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Protein

ATP synthase F(0) complex subunit C2, mitochondrial

Gene

ATP5G2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei124 – 1241Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. lipid binding Source: UniProtKB-KW
  3. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular metabolic process Source: Reactome
  3. mitochondrial ATP synthesis coupled proton transport Source: Reactome
  4. respiratory electron transport chain Source: Reactome
  5. response to ethanol Source: Ensembl
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit C2, mitochondrial
Alternative name(s):
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
Gene namesi
Name:ATP5G2
ORF Names:PSEC0033
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:842. ATP5G2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Transmembranei117 – 13721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: Reactome
  3. mitochondrial proton-transporting ATP synthase complex Source: ProtInc
  4. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6666MitochondrionBy similarityAdd
BLAST
Chaini67 – 14175ATP synthase F(0) complex subunit C2, mitochondrialPRO_0000002562Add
BLAST

Proteomic databases

PaxDbiQ06055.
PRIDEiQ06055.

PTM databases

PhosphoSiteiQ06055.

Expressioni

Gene expression databases

BgeeiQ06055.
CleanExiHS_ATP5G2.
GenevestigatoriQ06055.

Organism-specific databases

HPAiHPA051469.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

Protein-protein interaction databases

BioGridi107002. 4 interactions.
IntActiQ06055. 3 interactions.
STRINGi9606.ENSP00000377878.

Structurei

3D structure databases

ProteinModelPortaliQ06055.
SMRiQ06055. Positions 68-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiQ06055.
KOiK02128.
OMAiHPLKMYT.
OrthoDBiEOG7VHT0K.
PhylomeDBiQ06055.
TreeFamiTF300140.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06055-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL
60 70 80 90 100
TSLVSSRSFQ TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII
110 120 130 140
GYARNPSLKQ QLFSYAILGF ALSEAMGLFC LMVAFLILFA M
Length:141
Mass (Da):14,637
Last modified:January 31, 1994 - v1
Checksum:i6E627A504A7AE52D
GO
Isoform 2 (identifier: Q06055-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCSAPLCLLCSGSSSPATAPHPLKM

Note: Derived from EST data.

Show »
Length:198
Mass (Da):20,513
Checksum:i6ACCBD405F313CC8
GO
Isoform 3 (identifier: Q06055-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILSPATAPHPLKM

Note: Derived from EST data.

Show »
Length:157
Mass (Da):16,334
Checksum:i84032DCC16E10CED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631A → T in BAG52118 (PubMed:16303743).Curated
Sequence conflicti107 – 1071S → F in BAG52118 (PubMed:16303743).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581S → I.
Corresponds to variant rs13819 [ dbSNP | Ensembl ].
VAR_011920
Natural varianti141 – 1411M → K.
Corresponds to variant rs1803177 [ dbSNP | Ensembl ].
VAR_011921

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPELILYVAITLSVAERLVG PGHACAEPSFRSSRCSAPLC LLCSGSSSPATAPHPLKM in isoform 2. CuratedVSP_037348
Alternative sequencei1 – 11M → MPELILSPATAPHPLKM in isoform 3. CuratedVSP_037349

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69908 Genomic DNA. Translation: CAA49533.1.
D13119 mRNA. Translation: BAA02421.1.
AK075351 mRNA. Translation: BAG52118.1.
AC073594 Genomic DNA. No translation available.
BC020826 mRNA. Translation: AAH20826.1.
CCDSiCCDS31812.1. [Q06055-3]
CCDS8863.2. [Q06055-2]
PIRiS34067.
RefSeqiNP_001002031.1. NM_001002031.2. [Q06055-3]
NP_005167.2. NM_005176.5. [Q06055-2]
UniGeneiHs.524464.

Genome annotation databases

EnsembliENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
ENST00000552242; ENSP00000448801; ENSG00000135390. [Q06055-1]
ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
GeneIDi517.
KEGGihsa:517.
UCSCiuc001sec.3. human. [Q06055-2]
uc001sed.3. human. [Q06055-3]
uc009znc.3. human. [Q06055-1]

Polymorphism databases

DMDMi461592.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69908 Genomic DNA. Translation: CAA49533.1.
D13119 mRNA. Translation: BAA02421.1.
AK075351 mRNA. Translation: BAG52118.1.
AC073594 Genomic DNA. No translation available.
BC020826 mRNA. Translation: AAH20826.1.
CCDSiCCDS31812.1. [Q06055-3]
CCDS8863.2. [Q06055-2]
PIRiS34067.
RefSeqiNP_001002031.1. NM_001002031.2. [Q06055-3]
NP_005167.2. NM_005176.5. [Q06055-2]
UniGeneiHs.524464.

3D structure databases

ProteinModelPortaliQ06055.
SMRiQ06055. Positions 68-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107002. 4 interactions.
IntActiQ06055. 3 interactions.
STRINGi9606.ENSP00000377878.

PTM databases

PhosphoSiteiQ06055.

Polymorphism databases

DMDMi461592.

Proteomic databases

PaxDbiQ06055.
PRIDEiQ06055.

Protocols and materials databases

DNASUi517.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
ENST00000552242; ENSP00000448801; ENSG00000135390. [Q06055-1]
ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
GeneIDi517.
KEGGihsa:517.
UCSCiuc001sec.3. human. [Q06055-2]
uc001sed.3. human. [Q06055-3]
uc009znc.3. human. [Q06055-1]

Organism-specific databases

CTDi517.
GeneCardsiGC12M054030.
H-InvDBHIX0201895.
HGNCiHGNC:842. ATP5G2.
HPAiHPA051469.
MIMi603193. gene.
neXtProtiNX_Q06055.
PharmGKBiPA25132.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0636.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiQ06055.
KOiK02128.
OMAiHPLKMYT.
OrthoDBiEOG7VHT0K.
PhylomeDBiQ06055.
TreeFamiTF300140.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5G2. human.
GeneWikiiATP5G2.
GenomeRNAii517.
NextBioi2145.
PROiQ06055.
SOURCEiSearch...

Gene expression databases

BgeeiQ06055.
CleanExiHS_ATP5G2.
GenevestigatoriQ06055.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase."
    Dyer M.R., Walker J.E.
    Biochem. J. 293:51-64(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria."
    Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.
    Biochim. Biophys. Acta 1173:87-90(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    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.
    DNA Res. 12:117-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The finished DNA sequence of human chromosome 12."
    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.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  6. "Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex."
    Farrell L.B., Nagley P.
    Biochem. Biophys. Res. Commun. 144:1257-1264(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-141 (ISOFORMS 1/2/3).
    Tissue: Liver.

Entry informationi

Entry nameiAT5G2_HUMAN
AccessioniPrimary (citable) accession number: Q06055
Secondary accession number(s): B3KQQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: January 31, 1994
Last modified: March 3, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.