFGKI APDFEILEIG
ELDRDRFRGI FKIDYQGDFH LTLHTKVQAN PLNIYYHNSL EKEVCNCTQD EFITPNFLLS
NEQFAIPLDL KLSDIKINGI GIIVFSKSKG LTLVFRNDPL DSIKVSSTFD TVQVLANFLQ
KQIENQIRDL FRETLPTLIH QLSLKYLSLD NNINEIKSKL SQQDSVSMTN NELASSLKLF
DDEENEFPLI YSSKNLQKNM QLFKSRETFR LSVPKFKNIV QRTRLDKFTK SYPNLLNSLY
ANNVDLQHRY VNNINHNNNN NASSTGIPIE LLLSHDDKQH YDKTDSLLKD ISSIQANNFY
KYSNKDAPTK PKRRRIKVHK KNKSKHDETT TTTSKPSELQ NVDNTFMESR SISPQETIDT
VSTLIESVPM TRNVSSNIKS PTLDTLSTGS SSAASSQVIA HPTPKRAYQP NDTTTAATTT
LNKENHIDYI KARNLYQDFI QMSQSPGYYD KVISNGGGIG LGNNNGGNYF GLERTISSSP
IKHLNKDKKS INYIDTSKIN EKLNQFRFDG GKNNNTNDNN SKNFRPGFTR NESNGQQGIL
FEAFNFPSMT AAATPPPPPP YC
