MDM28_SCHPO
ID MDM28_SCHPO Reviewed; 485 AA.
AC O13920; P78769;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=LETM1 domain-containing protein mdm28, mitochondrial;
DE Flags: Precursor;
GN Name=mdm28; ORFNames=SPAC23C11.17;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-485.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in mitochondrial potassium homeostasis through the
CC mitochondrial K(+)/H(+) exchange regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB11168.1; -; Genomic_DNA.
DR EMBL; D89117; BAA13779.1; -; mRNA.
DR PIR; T38255; T38255.
DR PIR; T42226; T42226.
DR RefSeq; NP_593648.1; NM_001019079.2.
DR AlphaFoldDB; O13920; -.
DR SMR; O13920; -.
DR BioGRID; 278439; 1.
DR STRING; 4896.SPAC23C11.17.1; -.
DR MaxQB; O13920; -.
DR PaxDb; O13920; -.
DR EnsemblFungi; SPAC23C11.17.1; SPAC23C11.17.1:pep; SPAC23C11.17.
DR GeneID; 2541952; -.
DR KEGG; spo:SPAC23C11.17; -.
DR PomBase; SPAC23C11.17; mdm28.
DR VEuPathDB; FungiDB:SPAC23C11.17; -.
DR eggNOG; KOG1043; Eukaryota.
DR HOGENOM; CLU_008958_5_2_1; -.
DR InParanoid; O13920; -.
DR OMA; LSNAFMY; -.
DR PhylomeDB; O13920; -.
DR PRO; PR:O13920; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; ISO:PomBase.
DR InterPro; IPR011685; LETM1-like.
DR InterPro; IPR044202; LETM1/MDM38-like.
DR InterPro; IPR033122; LETM1_RBD.
DR PANTHER; PTHR14009; PTHR14009; 1.
DR Pfam; PF07766; LETM1; 1.
DR PROSITE; PS51758; LETM1_RBD; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..85
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 86..485
FT /note="LETM1 domain-containing protein mdm28,
FT mitochondrial"
FT /id="PRO_0000116675"
FT TOPO_DOM 86..173
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..485
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT DOMAIN 217..410
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT REGION 442..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 134
FT /note="K -> I (in Ref. 2; BAA13779)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="V -> G (in Ref. 2; BAA13779)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="D -> H (in Ref. 2; BAA13779)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="S -> P (in Ref. 2; BAA13779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55724 MW; 0EABBA137F329695 CRC64;
MKYPRTHIQF PSMLRNRLFK TPHQTGFQWR LGAPATGITI RNQPIRSYSG LRGNFLIDKR
LSPVKFNKYS PSDIVFYNIG SSRLYSTETP TPSKVKEAPK QVAAEETKPT TVVKKPSIWQ
RVKGGVLHFW DGTKLLGVEI KISSKLVYKM AVGYELTRRE SRQLTRTLKD IGRLVPFSVF
VVVPFAELLL PIAVKLFPNL LPSTFEDAKD KEAKKAQLRK TRNEVSNMLR STLKSGKFTF
SNETRESKEF RDFFQKVRTS GQSPSREELI EVCKYFKDDI TLDNLSRAQL VAMCRYMNLN
AFGTDPLLRY NIRHRMRQIR RDDRAIYIEG INSLSIPELF NACNSRGIRT QGLSPAKLKE
ELSVWLDMRI KHGIPSVILM LSNAFSYGYN EGTYDSRWDA LQDTLASIPD ELYHETVVDM
PTKQVSNKER LEILREQEEL IEEEAEHVAE HPDLAKKQTE ENKATSKPAV SAKSPESNIP
KNERK
