ATPO_RAT
ID ATPO_RAT Reviewed; 213 AA.
AC Q06647;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000305};
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE AltName: Full=Sperm flagella protein 4;
DE Flags: Precursor;
GN Name=Atp5po {ECO:0000312|RGD:621379}; Synonyms=Atp5o;
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=Hepatocyte;
RX PubMed=8448208; DOI=10.1016/0167-4781(93)90219-4;
RA Higuti T., Kuroiwa K., Kawamura Y., Morimoto K., Tsujita H.;
RT "Molecular cloning and sequence of cDNAs for the import precursors of
RT oligomycin sensitivity conferring protein, ATPase inhibitor protein, and
RT subunit c of H(+)-ATP synthase in rat mitochondria.";
RL Biochim. Biophys. Acta 1172:311-314(1993).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 27-40, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC STRAIN=Holtzman; TISSUE=Epididymis, and Sperm;
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
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.
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. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the principal cells of the epididymis.
CC Detected in flagella of epididymal sperm (at protein level).
CC {ECO:0000269|PubMed:19423663}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; D13127; BAA02429.1; -; mRNA.
DR EMBL; BC060544; AAH60544.1; -; mRNA.
DR PIR; S30181; S30181.
DR RefSeq; NP_620238.1; NM_138883.1.
DR AlphaFoldDB; Q06647; -.
DR SMR; Q06647; -.
DR BioGRID; 251369; 4.
DR CORUM; Q06647; -.
DR IntAct; Q06647; 8.
DR MINT; Q06647; -.
DR STRING; 10116.ENSRNOP00000002732; -.
DR CarbonylDB; Q06647; -.
DR iPTMnet; Q06647; -.
DR PhosphoSitePlus; Q06647; -.
DR SwissPalm; Q06647; -.
DR jPOST; Q06647; -.
DR PaxDb; Q06647; -.
DR PRIDE; Q06647; -.
DR Ensembl; ENSRNOT00000002732; ENSRNOP00000002732; ENSRNOG00000001991.
DR GeneID; 192241; -.
DR KEGG; rno:192241; -.
DR UCSC; RGD:621379; rat.
DR CTD; 539; -.
DR RGD; 621379; Atp5po.
DR eggNOG; KOG1662; Eukaryota.
DR GeneTree; ENSGT00390000015060; -.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; Q06647; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 1178688at2759; -.
DR PhylomeDB; Q06647; -.
DR TreeFam; TF106241; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:Q06647; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001991; Expressed in heart and 20 other tissues.
DR Genevisible; Q06647; RN.
DR GO; GO:0009986; C:cell surface; 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:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:1903924; F:estradiol binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; IGI:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; 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 Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT CHAIN 24..213
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000002649"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 100
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48047"
FT MOD_RES 199
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
SQ SEQUENCE 213 AA; 23398 MW; BBAB7331A715E686 CRC64;
MAAPATSVLS RQVRSFSTSV VRPFSKLVRP PVQVYGIEGR YATALYSAAS KQKRLDQVEK
ELLRVGQLLK DPKVSLAVLN PYIKRSIKVK SLKDITTKEK FSPLTANLMN LLAENGRLGN
TQGVISAFST IMSVHRGEVP CTVTTAFPLD EAVLSELKTV LNSFLSKGQI LNLEVKTDPS
IMGGMIVRIG EKYVDMSAKS KIQKLSKAMR DLL
