TMM70_CHICK
ID TMM70_CHICK Reviewed; 246 AA.
AC Q5ZLJ4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Transmembrane protein 70, mitochondrial {ECO:0000250|UniProtKB:Q9BUB7};
DE Flags: Precursor;
GN Name=TMEM70 {ECO:0000250|UniProtKB:Q9BUB7}; ORFNames=RCJMB04_5o22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. Therefore, participates in the early stage of
CC mitochondrial ATP synthase biogenesis and also protects subunit
CC c/ATP5MC1 against intramitochondrial proteolysis.
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; AJ719740; CAG31399.1; -; mRNA.
DR RefSeq; NP_001012866.1; NM_001012848.1.
DR AlphaFoldDB; Q5ZLJ4; -.
DR STRING; 9031.ENSGALP00000030240; -.
DR PaxDb; Q5ZLJ4; -.
DR GeneID; 420188; -.
DR KEGG; gga:420188; -.
DR CTD; 54968; -.
DR VEuPathDB; HostDB:geneid_420188; -.
DR eggNOG; KOG4478; Eukaryota.
DR InParanoid; Q5ZLJ4; -.
DR OrthoDB; 1513532at2759; -.
DR PhylomeDB; Q5ZLJ4; -.
DR PRO; PR:Q5ZLJ4; -.
DR Proteomes; UP000000539; 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..79
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 80..246
FT /note="Transmembrane protein 70, mitochondrial"
FT /id="PRO_0000361547"
FT TOPO_DOM 80..96
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..131
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..246
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
SQ SEQUENCE 246 AA; 27432 MW; 78D0E3A2A468407C CRC64;
MLLRAAGCWR AAASRPGPVW LRGAEHRGLP LASRRLGLPL PLPLAAGGRR LRSGCGALPE
VASFQGVAVR SLSTSAPSDH PEHGRLVYKG NLAKAVLGVR FFSYSTSIFN LFMAPYLMLK
TGIGFDSLFL QAAFYGLIGF FTFVTPVTLH ILTKGYVIRL YYKEEMDTYT AITYNAILAE
KATVFHQKDV KIPDITKMFT TFYAKTKSML VNPTLFPDPQ DYNRLMGYDK AFCFDFEEEE
KDGESK