TMM70_MOUSE
ID TMM70_MOUSE Reviewed; 253 AA.
AC Q921N7; Q3TKB6; Q3UAP8; Q9CQY4; Q9D7R8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transmembrane protein 70, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=Tmem70 {ECO:0000312|MGI:MGI:1915068};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Embryo, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=28173120; DOI=10.1093/hmg/ddw295;
RA Vrbacky M., Kovalcikova J., Chawengsaksophak K., Beck I.M., Mracek T.,
RA Nuskova H., Sedmera D., Papousek F., Kolar F., Sobol M., Hozak P.,
RA Sedlacek R., Houstek J.;
RT "Knockout of Tmem70 alters biogenesis of ATP synthase and leads to
RT embryonal lethality in mice.";
RL Hum. Mol. Genet. 25:4674-4685(2016).
RN [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=31652072; DOI=10.1096/fj.201900685rr;
RA Kovalcikova J., Vrbacky M., Pecina P., Tauchmannova K., Nuskova H.,
RA Kaplanova V., Brazdova A., Alan L., Elias J., Cunatova K., Korinek V.,
RA Sedlacek R., Mracek T., Houstek J.;
RT "TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting
RT subunit c incorporation into the rotor structure of the enzyme.";
RL FASEB J. 33:14103-14117(2019).
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 (By similarity). Therefore,
CC participates in the early stage of mitochondrial ATP synthase
CC biogenesis and also protects subunit c/ATP5MC1 against
CC intramitochondrial proteolysis (PubMed:31652072, PubMed:28173120). 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 (By similarity). {ECO:0000250|UniProtKB:Q9BUB7,
CC ECO:0000269|PubMed:28173120, ECO:0000269|PubMed:31652072}.
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 -!- TISSUE SPECIFICITY: Higher expressed in the heart than in the liver (at
CC protein level). {ECO:0000269|PubMed:31652072}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for Tmem70 are
CC embryonically lethal at about 9.5 days post coitum and exhibit profound
CC growth retardation (PubMed:28173120). Embryos exhibit delayed
CC development of the cardiovascular system and a disturbed heart
CC mitochondrial ultrastructure, with concentric or irregular cristae
CC structures (PubMed:28173120). {ECO:0000269|PubMed:28173120}.
CC -!- SIMILARITY: Belongs to the TMEM70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25987.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003839; BAB23030.1; -; mRNA.
DR EMBL; AK005075; BAB23799.1; -; mRNA.
DR EMBL; AK008955; BAB25987.1; ALT_FRAME; mRNA.
DR EMBL; AK151280; BAE30266.1; -; mRNA.
DR EMBL; AK167069; BAE39229.1; -; mRNA.
DR EMBL; AK169031; BAE40822.1; -; mRNA.
DR EMBL; BC011320; AAH11320.1; -; mRNA.
DR CCDS; CCDS56623.1; -.
DR RefSeq; NP_080668.1; NM_026392.1.
DR RefSeq; NP_081691.2; NM_027415.2.
DR AlphaFoldDB; Q921N7; -.
DR BioGRID; 214025; 2.
DR STRING; 10090.ENSMUSP00000135483; -.
DR PhosphoSitePlus; Q921N7; -.
DR MaxQB; Q921N7; -.
DR PaxDb; Q921N7; -.
DR PeptideAtlas; Q921N7; -.
DR PRIDE; Q921N7; -.
DR ProteomicsDB; 259040; -.
DR Antibodypedia; 42550; 145 antibodies from 29 providers.
DR Ensembl; ENSMUST00000065373; ENSMUSP00000070497; ENSMUSG00000025940.
DR GeneID; 70397; -.
DR KEGG; mmu:70397; -.
DR UCSC; uc007ajx.1; mouse.
DR CTD; 54968; -.
DR MGI; MGI:1915068; Tmem70.
DR VEuPathDB; HostDB:ENSMUSG00000025940; -.
DR eggNOG; KOG4478; Eukaryota.
DR GeneTree; ENSGT00390000018710; -.
DR HOGENOM; CLU_096509_1_0_1; -.
DR InParanoid; Q921N7; -.
DR OrthoDB; 1513532at2759; -.
DR PhylomeDB; Q921N7; -.
DR TreeFam; TF314656; -.
DR BioGRID-ORCS; 70397; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Tmem70; mouse.
DR PRO; PR:Q921N7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q921N7; protein.
DR Bgee; ENSMUSG00000025940; Expressed in intercostal muscle and 267 other tissues.
DR ExpressionAtlas; Q921N7; baseline and differential.
DR Genevisible; Q921N7; MM.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR InterPro; IPR009724; TMEM70.
DR InterPro; IPR045325; TMEM70/TMEM186/TMEM223.
DR PANTHER; PTHR13281; PTHR13281; 1.
DR Pfam; PF06979; TMEM70; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..77
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 78..253
FT /note="Transmembrane protein 70, mitochondrial"
FT /id="PRO_0000251473"
FT TOPO_DOM 78..99
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..135
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..253
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB7"
FT CONFLICT 7
FT /note="G -> D (in Ref. 1; BAE30266)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> T (in Ref. 1; BAB25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="E -> V (in Ref. 1; BAE30266)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> AQ (in Ref. 1; BAE39229)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="Q -> R (in Ref. 2; AAH11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="D -> E (in Ref. 1; BAB25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> A (in Ref. 2; AAH11320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28275 MW; 43495724B0F45D56 CRC64;
MLLGLGGRWA AGLWPGRTRT TWCVAAALRG SGIAFWRAAS LAEPERLRSG GHLALAESCG
PPGRAQIPVC WEQCVRCFHT QVDKPENGRL IYTGNLARTI FGVKCFSYST SVVSLAFLPY
LLSQNNMMFG SLPLQVLFYG VMGSFTVITP TLLHLLTKGY VIRLYHEATS DTYRAVTYNV
MLSETSTVFH QDDVTIPESA HIFTSFYAKT KSLLVNPALF LNPEDYNHLM GYDKPFTFDM
EEVDEKKLHE GEK
