ID   TMM70_BOVIN             Reviewed;         254 AA.
AC   A6H773;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Transmembrane protein 70, mitochondrial {ECO:0000250|UniProtKB:Q9BUB7};
DE   Flags: Precursor;
GN   Name=TMEM70 {ECO:0000250|UniProtKB:Q9BUB7};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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/ATP5MC1 through its interaction. Therefore, participates in
CC       the early stage of mitochondrial ATP synthase biogenesis and also
CC       protects subunit c/ATP5MC1 against intramitochondrial proteolysis. In
CC       addition, binds the mitochondrial proton-transporting ATP synthase
CC       complexes I and may play a role in the stability of its membrane-bound
CC       subassemblies. {ECO:0000250|UniProtKB:Q9BUB7}.
CC   -!- SUBUNIT: Homooligomer. Interacts (homooligomer form) with ATP5MC1; this
CC       interaction facilitates the oligomer formation of subunit c/ATP5MC1 (c-
CC       ring) and the c-ring membrane insertion and also protects ATP5MC1
CC       against intramitochondrial proteolysis. Interacts with the core
CC       subunits TMEM126B, NDUFAF1, ECSIT and ACAD9 of the MCIA complex.
CC       Interacts with ATP5MC3, TMEM242 AND TIMMDC1.
CC       {ECO:0000250|UniProtKB:Q9BUB7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9BUB7}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9BUB7}. Note=Mostly located within the inner
CC       cristae membrane. {ECO:0000250|UniProtKB:Q9BUB7}.
CC   -!- SIMILARITY: Belongs to the TMEM70 family. {ECO:0000305}.
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DR   EMBL; BC146138; AAI46139.1; -; mRNA.
DR   RefSeq; NP_001092596.1; NM_001099126.2.
DR   AlphaFoldDB; A6H773; -.
DR   STRING; 9913.ENSBTAP00000017169; -.
DR   PaxDb; A6H773; -.
DR   PRIDE; A6H773; -.
DR   GeneID; 613774; -.
DR   KEGG; bta:613774; -.
DR   CTD; 54968; -.
DR   eggNOG; KOG4478; Eukaryota.
DR   HOGENOM; CLU_096509_1_0_1; -.
DR   InParanoid; A6H773; -.
DR   OrthoDB; 1513532at2759; -.
DR   TreeFam; TF314656; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0032592; C:integral component of mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0140260; F:mitochondrial proton-transporting ATP synthase complex binding; ISS:UniProtKB.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR   InterPro; IPR009724; TMEM70.
DR   InterPro; IPR045325; TMEM70/TMEM186/TMEM223.
DR   PANTHER; PTHR13281; PTHR13281; 1.
DR   Pfam; PF06979; TMEM70; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..78
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           79..254
FT                   /note="Transmembrane protein 70, mitochondrial"
FT                   /id="PRO_0000361546"
FT   TOPO_DOM        79..112
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..136
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..254
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUB7"
SQ   SEQUENCE   254 AA;  28139 MW;  96E80DA818A25DD2 CRC64;
     MLFLALGGPW AAGLRLSGKR TALWASSALR DPRAAVSRAA SCRGSSGRVG GTGLSAAAPV
     LRRVRAQIPV CWERGVRCSH TQLDKSEDGR LIYTGNLART VFGVKCFSYS TSLISLAFLP
     YIFAQNNVIF GSLPLQILFY GTIGSFTVIT PALLHFLTKG YVIRLYHEAR TDTYKAITYS
     VVLSEKSTVF HQNDVKIPNS THVFTTFYAK TKSLLVNPAL FPNPEDYNHL MGYDKPFTFD
     LEEASEKKQL KEEK