ID   TM242_XENLA             Reviewed;         145 AA.
AC   Q63ZZ0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Transmembrane protein 242 {ECO:0000250|UniProtKB:Q9NWH2};
GN   Name=tmem242 {ECO:0000250|UniProtKB:Q9NWH2};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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   -!- 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; BC082742; AAH82742.1; -; mRNA.
DR   RefSeq; NP_001088020.1; NM_001094551.1.
DR   AlphaFoldDB; Q63ZZ0; -.
DR   DNASU; 494711; -.
DR   GeneID; 494711; -.
DR   KEGG; xla:494711; -.
DR   CTD; 494711; -.
DR   Xenbase; XB-GENE-6077997; tmem242.S.
DR   OrthoDB; 1365284at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 494711; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009792; TMEM242.
DR   PANTHER; PTHR13141; PTHR13141; 1.
DR   Pfam; PF07096; DUF1358; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..145
FT                   /note="Transmembrane protein 242"
FT                   /id="PRO_0000295852"
FT   TOPO_DOM        1..25
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..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..145
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
SQ   SEQUENCE   145 AA;  15765 MW;  34F9BF0A7191CF69 CRC64;
     MGTQKALNEQ SLTSETDTGR REEKLFLIKG GIFLGMVATA GMFAGFGTTL SLAKKRSPNW
     FNKGVAATAT LPESGSSLAL RALGWGSLYA WCGVGLISFA VWKALGVHSL KDFREKMQTI
     FPTVSKDPEH QPTSEFSFED LLKSK