Full text data of ATP5G3
ATP5G3
[Confidence: low (only semi-automatic identification from reviews)]
ATP synthase F(0) complex subunit C3, mitochondrial (ATP synthase lipid-binding protein; ATP synthase proteolipid P3; ATP synthase proton-transporting mitochondrial F(0) complex subunit C3; ATPase protein 9; ATPase subunit c; Flags: Precursor)
ATP synthase F(0) complex subunit C3, mitochondrial (ATP synthase lipid-binding protein; ATP synthase proteolipid P3; ATP synthase proton-transporting mitochondrial F(0) complex subunit C3; ATPase protein 9; ATPase subunit c; Flags: Precursor)
UniProt
P48201
ID AT5G3_HUMAN Reviewed; 142 AA.
AC P48201; B2R4Z0; D3DPF0; Q4ZFX7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=ATP synthase F(0) complex subunit C3, mitochondrial;
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase proteolipid P3;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C3;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5G3;
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=Liver;
RX PubMed=7698763; DOI=10.1006/geno.1994.1631;
RA Yan W.L., Lerner T.J., Haines J.L., Gusella J.F.;
RT "Sequence analysis and mapping of a novel human mitochondrial ATP
RT synthase subunit 9 cDNA (ATP5G3).";
RL Genomics 24:375-377(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
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.
CC -!- INTERACTION:
CC O95870:ABHD16A; NbExp=1; IntAct=EBI-347797, EBI-348517;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: There are three genes which encode the
CC mitochondrial ATP synthase proteolipid and they specify precursors
CC with different import sequences but identical mature proteins. Is
CC the major protein stored in the storage bodies of animals or
CC humans affected with ceroid lipofuscinosis (Batten disease).
CC -!- SIMILARITY: Belongs to the ATPase C 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; U09813; AAA78807.1; -; mRNA.
DR EMBL; AK311999; BAG34937.1; -; mRNA.
DR EMBL; AC096649; AAX88970.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11106.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11107.1; -; Genomic_DNA.
DR EMBL; BC106881; AAI06882.1; -; mRNA.
DR PIR; I38612; I38612.
DR RefSeq; NP_001002258.1; NM_001002258.4.
DR RefSeq; NP_001680.1; NM_001689.4.
DR UniGene; Hs.429; -.
DR ProteinModelPortal; P48201; -.
DR SMR; P48201; 69-140.
DR IntAct; P48201; 1.
DR MINT; MINT-1036155; -.
DR STRING; 9606.ENSP00000284727; -.
DR PhosphoSite; P48201; -.
DR DMDM; 1352048; -.
DR PaxDb; P48201; -.
DR PRIDE; P48201; -.
DR DNASU; 518; -.
DR Ensembl; ENST00000284727; ENSP00000284727; ENSG00000154518.
DR Ensembl; ENST00000392541; ENSP00000376324; ENSG00000154518.
DR Ensembl; ENST00000409194; ENSP00000387317; ENSG00000154518.
DR GeneID; 518; -.
DR KEGG; hsa:518; -.
DR UCSC; uc002ujz.4; human.
DR CTD; 518; -.
DR GeneCards; GC02M176040; -.
DR HGNC; HGNC:843; ATP5G3.
DR MIM; 602736; gene.
DR neXtProt; NX_P48201; -.
DR PharmGKB; PA25133; -.
DR eggNOG; COG0636; -.
DR HOGENOM; HOG000235246; -.
DR HOVERGEN; HBG050605; -.
DR InParanoid; P48201; -.
DR KO; K02128; -.
DR OMA; CKMFACA; -.
DR OrthoDB; EOG7VHT0K; -.
DR PhylomeDB; P48201; -.
DR ChiTaRS; ATP5G3; human.
DR GeneWiki; ATP5G3; -.
DR GenomeRNAi; 518; -.
DR NextBio; 2151; -.
DR PRO; PR:P48201; -.
DR Bgee; P48201; -.
DR CleanEx; HS_ATP5G3; -.
DR Genevestigator; P48201; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; TAS:ProtInc.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; NAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR Gene3D; 1.20.20.10; -; 1.
DR InterPro; IPR000454; ATPase_F0-cplx_csu.
DR InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS.
DR InterPro; IPR002379; ATPase_proteolipid_c_like_dom.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Mitochondrion; Polymorphism;
KW Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1 67 Mitochondrion.
FT CHAIN 68 142 ATP synthase F(0) complex subunit C3,
FT mitochondrial.
FT /FTId=PRO_0000002567.
FT TRANSMEM 83 103 Helical; (Potential).
FT TRANSMEM 118 138 Helical; (Potential).
FT SITE 125 125 Reversibly protonated during proton
FT transport (By similarity).
FT VARIANT 93 93 G -> E (in dbSNP:rs1802622).
FT /FTId=VAR_011922.
SQ SEQUENCE 142 AA; 14693 MW; 19EC0D1710A0AA3F CRC64;
MFACAKLACT PSLIRAGSRV AYRPISASVL SRPEASRTGE GSTVFNGAQN GVSQLIQREF
QTSAISRDID TAAKFIGAGA ATVGVAGSGA GIGTVFGSLI IGYARNPSLK QQLFSYAILG
FALSEAMGLF CLMVAFLILF AM
//
ID AT5G3_HUMAN Reviewed; 142 AA.
AC P48201; B2R4Z0; D3DPF0; Q4ZFX7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=ATP synthase F(0) complex subunit C3, mitochondrial;
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase proteolipid P3;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C3;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5G3;
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=Liver;
RX PubMed=7698763; DOI=10.1006/geno.1994.1631;
RA Yan W.L., Lerner T.J., Haines J.L., Gusella J.F.;
RT "Sequence analysis and mapping of a novel human mitochondrial ATP
RT synthase subunit 9 cDNA (ATP5G3).";
RL Genomics 24:375-377(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
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.
CC -!- INTERACTION:
CC O95870:ABHD16A; NbExp=1; IntAct=EBI-347797, EBI-348517;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: There are three genes which encode the
CC mitochondrial ATP synthase proteolipid and they specify precursors
CC with different import sequences but identical mature proteins. Is
CC the major protein stored in the storage bodies of animals or
CC humans affected with ceroid lipofuscinosis (Batten disease).
CC -!- SIMILARITY: Belongs to the ATPase C 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; U09813; AAA78807.1; -; mRNA.
DR EMBL; AK311999; BAG34937.1; -; mRNA.
DR EMBL; AC096649; AAX88970.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11106.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11107.1; -; Genomic_DNA.
DR EMBL; BC106881; AAI06882.1; -; mRNA.
DR PIR; I38612; I38612.
DR RefSeq; NP_001002258.1; NM_001002258.4.
DR RefSeq; NP_001680.1; NM_001689.4.
DR UniGene; Hs.429; -.
DR ProteinModelPortal; P48201; -.
DR SMR; P48201; 69-140.
DR IntAct; P48201; 1.
DR MINT; MINT-1036155; -.
DR STRING; 9606.ENSP00000284727; -.
DR PhosphoSite; P48201; -.
DR DMDM; 1352048; -.
DR PaxDb; P48201; -.
DR PRIDE; P48201; -.
DR DNASU; 518; -.
DR Ensembl; ENST00000284727; ENSP00000284727; ENSG00000154518.
DR Ensembl; ENST00000392541; ENSP00000376324; ENSG00000154518.
DR Ensembl; ENST00000409194; ENSP00000387317; ENSG00000154518.
DR GeneID; 518; -.
DR KEGG; hsa:518; -.
DR UCSC; uc002ujz.4; human.
DR CTD; 518; -.
DR GeneCards; GC02M176040; -.
DR HGNC; HGNC:843; ATP5G3.
DR MIM; 602736; gene.
DR neXtProt; NX_P48201; -.
DR PharmGKB; PA25133; -.
DR eggNOG; COG0636; -.
DR HOGENOM; HOG000235246; -.
DR HOVERGEN; HBG050605; -.
DR InParanoid; P48201; -.
DR KO; K02128; -.
DR OMA; CKMFACA; -.
DR OrthoDB; EOG7VHT0K; -.
DR PhylomeDB; P48201; -.
DR ChiTaRS; ATP5G3; human.
DR GeneWiki; ATP5G3; -.
DR GenomeRNAi; 518; -.
DR NextBio; 2151; -.
DR PRO; PR:P48201; -.
DR Bgee; P48201; -.
DR CleanEx; HS_ATP5G3; -.
DR Genevestigator; P48201; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; TAS:ProtInc.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; NAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR Gene3D; 1.20.20.10; -; 1.
DR InterPro; IPR000454; ATPase_F0-cplx_csu.
DR InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS.
DR InterPro; IPR002379; ATPase_proteolipid_c_like_dom.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Mitochondrion; Polymorphism;
KW Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1 67 Mitochondrion.
FT CHAIN 68 142 ATP synthase F(0) complex subunit C3,
FT mitochondrial.
FT /FTId=PRO_0000002567.
FT TRANSMEM 83 103 Helical; (Potential).
FT TRANSMEM 118 138 Helical; (Potential).
FT SITE 125 125 Reversibly protonated during proton
FT transport (By similarity).
FT VARIANT 93 93 G -> E (in dbSNP:rs1802622).
FT /FTId=VAR_011922.
SQ SEQUENCE 142 AA; 14693 MW; 19EC0D1710A0AA3F CRC64;
MFACAKLACT PSLIRAGSRV AYRPISASVL SRPEASRTGE GSTVFNGAQN GVSQLIQREF
QTSAISRDID TAAKFIGAGA ATVGVAGSGA GIGTVFGSLI IGYARNPSLK QQLFSYAILG
FALSEAMGLF CLMVAFLILF AM
//
MIM
602736
*RECORD*
*FIELD* NO
602736
*FIELD* TI
*602736 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL FO COMPLEX, SUBUNIT C,
ISOFORM 3; ATP5G3
read more;;MITOCHONDRIAL ATP SYNTHASE, SUBUNIT C, ISOFORM 3;;
MITOCHONDRIAL ATP SYNTHASE, SUBUNIT 9, ISOFORM 3
*FIELD* TX
DESCRIPTION
Mitochondrial ATP synthase is a multisubunit enzyme that catalyzes ATP
synthesis during oxidative phosphorylation (see 601519). Subunit 9,
encoded by the ATP5G3 gene, transports protons across the mitochondrial
inner membrane to the F1-ATPase (see 108729) protruding from the matrix
side, harnessing the energy from an electrochemical gradient for the ATP
generation. Each ATP synthase complex has multiple copies of subunit 9
in the transmembrane portion (Fo) of the complex (summary by Yan et al.,
1994).
CLONING
By screening a human liver cDNA library with oligonucleotides derived
from an ATP5G1 (603192) cDNA, Yan et al. (1994) identified cDNAs
encoding a novel subunit 9, ATP5G3. Like ATP5G1 and ATP5G2 (603193),
ATP5G3 has a long leader sequence that is cleaved to produce a predicted
75-amino acid mature protein. The amino acid sequence of the ATP5G3
leader peptide differs from the sequences of the ATP5G1 and ATP5G2
leader peptides, but it retains a motif critical for mitochondrial
import and maturation. While the nucleotide sequence encoding the mature
ATP5G3 protein is 80% identical to the coding regions of the mature
ATP5G1 and ATP5G3 proteins, the amino acid sequences of the 3 mature
subunit 9 proteins are identical.
MAPPING
Yan et al. (1994) mapped the ATP5G3 gene to chromosome 2 by analysis of
somatic cell hybrid panels.
*FIELD* RF
1. Yan, W. L.; Lerner, T. J.; Haines, J. L.; Gusella, J. F.: Sequence
analysis and mapping of a novel human mitochondrial ATP synthase subunit
9 cDNA (ATP5G3). Genomics 24: 375-377, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/19/1998
*FIELD* ED
carol: 06/13/2011
alopez: 5/7/2010
alopez: 10/23/1998
carol: 6/24/1998
psherman: 6/22/1998
*RECORD*
*FIELD* NO
602736
*FIELD* TI
*602736 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL FO COMPLEX, SUBUNIT C,
ISOFORM 3; ATP5G3
read more;;MITOCHONDRIAL ATP SYNTHASE, SUBUNIT C, ISOFORM 3;;
MITOCHONDRIAL ATP SYNTHASE, SUBUNIT 9, ISOFORM 3
*FIELD* TX
DESCRIPTION
Mitochondrial ATP synthase is a multisubunit enzyme that catalyzes ATP
synthesis during oxidative phosphorylation (see 601519). Subunit 9,
encoded by the ATP5G3 gene, transports protons across the mitochondrial
inner membrane to the F1-ATPase (see 108729) protruding from the matrix
side, harnessing the energy from an electrochemical gradient for the ATP
generation. Each ATP synthase complex has multiple copies of subunit 9
in the transmembrane portion (Fo) of the complex (summary by Yan et al.,
1994).
CLONING
By screening a human liver cDNA library with oligonucleotides derived
from an ATP5G1 (603192) cDNA, Yan et al. (1994) identified cDNAs
encoding a novel subunit 9, ATP5G3. Like ATP5G1 and ATP5G2 (603193),
ATP5G3 has a long leader sequence that is cleaved to produce a predicted
75-amino acid mature protein. The amino acid sequence of the ATP5G3
leader peptide differs from the sequences of the ATP5G1 and ATP5G2
leader peptides, but it retains a motif critical for mitochondrial
import and maturation. While the nucleotide sequence encoding the mature
ATP5G3 protein is 80% identical to the coding regions of the mature
ATP5G1 and ATP5G3 proteins, the amino acid sequences of the 3 mature
subunit 9 proteins are identical.
MAPPING
Yan et al. (1994) mapped the ATP5G3 gene to chromosome 2 by analysis of
somatic cell hybrid panels.
*FIELD* RF
1. Yan, W. L.; Lerner, T. J.; Haines, J. L.; Gusella, J. F.: Sequence
analysis and mapping of a novel human mitochondrial ATP synthase subunit
9 cDNA (ATP5G3). Genomics 24: 375-377, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/19/1998
*FIELD* ED
carol: 06/13/2011
alopez: 5/7/2010
alopez: 10/23/1998
carol: 6/24/1998
psherman: 6/22/1998