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ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase proteolipid P2) (ATP synthase proton-transporting mitochondrial F(0) complex subunit C2) (ATPase protein 9) (ATPase subunit c)

 AT5G2_HUMAN             Reviewed;         141 AA.
Q06055; B3KQQ6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-SEP-2018, entry version 168.
RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase lipid-binding protein;
AltName: Full=ATP synthase membrane subunit c locus 2 {ECO:0000312|HGNC:HGNC:842};
AltName: Full=ATP synthase proteolipid P2;
AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C2;
AltName: Full=ATPase protein 9;
AltName: Full=ATPase subunit c;
Flags: Precursor;
Name=ATP5MC2 {ECO:0000312|HGNC:HGNC:842};
Synonyms=ATP5G2 {ECO:0000312|HGNC:HGNC:842}; ORFNames=PSEC0033;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8328972; DOI=10.1042/bj2930051;
Dyer M.R., Walker J.E.;
"Sequences of members of the human gene family for the c subunit of
mitochondrial ATP synthase.";
Biochem. J. 293:51-64(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8485160; DOI=10.1016/0167-4781(93)90249-D;
Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.;
"Molecular cloning and sequence of two cDNAs for human subunit c of
H(+)-ATP synthase in mitochondria.";
Biochim. Biophys. Acta 1173:87-90(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 87-141 (ISOFORMS 1/2/3).
TISSUE=Liver;
PubMed=2883974; DOI=10.1016/0006-291X(87)91446-X;
Farrell L.B., Nagley P.;
"Human liver cDNA clones encoding proteolipid subunit 9 of the
mitochondrial ATPase complex.";
Biochem. Biophys. Res. Commun. 144:1257-1264(1987).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core and F(0) - containing the membrane
proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain. A homomeric c-ring of probably 10 subunits is part of the
complex rotary element.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q06055-1; Sequence=Displayed;
Name=2;
IsoId=Q06055-2; Sequence=VSP_037348;
Note=Derived from EST data.;
Name=3;
IsoId=Q06055-3; Sequence=VSP_037349;
Note=Derived from EST data.;
-!- MISCELLANEOUS: There are three genes which encode the
mitochondrial ATP synthase proteolipid and they specify precursors
with different import sequences but identical mature proteins. Is
the major protein stored in the storage bodies of animals or
humans affected with ceroid lipofuscinosis (Batten disease).
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X69908; CAA49533.1; -; Genomic_DNA.
EMBL; D13119; BAA02421.1; -; mRNA.
EMBL; AK075351; BAG52118.1; -; mRNA.
EMBL; AC073594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020826; AAH20826.1; -; mRNA.
CCDS; CCDS31812.1; -. [Q06055-3]
CCDS; CCDS81694.1; -. [Q06055-1]
PIR; S34067; S34067.
RefSeq; NP_001002031.1; NM_001002031.2. [Q06055-3]
RefSeq; NP_001317198.1; NM_001330269.1. [Q06055-1]
RefSeq; NP_005167.2; NM_005176.5. [Q06055-1]
RefSeq; XP_016874949.1; XM_017019460.1. [Q06055-2]
RefSeq; XP_016874950.1; XM_017019461.1. [Q06055-3]
UniGene; Hs.524464; -.
ProteinModelPortal; Q06055; -.
SMR; Q06055; -.
BioGrid; 107002; 3.
IntAct; Q06055; 3.
STRING; 9606.ENSP00000377878; -.
iPTMnet; Q06055; -.
PhosphoSitePlus; Q06055; -.
DMDM; 461592; -.
EPD; Q06055; -.
MaxQB; Q06055; -.
PaxDb; Q06055; -.
PeptideAtlas; Q06055; -.
PRIDE; Q06055; -.
ProteomicsDB; 58411; -.
ProteomicsDB; 58412; -. [Q06055-2]
ProteomicsDB; 58413; -. [Q06055-3]
TopDownProteomics; Q06055-1; -. [Q06055-1]
TopDownProteomics; Q06055-2; -. [Q06055-2]
TopDownProteomics; Q06055-3; -. [Q06055-3]
DNASU; 517; -.
Ensembl; ENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
Ensembl; ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
Ensembl; ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
Ensembl; ENST00000552242; ENSP00000448801; ENSG00000135390. [Q06055-1]
Ensembl; ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
GeneID; 517; -.
KEGG; hsa:517; -.
UCSC; uc001sec.4; human. [Q06055-1]
CTD; 517; -.
DisGeNET; 517; -.
EuPathDB; HostDB:ENSG00000135390.17; -.
GeneCards; ATP5MC2; -.
H-InvDB; HIX0201895; -.
HGNC; HGNC:842; ATP5MC2.
HPA; HPA051469; -.
MIM; 603193; gene.
neXtProt; NX_Q06055; -.
OpenTargets; ENSG00000135390; -.
PharmGKB; PA25132; -.
eggNOG; KOG3025; Eukaryota.
eggNOG; COG0636; LUCA.
GeneTree; ENSGT00390000006210; -.
HOGENOM; HOG000235246; -.
HOVERGEN; HBG050605; -.
InParanoid; Q06055; -.
KO; K02128; -.
OMA; HPLKMYT; -.
OrthoDB; EOG091G13J1; -.
PhylomeDB; Q06055; -.
TreeFam; TF300140; -.
Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-HSA-8949613; Cristae formation.
ChiTaRS; ATP5G2; human.
GeneWiki; ATP5G2; -.
GenomeRNAi; 517; -.
PRO; PR:Q06055; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135390; Expressed in 232 organ(s), highest expression level in apex of heart.
CleanEx; HS_ATP5G2; -.
ExpressionAtlas; Q06055; baseline and differential.
Genevisible; Q06055; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; TAS:ProtInc.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0005215; F:transporter activity; NAS:ProtInc.
GO; GO:0006754; P:ATP biosynthetic process; TAS:Reactome.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0042407; P:cristae formation; TAS:Reactome.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
PROSITE; PS00605; ATPASE_C; 1.
2: Evidence at transcript level;
Alternative splicing; CF(0); Complete proteome;
Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
Mitochondrion; Polymorphism; Reference proteome; Transit peptide;
Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 66 Mitochondrion. {ECO:0000250}.
CHAIN 67 141 ATP synthase F(0) complex subunit C2,
mitochondrial.
/FTId=PRO_0000002562.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
SITE 124 124 Reversibly protonated during proton
transport. {ECO:0000250}.
VAR_SEQ 1 1 M -> MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCS
APLCLLCSGSSSPATAPHPLKM (in isoform 2).
{ECO:0000305}.
/FTId=VSP_037348.
VAR_SEQ 1 1 M -> MPELILSPATAPHPLKM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_037349.
VARIANT 58 58 S -> I (in dbSNP:rs13819).
/FTId=VAR_011920.
VARIANT 141 141 M -> K (in dbSNP:rs1803177).
/FTId=VAR_011921.
CONFLICT 63 63 A -> T (in Ref. 3; BAG52118).
{ECO:0000305}.
CONFLICT 107 107 S -> F (in Ref. 3; BAG52118).
{ECO:0000305}.
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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