MDM34_UNCRE
ID MDM34_UNCRE Reviewed; 573 AA.
AC C4JQ45;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 51.
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=UREG_03278;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEP78432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476616; EEP78432.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002543761.1; XM_002543715.1.
DR AlphaFoldDB; C4JQ45; -.
DR STRING; 33188.XP_002543761.1; -.
DR EnsemblFungi; EEP78432; EEP78432; UREG_03278.
DR GeneID; 8442761; -.
DR KEGG; ure:UREG_03278; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR InParanoid; C4JQ45; -.
DR OrthoDB; 1120952at2759; -.
DR Proteomes; UP000002058; 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..573
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384366"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 301..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62088 MW; 3C6955D2A3495902 CRC64;
MAFNFNWSPL MADAGFYTRA QDLLTAALNK SPKPPIIVDD IAVTELNLGS IPPELEILEV
GDLAEDRFRG IFKMSYSGDA FLTLKTRVQA NPLNTFLITR PAYASPKPLA AASGLTIPLQ
ITLSNFRLSG FVVLVFSKQK GITVVFRNDP LESLKVSSTF DSIPSVRDYL QREIEGQLRI
LFMDELPAII HRLSLRLWVP EYRGLEAGIP ETAIPSSLGP GEDTLLNPPK DPVDASGNLL
SSAEIASLSL DSGVEMHSLF SQKNLLRLAA LTNSQRTLSL FTPSIREVMF RARTGLADQG
EGLGSGLMSP GSPALSRTHS HISSPLSSFQ DSSSVLSLQQ RSTTAASSFS GYGLSLGAGR
HTKARPTKKR KKRVVDLRKQ SKPTDPEITS ADGGYTETST ASTTFSSSTV PEEVNDDPVT
PPLSPETTIR FPNRQHRFST SEGKVIARAP AQQLTYSEPS HSALHTQTAN PVPAVPLHAE
GAAVPPQQAL VFGDEHLGSR EKSMEAQSSH GPNPGLSITD AAPNSSILEQ AWMMKMANEI
ARRIQEQNSL VNNNYPGPWE QTRARTPPPA YGQ
