ID   TM242_PONAB             Reviewed;         141 AA.
AC   Q5R987;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Transmembrane protein 242 {ECO:0000250|UniProtKB:Q9NWH2};
GN   Name=TMEM242 {ECO:0000250|UniProtKB:Q9NWH2};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Scaffold protein that participates in the c-ring assembly of
CC       mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by
CC       facilitating the membrane insertion and oligomer formation of the
CC       subunit c/ATP5MC3. Participates in the incorporation of the c-ring into
CC       vestigial complexes. Additionally influences the incorporation of
CC       subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase.
CC       {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- SUBUNIT: Interacts with the core subunits NDUFAF1, ECSIT and ACAD9 of
CC       the MCIA complex. Interacts with ATP5MC3, NDUFC2, TMEM70, MT-ND2 AND
CC       MT-ND3. {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9NWH2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- SIMILARITY: Belongs to the TMEM242 family. {ECO:0000305}.
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DR   EMBL; CR859504; CAH91673.1; -; mRNA.
DR   RefSeq; NP_001125980.1; NM_001132508.1.
DR   AlphaFoldDB; Q5R987; -.
DR   STRING; 9601.ENSPPYP00000019363; -.
DR   Ensembl; ENSPPYT00000020124; ENSPPYP00000019363; ENSPPYG00000017271.
DR   GeneID; 100172919; -.
DR   KEGG; pon:100172919; -.
DR   CTD; 729515; -.
DR   eggNOG; ENOG502S2GB; Eukaryota.
DR   GeneTree; ENSGT00390000008642; -.
DR   HOGENOM; CLU_115460_0_0_1; -.
DR   InParanoid; Q5R987; -.
DR   OMA; YAVMGTG; -.
DR   OrthoDB; 1298607at2759; -.
DR   TreeFam; TF323317; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IEA:Ensembl.
DR   InterPro; IPR009792; TMEM242.
DR   PANTHER; PTHR13141; PTHR13141; 1.
DR   Pfam; PF07096; DUF1358; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..141
FT                   /note="Transmembrane protein 242"
FT                   /id="PRO_0000295850"
FT   TOPO_DOM        1..29
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..81
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..141
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
SQ   SEQUENCE   141 AA;  14729 MW;  CA18CF01870E395E CRC64;
     METAGAGTGQ PASGLEAPGS ADDRLFLVKG GIFLGTVAAA GMLAGFITTL SLAKKKSPEW
     FNKGSMATAA LPESGSSLAL RALGWGSLYA WCGVGVISFA VWKALGVHSM KDFRSKMQSI
     FPTIPKNSES AVEWEETLKS K