ID AT5G2_HUMAN Reviewed; 141 AA.
AC Q06055; B3KQQ6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 18-JAN-2017, entry version 154.
DE RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial;
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase proteolipid P2;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C2;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5G2; ORFNames=PSEC0033;
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 [GENOMIC DNA].
RX PubMed=8328972; DOI=10.1042/bj2930051;
RA Dyer M.R., Walker J.E.;
RT "Sequences of members of the human gene family for the c subunit of
RT mitochondrial ATP synthase.";
RL Biochem. J. 293:51-64(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8485160; DOI=10.1016/0167-4781(93)90249-D;
RA Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.;
RT "Molecular cloning and sequence of two cDNAs for human subunit c of
RT H(+)-ATP synthase in mitochondria.";
RL Biochim. Biophys. Acta 1173:87-90(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-141 (ISOFORMS 1/2/3).
RC TISSUE=Liver;
RX PubMed=2883974; DOI=10.1016/0006-291X(87)91446-X;
RA Farrell L.B., Nagley P.;
RT "Human liver cDNA clones encoding proteolipid subunit 9 of the
RT mitochondrial ATPase complex.";
RL Biochem. Biophys. Res. Commun. 144:1257-1264(1987).
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 -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q06055-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06055-2; Sequence=VSP_037348;
CC Note=Derived from EST data.;
CC Name=3;
CC IsoId=Q06055-3; Sequence=VSP_037349;
CC Note=Derived from EST data.;
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. {ECO:0000305}.
DR EMBL; X69908; CAA49533.1; -; Genomic_DNA.
DR EMBL; D13119; BAA02421.1; -; mRNA.
DR EMBL; AK075351; BAG52118.1; -; mRNA.
DR EMBL; AC073594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020826; AAH20826.1; -; mRNA.
DR CCDS; CCDS31812.1; -. [Q06055-3]
DR CCDS; CCDS81694.1; -. [Q06055-1]
DR CCDS; CCDS8863.2; -. [Q06055-2]
DR PIR; S34067; S34067.
DR RefSeq; NP_001002031.1; NM_001002031.2. [Q06055-3]
DR RefSeq; NP_001317198.1; NM_001330269.1. [Q06055-1]
DR RefSeq; NP_005167.2; NM_005176.5. [Q06055-2]
DR RefSeq; XP_016874949.1; XM_017019460.1. [Q06055-2]
DR RefSeq; XP_016874950.1; XM_017019461.1. [Q06055-3]
DR UniGene; Hs.524464; -.
DR ProteinModelPortal; Q06055; -.
DR SMR; Q06055; -.
DR BioGrid; 107002; 3.
DR IntAct; Q06055; 3.
DR STRING; 9606.ENSP00000377878; -.
DR PhosphoSitePlus; Q06055; -.
DR DMDM; 461592; -.
DR MaxQB; Q06055; -.
DR PaxDb; Q06055; -.
DR PRIDE; Q06055; -.
DR TopDownProteomics; Q06055-1; -. [Q06055-1]
DR TopDownProteomics; Q06055-2; -. [Q06055-2]
DR DNASU; 517; -.
DR Ensembl; ENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
DR Ensembl; ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
DR Ensembl; ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
DR Ensembl; ENST00000552242; ENSP00000448801; ENSG00000135390. [Q06055-1]
DR Ensembl; ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
DR GeneID; 517; -.
DR KEGG; hsa:517; -.
DR UCSC; uc001sec.4; human. [Q06055-1]
DR CTD; 517; -.
DR DisGeNET; 517; -.
DR GeneCards; ATP5G2; -.
DR H-InvDB; HIX0201895; -.
DR HGNC; HGNC:842; ATP5G2.
DR HPA; HPA051469; -.
DR MIM; 603193; gene.
DR neXtProt; NX_Q06055; -.
DR OpenTargets; ENSG00000135390; -.
DR PharmGKB; PA25132; -.
DR eggNOG; KOG3025; Eukaryota.
DR eggNOG; COG0636; LUCA.
DR GeneTree; ENSGT00390000006210; -.
DR HOGENOM; HOG000235246; -.
DR HOVERGEN; HBG050605; -.
DR InParanoid; Q06055; -.
DR KO; K02128; -.
DR OMA; HPLKMYT; -.
DR OrthoDB; EOG091G13J1; -.
DR PhylomeDB; Q06055; -.
DR TreeFam; TF300140; -.
DR BioCyc; ZFISH:HS05994-MONOMER; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR ChiTaRS; ATP5G2; human.
DR GeneWiki; ATP5G2; -.
DR GenomeRNAi; 517; -.
DR PRO; PR:Q06055; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000135390; -.
DR CleanEx; HS_ATP5G2; -.
DR ExpressionAtlas; Q06055; baseline and differential.
DR Genevisible; Q06055; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; TAS:ProtInc.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0005215; F:transporter activity; NAS:ProtInc.
DR GO; GO:0006754; P:ATP biosynthetic process; TAS:Reactome.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; TAS:Reactome.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_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 2: Evidence at transcript level;
KW Alternative splicing; CF(0); Complete proteome;
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Mitochondrion; Polymorphism; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1 66 Mitochondrion. {ECO:0000250}.
FT CHAIN 67 141 ATP synthase F(0) complex subunit C2,
FT mitochondrial.
FT /FTId=PRO_0000002562.
FT TRANSMEM 82 102 Helical. {ECO:0000255}.
FT TRANSMEM 117 137 Helical. {ECO:0000255}.
FT SITE 124 124 Reversibly protonated during proton
FT transport. {ECO:0000250}.
FT VAR_SEQ 1 1 M -> MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCS
FT APLCLLCSGSSSPATAPHPLKM (in isoform 2).
FT {ECO:0000305}.
FT /FTId=VSP_037348.
FT VAR_SEQ 1 1 M -> MPELILSPATAPHPLKM (in isoform 3).
FT {ECO:0000305}.
FT /FTId=VSP_037349.
FT VARIANT 58 58 S -> I (in dbSNP:rs13819).
FT /FTId=VAR_011920.
FT VARIANT 141 141 M -> K (in dbSNP:rs1803177).
FT /FTId=VAR_011921.
FT CONFLICT 63 63 A -> T (in Ref. 3; BAG52118).
FT {ECO:0000305}.
FT CONFLICT 107 107 S -> F (in Ref. 3; BAG52118).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 70 138 ihamap:ATP_synth_c_bact [T]
FT MYHIT 103 124 ipat:ATPASE_C [T]
FT MYHIT 75 137 ipfam:ATP-synt_C [T]
SQ SEQUENCE 141 AA; 14637 MW; 6E627A504A7AE52D CRC64;
MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL TSLVSSRSFQ
TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
ALSEAMGLFC LMVAFLILFA M
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