ATP6_RAT
ID ATP6_RAT Reviewed; 226 AA.
AC P05504; Q9T2E9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=Mt-atp6; Synonyms=Atp6, Atpase6, Mtatp6;
OS Rattus norvegicus (Rat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=24185961; DOI=10.1007/bf00365694;
RA Grosskopf R., Feldmann H.;
RT "Analysis of a DNA segment from rat liver mitochondria containing the genes
RT for the cytochrome oxidase subunits I, II and III, ATPase subunit 6, and
RT several tRNA genes.";
RL Curr. Genet. 4:151-158(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2504926; DOI=10.1007/bf02602930;
RA Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT "The complete nucleotide sequence of the Rattus norvegicus mitochondrial
RT genome: cryptic signals revealed by comparative analysis between
RT vertebrates.";
RL J. Mol. Evol. 28:497-516(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BHE/CDB, and Sprague-Dawley; TISSUE=Liver;
RX PubMed=8529844; DOI=10.1096/fasebj.9.15.8529844;
RA Mathews C.E., McGraw R.A., Berdanier C.D.;
RT "A point mutation in the mitochondrial DNA of diabetes-prone BHE/cdb
RT rats.";
RL FASEB J. 9:1638-1642(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 29-41.
RX PubMed=11163232; DOI=10.1016/s1074-7613(01)00091-7;
RA Speir J.A., Stevens J., Joly E., Butcher G.W., Wilson I.A.;
RT "Two different, highly exposed, bulged structures for an unusually long
RT peptide bound to rat MHC class I RT1-A(a).";
RL Immunity 14:81-92(2001).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC (By similarity). {ECO:0000250|UniProtKB:P00846,
CC ECO:0000250|UniProtKB:P00847}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01435; AAD15019.1; -; Genomic_DNA.
DR EMBL; X14848; CAA32959.1; -; Genomic_DNA.
DR EMBL; AF115770; AAD22965.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77599.1; -; Genomic_DNA.
DR PIR; S04752; S04752.
DR RefSeq; AP_004897.1; AC_000022.2.
DR RefSeq; YP_665634.1; NC_001665.2.
DR PDB; 1ED3; X-ray; 2.55 A; C/F=29-41.
DR PDBsum; 1ED3; -.
DR AlphaFoldDB; P05504; -.
DR SMR; P05504; -.
DR CORUM; P05504; -.
DR STRING; 10116.ENSRNOP00000049769; -.
DR BindingDB; P05504; -.
DR PaxDb; P05504; -.
DR PRIDE; P05504; -.
DR Ensembl; ENSRNOT00000046108; ENSRNOP00000049769; ENSRNOG00000031979.
DR GeneID; 26197; -.
DR KEGG; rno:26197; -.
DR CTD; 4508; -.
DR RGD; 621239; Mt-atp6.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P05504; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR EvolutionaryTrace; P05504; -.
DR PRO; PR:P05504; -.
DR Proteomes; UP000002494; Mitochondrion.
DR Bgee; ENSRNOG00000031979; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; P05504; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR Gene3D; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082163"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="A -> P (in Ref. 1; AAD15019)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="N -> D (in Ref. 2; CAA32959)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="L -> S (in Ref. 2; CAA32959 and 3; AAD22965)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="A -> V (in Ref. 1; AAD15019)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1ED3"
SQ SEQUENCE 226 AA; 25076 MW; A3674941F4143BCF CRC64;
MNENLFASFI TPTMMGLPIV VTIIMFPSIL FPSSERLISN RLHSFQHWLI KLIIKQMMLI
HTPKGRTWAL MIVSLIMFIG STNLLGLLPH TFTPTTQLSM NLSMAIPLWA GAVILGFRHK
LKNSLAHFLP QGTPISLIPM LIIIETISLF IQPMALAVRL TANITAGHLL MHLIGGATLV
LMDISPPTAT ITFIILLLLT VLEFAVALIQ AYVFTLLVSL YLHDNT
