MDM12_COCIM
ID MDM12_COCIM Reviewed; 446 AA.
AC Q1E2F1; J3KB73;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Mitochondrial distribution and morphology protein 12 {ECO:0000255|HAMAP-Rule:MF_03104};
DE AltName: Full=Mitochondrial inheritance component MDM12 {ECO:0000255|HAMAP-Rule:MF_03104};
GN Name=MDM12 {ECO:0000255|HAMAP-Rule:MF_03104}; ORFNames=CIMG_03262;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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. MDM12
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. The MDM12-MMM1 subcomplex functions in the major beta-barrel
CC assembly pathway that is responsible for biogenesis of all
CC mitochondrial outer membrane beta-barrel proteins, and acts in a late
CC step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further
CC acts in the TOM40-specific pathway after the action of the MDM12-MMM1
CC complex. Essential for establishing and maintaining the structure of
CC mitochondria and maintenance of mtDNA nucleoids. {ECO:0000255|HAMAP-
CC Rule:MF_03104}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1
CC homodimer associates with one molecule of MDM12 on each side in a
CC pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12
CC generate a continuous hydrophobic tunnel for phospholipid trafficking.
CC {ECO:0000255|HAMAP-Rule:MF_03104}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03104}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03104}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03104}.
CC Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03104};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03104};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03104}. Note=The ERMES/MDM
CC complex localizes to a few discrete foci (around 10 per single cell),
CC that represent mitochondria-endoplasmic reticulum junctions. These foci
CC are often found next to mtDNA nucleoids. {ECO:0000255|HAMAP-
CC Rule:MF_03104}.
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_03104}.
CC -!- SIMILARITY: Belongs to the MDM12 family. {ECO:0000255|HAMAP-
CC Rule:MF_03104}.
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DR EMBL; GG704916; EAS32238.3; -; Genomic_DNA.
DR RefSeq; XP_001243821.1; XM_001243820.2.
DR AlphaFoldDB; Q1E2F1; -.
DR STRING; 246410.Q1E2F1; -.
DR PRIDE; Q1E2F1; -.
DR EnsemblFungi; EAS32238; EAS32238; CIMG_03262.
DR GeneID; 4564643; -.
DR KEGG; cim:CIMG_03262; -.
DR VEuPathDB; FungiDB:CIMG_03262; -.
DR InParanoid; Q1E2F1; -.
DR OMA; KRAHFCF; -.
DR OrthoDB; 1179924at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; 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 GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03104; Mdm12; 1.
DR InterPro; IPR027532; Mdm12.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR28204; PTHR28204; 1.
DR Pfam; PF10296; MMM1; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome; Transport.
FT CHAIN 1..446
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000384283"
FT DOMAIN 1..446
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 75..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49598 MW; 44E497B0918DD6FB CRC64;
MSIDINWEAA TSGPDGEALA ERIRSFIHDK FQQIALPRFI RSVEVNSFDF GTIKPELQIK
DLCDPFEDFY EEDEDNEIGD GEVSDIQDRS PKPRPSSAGN ERSAADAWQA EHPAFLDDRL
CGRIEPHDVP IPSKEDPLAS RPIRSPMSFG DPLNPYFFPR AGTPGIPGGT SNLGYYYMPL
GGISGTQTPL SSVPRGPFSP GLRDASVFGE PSNSQRPNPS GPARRQSEID IDTGNSRPST
ADTLDSLNIH GIPDPVLPRS SDDAHPNVLP RRDNSPAPRR VREKRPEDLQ VLCRLRYNGN
IRLSLTALVL LDYPMPNFVG LPLKLNITGL TFDGVAVVAY IRKRVHFCFL SPEDADTLFG
ADDTNEAGHL QSRDSLAGGI NDTSYSSRRP HDSLLRDVRV ESEIGRKEDG KQVLKNVGKV
EKFVLEQVRR IFEEEFVYPS FWTFLV
