MDM12_SCHPO
ID MDM12_SCHPO Reviewed; 273 AA.
AC Q92377; P78933;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=SPBC28F2.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9024686; DOI=10.1083/jcb.136.3.545;
RA Berger K.H., Sogo L.F., Yaffe M.P.;
RT "Mdm12p, a component required for mitochondrial inheritance that is
RT conserved between budding and fission yeast.";
RL J. Cell Biol. 136:545-553(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K.,
RA Yanagida M.;
RT "S.pombe chromosome II cosmid 1228 sequence.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12181.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U64674; AAB17957.1; -; Genomic_DNA.
DR EMBL; D83992; BAA12181.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329671; CAB57935.1; -; Genomic_DNA.
DR PIR; T48693; T48693.
DR RefSeq; NP_595667.1; NM_001021562.2.
DR AlphaFoldDB; Q92377; -.
DR SMR; Q92377; -.
DR BioGRID; 277089; 16.
DR STRING; 4896.SPBC28F2.06c.1; -.
DR iPTMnet; Q92377; -.
DR MaxQB; Q92377; -.
DR PaxDb; Q92377; -.
DR PRIDE; Q92377; -.
DR EnsemblFungi; SPBC28F2.06c.1; SPBC28F2.06c.1:pep; SPBC28F2.06c.
DR GeneID; 2540562; -.
DR KEGG; spo:SPBC28F2.06c; -.
DR PomBase; SPBC28F2.06c; mdm12.
DR VEuPathDB; FungiDB:SPBC28F2.06c; -.
DR eggNOG; ENOG502S3PB; Eukaryota.
DR HOGENOM; CLU_026794_2_0_1; -.
DR InParanoid; Q92377; -.
DR OMA; AAWPSWI; -.
DR PhylomeDB; Q92377; -.
DR PRO; PR:Q92377; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0140474; F:mitochondrion-endoplasmic reticulum membrane tether activity; IC:PomBase.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; TAS:PomBase.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0007006; P:mitochondrial membrane organization; IC:PomBase.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
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; IPR031468; SMP_LBD.
DR PANTHER; PTHR28204; PTHR28204; 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..273
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000096328"
FT DOMAIN 1..273
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 30517 MW; 81324A7D4956FDD8 CRC64;
MSIDFDWSKL DSELEAKVLH LLEGQVSNLS LPSYIKHLKV VDFHFGKVSP QITIQEIGDP
DPQFYENEAF ELANQELEGD QCSRNNVSPV LTDLPPYAAE HPFSRLAYFN PAFNSPGILS
ASGLTSPIPE SRPSTPMDNH QERDRSNDFQ VTAHVSYDGD ANLSLEAVLS MNYPNSEFAV
LPFKLSFIRI SIDAIAVLAK MGKRTHLCFV DTLLHGTGEH ASSVIRDLTV ESIIGESNKQ
LLKNVAKVEK FVSEKVKRII EDELVWPSYI TIE
