ATP5J_RAT
ID ATP5J_RAT Reviewed; 108 AA.
AC P21571;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP synthase-coupling factor 6, mitochondrial {ECO:0000305};
DE Short=ATPase subunit F6;
DE AltName: Full=ATP synthase peripheral stalk subunit F6 {ECO:0000305};
DE Flags: Precursor;
GN Name=Atp5pf {ECO:0000312|RGD:621376}; Synonyms=Atp5j;
OS Rattus norvegicus (Rat).
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=2145831; DOI=10.1016/0006-291x(90)90794-n;
RA Higuti T., Osaka F., Yoshihara Y., Tsurumi C., Kawamura Y., Tani I.,
RA Toda H., Kakuno T., Sakiyama F., Tanaka K., Ichihara A.;
RT "cDNA cloning and sequencing for the import precursor of coupling factor 6
RT in H(+)-ATP synthase from rat liver mitochondria.";
RL Biochem. Biophys. Res. Commun. 171:1079-1086(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary anterior lobe;
RX PubMed=1386054; DOI=10.1016/0378-1119(92)90528-w;
RA Tracer H.L., Loh Y.P., Birch N.P.;
RT "Rat mitochondrial coupling factor 6: molecular cloning of a cDNA encoding
RT the imported precursor.";
RL Gene 116:291-292(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP PROTEIN SEQUENCE OF 33-66.
RC TISSUE=Liver;
RX PubMed=1429613; DOI=10.1016/s0021-9258(18)41722-x;
RA Higuti T., Yoshihara Y., Kuroiwa K., Kawamura Y., Toda H., Sakiyama F.;
RT "A simple, rapid method for purification of epsilon-subunit, coupling
RT factor 6, subunit d, and subunit e from rat liver H(+)-ATP synthase and
RT determination of the complete amino acid sequence of epsilon-subunit.";
RL J. Biol. Chem. 267:22658-22661(1992).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. Also involved in the restoration of
CC oligomycin-sensitive ATPase activity to depleted F1-F0 complexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
CC {ECO:0000305}.
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DR EMBL; M73030; AAA40954.1; -; mRNA.
DR EMBL; X54510; CAA38369.1; -; mRNA.
DR EMBL; BC059121; AAH59121.1; -; mRNA.
DR PIR; JC1167; JC1167.
DR RefSeq; NP_446054.1; NM_053602.2.
DR RefSeq; XP_008766824.1; XM_008768602.2.
DR RefSeq; XP_008766825.1; XM_008768603.1.
DR RefSeq; XP_017453574.1; XM_017598085.1.
DR RefSeq; XP_017453575.1; XM_017598086.1.
DR AlphaFoldDB; P21571; -.
DR SMR; P21571; -.
DR BioGRID; 250190; 2.
DR CORUM; P21571; -.
DR IntAct; P21571; 1.
DR MINT; P21571; -.
DR STRING; 10116.ENSRNOP00000002116; -.
DR iPTMnet; P21571; -.
DR PhosphoSitePlus; P21571; -.
DR UCD-2DPAGE; P21571; -.
DR jPOST; P21571; -.
DR PaxDb; P21571; -.
DR PRIDE; P21571; -.
DR GeneID; 94271; -.
DR KEGG; rno:94271; -.
DR UCSC; RGD:621376; rat.
DR CTD; 522; -.
DR RGD; 621376; Atp5pf.
DR VEuPathDB; HostDB:ENSRNOG00000001551; -.
DR eggNOG; KOG4634; Eukaryota.
DR HOGENOM; CLU_145649_1_0_1; -.
DR InParanoid; P21571; -.
DR OMA; PKFEVFD; -.
DR OrthoDB; 1559269at2759; -.
DR PhylomeDB; P21571; -.
DR TreeFam; TF318998; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:P21571; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001551; Expressed in heart and 20 other tissues.
DR Genevisible; P21571; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:1900139; P:negative regulation of arachidonic acid secretion; IDA:RGD.
DR GO; GO:0032307; P:negative regulation of prostaglandin secretion; IDA:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; IDA:RGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR Gene3D; 1.10.246.110; -; 1.
DR InterPro; IPR008387; ATP_synth_f6_mt.
DR InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR PANTHER; PTHR12441; PTHR12441; 1.
DR Pfam; PF05511; ATP-synt_F6; 1.
DR PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR SUPFAM; SSF111357; SSF111357; 1.
PE 1: Evidence at protein level;
KW Acetylation; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1429613"
FT CHAIN 33..108
FT /note="ATP synthase-coupling factor 6, mitochondrial"
FT /id="PRO_0000002531"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 99
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 99
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 108 AA; 12494 MW; FF1177C9681B5F51 CRC64;
MTVQRIFRLS SVLRSAVSVH LRRNIGVTAV AFNKELDPVQ KLFLDKIREY KAKRLASGGP
VDTGPEYQQE VDRELFKLKQ MYGKGEMDKF PTFNFEDPKF EVLDKPQS
