Full text data of ATP5O
ATP5O
(ATPO)
[Confidence: low (only semi-automatic identification from reviews)]
ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein; OSCP; Flags: Precursor)
ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein; OSCP; Flags: Precursor)
UniProt
P48047
ID ATPO_HUMAN Reviewed; 213 AA.
AC P48047; B2R4E2; Q5U042; Q6IBI2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=ATP synthase subunit O, mitochondrial;
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATP5O; Synonyms=ATPO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Muscle;
RX PubMed=7490082; DOI=10.1006/geno.1995.1176;
RA Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.;
RT "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O)
RT by exon trapping and mapping to chromosome 21q22.1-q22.2.";
RL Genomics 28:470-476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RC TISSUE=Heart;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 24-40.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-162; LYS-172 AND
RP LYS-192, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC 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
CC core - and CF(0) - the membrane proton channel. CF(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC has three main subunits: a, b and c. Component of an ATP synthase
CC complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J,
CC ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O,
CC ATP5L, USMG5 and MP68 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Mitochondrion
CC inner membrane (By similarity).
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X83218; CAA58219.1; -; mRNA.
DR EMBL; BT019836; AAV38639.1; -; mRNA.
DR EMBL; CR456822; CAG33103.1; -; mRNA.
DR EMBL; AK222962; BAD96682.1; -; mRNA.
DR EMBL; AK311796; BAG34739.1; -; mRNA.
DR EMBL; CH471079; EAX09802.1; -; Genomic_DNA.
DR EMBL; BC021233; AAH21233.1; -; mRNA.
DR EMBL; BC022865; AAH22865.1; -; mRNA.
DR RefSeq; NP_001688.1; NM_001697.2.
DR UniGene; Hs.409140; -.
DR ProteinModelPortal; P48047; -.
DR SMR; P48047; 24-212.
DR IntAct; P48047; 11.
DR MINT; MINT-5002594; -.
DR STRING; 9606.ENSP00000290299; -.
DR PhosphoSite; P48047; -.
DR DMDM; 1352049; -.
DR OGP; P48047; -.
DR UCD-2DPAGE; P48047; -.
DR PaxDb; P48047; -.
DR PeptideAtlas; P48047; -.
DR PRIDE; P48047; -.
DR DNASU; 539; -.
DR Ensembl; ENST00000290299; ENSP00000290299; ENSG00000241837.
DR GeneID; 539; -.
DR KEGG; hsa:539; -.
DR UCSC; uc002ytl.3; human.
DR CTD; 539; -.
DR GeneCards; GC21M035275; -.
DR H-InvDB; HIX0158705; -.
DR HGNC; HGNC:850; ATP5O.
DR HPA; CAB016209; -.
DR MIM; 600828; gene.
DR neXtProt; NX_P48047; -.
DR PharmGKB; PA25144; -.
DR eggNOG; COG0712; -.
DR HOGENOM; HOG000075825; -.
DR HOVERGEN; HBG004309; -.
DR InParanoid; P48047; -.
DR KO; K02137; -.
DR OMA; AEVTSAH; -.
DR PhylomeDB; P48047; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; ATP5O; human.
DR GeneWiki; ATP5O; -.
DR GenomeRNAi; 539; -.
DR NextBio; 2235; -.
DR PRO; PR:P48047; -.
DR ArrayExpress; P48047; -.
DR Bgee; P48047; -.
DR CleanEx; HS_ATP5O; -.
DR Genevestigator; P48047; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:UniProtKB.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR Gene3D; 1.10.520.20; -; 1.
DR InterPro; IPR000711; ATPase_F1-cplx_OSCP/dsu.
DR InterPro; IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
DR InterPro; IPR026015; ATPase_OSCP/delta_N.
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; Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Polymorphism;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1 23 Mitochondrion.
FT CHAIN 24 213 ATP synthase subunit O, mitochondrial.
FT /FTId=PRO_0000002646.
FT MOD_RES 54 54 N6-acetyllysine.
FT MOD_RES 60 60 N6-acetyllysine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine (By similarity).
FT MOD_RES 73 73 N6-acetyllysine (By similarity).
FT MOD_RES 158 158 N6-acetyllysine (By similarity).
FT MOD_RES 162 162 N6-acetyllysine.
FT MOD_RES 172 172 N6-acetyllysine.
FT MOD_RES 176 176 N6-acetyllysine (By similarity).
FT MOD_RES 192 192 N6-acetyllysine.
FT VARIANT 98 98 K -> R (in dbSNP:rs4842).
FT /FTId=VAR_011930.
SQ SEQUENCE 213 AA; 23277 MW; 311F53576A31FC93 CRC64;
MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER FSPLTTNLIN LLAENGRLSN
TQGVVSAFST MMSVHRGEVP CTVTSASPLE EATLSELKTV LKSFLSQGQV LKLEAKTDPS
ILGGMIVRIG EKYVDMSVKT KIQKLGRAMR EIV
//
ID ATPO_HUMAN Reviewed; 213 AA.
AC P48047; B2R4E2; Q5U042; Q6IBI2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=ATP synthase subunit O, mitochondrial;
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATP5O; Synonyms=ATPO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Muscle;
RX PubMed=7490082; DOI=10.1006/geno.1995.1176;
RA Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.;
RT "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O)
RT by exon trapping and mapping to chromosome 21q22.1-q22.2.";
RL Genomics 28:470-476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98.
RC TISSUE=Heart;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 24-40.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-162; LYS-172 AND
RP LYS-192, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC 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
CC core - and CF(0) - the membrane proton channel. CF(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC has three main subunits: a, b and c. Component of an ATP synthase
CC complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J,
CC ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O,
CC ATP5L, USMG5 and MP68 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Mitochondrion
CC inner membrane (By similarity).
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X83218; CAA58219.1; -; mRNA.
DR EMBL; BT019836; AAV38639.1; -; mRNA.
DR EMBL; CR456822; CAG33103.1; -; mRNA.
DR EMBL; AK222962; BAD96682.1; -; mRNA.
DR EMBL; AK311796; BAG34739.1; -; mRNA.
DR EMBL; CH471079; EAX09802.1; -; Genomic_DNA.
DR EMBL; BC021233; AAH21233.1; -; mRNA.
DR EMBL; BC022865; AAH22865.1; -; mRNA.
DR RefSeq; NP_001688.1; NM_001697.2.
DR UniGene; Hs.409140; -.
DR ProteinModelPortal; P48047; -.
DR SMR; P48047; 24-212.
DR IntAct; P48047; 11.
DR MINT; MINT-5002594; -.
DR STRING; 9606.ENSP00000290299; -.
DR PhosphoSite; P48047; -.
DR DMDM; 1352049; -.
DR OGP; P48047; -.
DR UCD-2DPAGE; P48047; -.
DR PaxDb; P48047; -.
DR PeptideAtlas; P48047; -.
DR PRIDE; P48047; -.
DR DNASU; 539; -.
DR Ensembl; ENST00000290299; ENSP00000290299; ENSG00000241837.
DR GeneID; 539; -.
DR KEGG; hsa:539; -.
DR UCSC; uc002ytl.3; human.
DR CTD; 539; -.
DR GeneCards; GC21M035275; -.
DR H-InvDB; HIX0158705; -.
DR HGNC; HGNC:850; ATP5O.
DR HPA; CAB016209; -.
DR MIM; 600828; gene.
DR neXtProt; NX_P48047; -.
DR PharmGKB; PA25144; -.
DR eggNOG; COG0712; -.
DR HOGENOM; HOG000075825; -.
DR HOVERGEN; HBG004309; -.
DR InParanoid; P48047; -.
DR KO; K02137; -.
DR OMA; AEVTSAH; -.
DR PhylomeDB; P48047; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; ATP5O; human.
DR GeneWiki; ATP5O; -.
DR GenomeRNAi; 539; -.
DR NextBio; 2235; -.
DR PRO; PR:P48047; -.
DR ArrayExpress; P48047; -.
DR Bgee; P48047; -.
DR CleanEx; HS_ATP5O; -.
DR Genevestigator; P48047; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:UniProtKB.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR Gene3D; 1.10.520.20; -; 1.
DR InterPro; IPR000711; ATPase_F1-cplx_OSCP/dsu.
DR InterPro; IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
DR InterPro; IPR026015; ATPase_OSCP/delta_N.
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; Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Polymorphism;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1 23 Mitochondrion.
FT CHAIN 24 213 ATP synthase subunit O, mitochondrial.
FT /FTId=PRO_0000002646.
FT MOD_RES 54 54 N6-acetyllysine.
FT MOD_RES 60 60 N6-acetyllysine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine (By similarity).
FT MOD_RES 73 73 N6-acetyllysine (By similarity).
FT MOD_RES 158 158 N6-acetyllysine (By similarity).
FT MOD_RES 162 162 N6-acetyllysine.
FT MOD_RES 172 172 N6-acetyllysine.
FT MOD_RES 176 176 N6-acetyllysine (By similarity).
FT MOD_RES 192 192 N6-acetyllysine.
FT VARIANT 98 98 K -> R (in dbSNP:rs4842).
FT /FTId=VAR_011930.
SQ SEQUENCE 213 AA; 23277 MW; 311F53576A31FC93 CRC64;
MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER FSPLTTNLIN LLAENGRLSN
TQGVVSAFST MMSVHRGEVP CTVTSASPLE EATLSELKTV LKSFLSQGQV LKLEAKTDPS
ILGGMIVRIG EKYVDMSVKT KIQKLGRAMR EIV
//
MIM
600828
*RECORD*
*FIELD* NO
600828
*FIELD* TI
*600828 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL F1 COMPLEX, O SUBUNIT;
ATP5O
;;MITOCHONDRIAL ATP SYNTHASE, O SUBUNIT;;
read moreOLIGOMYCIN SENSITIVITY-CONFERRING PROTEIN; OSCP
*FIELD* TX
DESCRIPTION
ATP synthase (complex V of the mitochondrial respiratory chain) is a
multimeric complex consisting of at least 16 different polypeptides, 2
of which are mitochondrially encoded and the remainder produced by
nuclear genes. One of these nuclear genes (ATP5O) encodes the oligomycin
sensitivity-conferring protein (OSCP) of ATP synthase and has been
described from yeast, cow, and mouse. OSCP is a component of the 'stalk'
region connecting the F1 and Fo domains of the ATP synthase complex
(summary by Chen et al., 1995).
CLONING
Chen et al. (1995) cloned a cDNA corresponding to human ATP5O. The
authors used exon trapping from pools of chromosome 21-specific cosmids
to identify a portion of the gene, which was then used to screen a fetal
brain cDNA library. The predicted polypeptide is 213 amino acids long
with more than 80% identity to the bovine and mouse homologs. Northern
blot analysis detected expression in all human tissues examined and at
highest levels in muscle and heart.
MAPPING
Chen et al. (1995) mapped the ATP5O gene to chromosome 21q22.1-q22.2 by
fluorescence in situ hybridization and by hybridization to somatic cell
hybrid DNAs containing defined portions of chromosome 21.
*FIELD* RF
1. Chen, H.; Morris, M. A.; Rossier, C.; Blouin, J.-L.; Antonarakis,
S. E.: Cloning of the cDNA for the human ATP synthase OSCP subunit
(ATP50) by exon trapping and mapping to chromosome 21q22.1-q22.2. Genomics 28:
470-476, 1995.
*FIELD* CD
Alan F. Scott: 10/3/1995
*FIELD* ED
carol: 06/13/2011
alopez: 5/7/2010
carol: 6/24/1998
psherman: 6/22/1998
alopez: 7/17/1997
mark: 4/7/1996
mark: 12/5/1995
mark: 10/3/1995
*RECORD*
*FIELD* NO
600828
*FIELD* TI
*600828 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL F1 COMPLEX, O SUBUNIT;
ATP5O
;;MITOCHONDRIAL ATP SYNTHASE, O SUBUNIT;;
read moreOLIGOMYCIN SENSITIVITY-CONFERRING PROTEIN; OSCP
*FIELD* TX
DESCRIPTION
ATP synthase (complex V of the mitochondrial respiratory chain) is a
multimeric complex consisting of at least 16 different polypeptides, 2
of which are mitochondrially encoded and the remainder produced by
nuclear genes. One of these nuclear genes (ATP5O) encodes the oligomycin
sensitivity-conferring protein (OSCP) of ATP synthase and has been
described from yeast, cow, and mouse. OSCP is a component of the 'stalk'
region connecting the F1 and Fo domains of the ATP synthase complex
(summary by Chen et al., 1995).
CLONING
Chen et al. (1995) cloned a cDNA corresponding to human ATP5O. The
authors used exon trapping from pools of chromosome 21-specific cosmids
to identify a portion of the gene, which was then used to screen a fetal
brain cDNA library. The predicted polypeptide is 213 amino acids long
with more than 80% identity to the bovine and mouse homologs. Northern
blot analysis detected expression in all human tissues examined and at
highest levels in muscle and heart.
MAPPING
Chen et al. (1995) mapped the ATP5O gene to chromosome 21q22.1-q22.2 by
fluorescence in situ hybridization and by hybridization to somatic cell
hybrid DNAs containing defined portions of chromosome 21.
*FIELD* RF
1. Chen, H.; Morris, M. A.; Rossier, C.; Blouin, J.-L.; Antonarakis,
S. E.: Cloning of the cDNA for the human ATP synthase OSCP subunit
(ATP50) by exon trapping and mapping to chromosome 21q22.1-q22.2. Genomics 28:
470-476, 1995.
*FIELD* CD
Alan F. Scott: 10/3/1995
*FIELD* ED
carol: 06/13/2011
alopez: 5/7/2010
carol: 6/24/1998
psherman: 6/22/1998
alopez: 7/17/1997
mark: 4/7/1996
mark: 12/5/1995
mark: 10/3/1995