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Q06055 (AT5G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATP5G2
ORF Names:PSEC0033
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01396

Subunit structure

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.

Subcellular location

Mitochondrion membrane; Multi-pass membrane protein HAMAP-Rule MF_01396.

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).

Sequence similarities

Belongs to the ATPase C chain family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06055-1)

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.
Isoform 2 (identifier: Q06055-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCSAPLCLLCSGSSSPATAPHPLKM
Note: Derived from EST data.
Isoform 3 (identifier: Q06055-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILSPATAPHPLKM
Note: Derived from EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6666Mitochondrion By similarity
Chain67 – 14175ATP synthase F(0) complex subunit C2, mitochondrial HAMAP-Rule MF_01396
PRO_0000002562

Regions

Transmembrane82 – 10221Helical; Potential
Transmembrane117 – 13721Helical; Potential

Sites

Site1241Reversibly protonated during proton transport By similarity

Natural variations

Alternative sequence11M → MPELILYVAITLSVAERLVG PGHACAEPSFRSSRCSAPLC LLCSGSSSPATAPHPLKM in isoform 2.
VSP_037348
Alternative sequence11M → MPELILSPATAPHPLKM in isoform 3.
VSP_037349
Natural variant581S → I.
Corresponds to variant rs13819 [ dbSNP | Ensembl ].
VAR_011920
Natural variant1411M → K.
Corresponds to variant rs1803177 [ dbSNP | Ensembl ].
VAR_011921

Experimental info

Sequence conflict631A → T in BAG52118. Ref.3
Sequence conflict1071S → F in BAG52118. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6E627A504A7AE52D

FASTA14114,637
        10         20         30         40         50         60 
MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL TSLVSSRSFQ 

        70         80         90        100        110        120 
TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF 

       130        140 
ALSEAMGLFC LMVAFLILFA M 

« Hide

Isoform 2 [UniParc].

Checksum: 6ACCBD405F313CC8
Show »

FASTA19820,513
Isoform 3 [UniParc].

Checksum: 84032DCC16E10CED
Show »

FASTA15716,334

References

« Hide 'large scale' references
[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(1993) [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(1993) [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. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [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. expand/collapse author list , 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(2006) [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(2004) [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(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-141 (ISOFORMS 1/2/3).
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS34067.
RefSeqNP_001002031.1. NM_001002031.2.
NP_005167.2. NM_005176.5.
UniGeneHs.524464.

3D structure databases

ProteinModelPortalQ06055.
SMRQ06055. Positions 68-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107002. 5 interactions.
IntActQ06055. 3 interactions.
STRING9606.ENSP00000377878.

PTM databases

PhosphoSiteQ06055.

Polymorphism databases

DMDM461592.

Proteomic databases

PaxDbQ06055.
PRIDEQ06055.

Protocols and materials databases

DNASU517.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
GeneID517.
KEGGhsa:517.
UCSCuc001sec.3. human. [Q06055-2]
uc001sed.3. human. [Q06055-3]
uc009znc.3. human. [Q06055-1]

Organism-specific databases

CTD517.
GeneCardsGC12M054030.
H-InvDBHIX0201895.
HGNCHGNC:842. ATP5G2.
HPAHPA051469.
MIM603193. gene.
neXtProtNX_Q06055.
PharmGKBPA25132.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000235246.
HOVERGENHBG050605.
InParanoidQ06055.
KOK02128.
OMAHPLKMYT.
OrthoDBEOG7VHT0K.
PhylomeDBQ06055.
TreeFamTF300140.

Gene expression databases

ArrayExpressQ06055.
BgeeQ06055.
CleanExHS_ATP5G2.
GenevestigatorQ06055.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5G2. human.
GeneWikiATP5G2.
GenomeRNAi517.
NextBio2145.
PROQ06055.
SOURCESearch...

Entry information

Entry nameAT5G2_HUMAN
AccessionPrimary (citable) accession number: Q06055
Secondary accession number(s): B3KQQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM