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Protein

ATP synthase F(0) complex subunit C2, mitochondrial

Gene

Atp5g2

Organism
Mus musculus (Mouse)
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
Sitei129 – 1291Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-163210. 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
ATPase protein 9
ATPase subunit c
Gene namesi
Name:Atp5g2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1915192. Atp5g2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease).

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7171MitochondrionBy similarityAdd
BLAST
Chaini72 – 14675ATP synthase F(0) complex subunit C2, mitochondrialPRO_0000002563Add
BLAST

Proteomic databases

MaxQBiP56383.
PaxDbiP56383.
PRIDEiP56383.
TopDownProteomicsiP56383.

PTM databases

iPTMnetiP56383.
PhosphoSiteiP56383.

Expressioni

Gene expression databases

BgeeiP56383.
ExpressionAtlasiP56383. baseline and differential.
GenevisibleiP56383. MM.

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

STRINGi10090.ENSMUSP00000136537.

Structurei

3D structure databases

ProteinModelPortaliP56383.
SMRiP56383. Positions 73-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3025. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiP56383.
KOiK02128.
OMAiHPLKMYT.
OrthoDBiEOG7VHT0K.
PhylomeDBiP56383.
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]

Sequencei

Sequence statusi: Complete.

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

P56383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYACSKFVST RSLIRSTSLR STSQLLSRPL SAVELKRPQM PTDESLSSLA
60 70 80 90 100
VRRPLTSLIP SRSFQTSAIS RDIDTAAKFI GAGAATVGVA GSGAGIGTVF
110 120 130 140
GSLIIGYARN PSLKQQLFSY AILGFALSEA MGLFCLMVAF LILFAM
Length:146
Mass (Da):15,476
Last modified:August 16, 2004 - v2
Checksum:iD49C8172BF16FBBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002311 mRNA. Translation: BAB22005.1.
AK007747 mRNA. Translation: BAB25231.1.
AK012279 mRNA. Translation: BAB28137.1.
AK075793 mRNA. Translation: BAC35962.1.
BC006813 mRNA. Translation: AAH06813.1.
BC081437 mRNA. Translation: AAH81437.1.
BC106138 mRNA. Translation: AAI06139.1.
CCDSiCCDS27888.1.
RefSeqiNP_080744.1. NM_026468.2.
UniGeneiMm.10314.
Mm.381662.

Genome annotation databases

EnsembliENSMUST00000075630; ENSMUSP00000075057; ENSMUSG00000062683.
ENSMUST00000185641; ENSMUSP00000140414; ENSMUSG00000062683.
GeneIDi67942.
KEGGimmu:67942.
UCSCiuc007xwr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002311 mRNA. Translation: BAB22005.1.
AK007747 mRNA. Translation: BAB25231.1.
AK012279 mRNA. Translation: BAB28137.1.
AK075793 mRNA. Translation: BAC35962.1.
BC006813 mRNA. Translation: AAH06813.1.
BC081437 mRNA. Translation: AAH81437.1.
BC106138 mRNA. Translation: AAI06139.1.
CCDSiCCDS27888.1.
RefSeqiNP_080744.1. NM_026468.2.
UniGeneiMm.10314.
Mm.381662.

3D structure databases

ProteinModelPortaliP56383.
SMRiP56383. Positions 73-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000136537.

PTM databases

iPTMnetiP56383.
PhosphoSiteiP56383.

Proteomic databases

MaxQBiP56383.
PaxDbiP56383.
PRIDEiP56383.
TopDownProteomicsiP56383.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075630; ENSMUSP00000075057; ENSMUSG00000062683.
ENSMUST00000185641; ENSMUSP00000140414; ENSMUSG00000062683.
GeneIDi67942.
KEGGimmu:67942.
UCSCiuc007xwr.1. mouse.

Organism-specific databases

CTDi517.
MGIiMGI:1915192. Atp5g2.

Phylogenomic databases

eggNOGiKOG3025. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiP56383.
KOiK02128.
OMAiHPLKMYT.
OrthoDBiEOG7VHT0K.
PhylomeDBiP56383.
TreeFamiTF300140.

Enzyme and pathway databases

ReactomeiR-MMU-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

PROiP56383.
SOURCEiSearch...

Gene expression databases

BgeeiP56383.
ExpressionAtlasiP56383. baseline and differential.
GenevisibleiP56383. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Pancreas.
  2. "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].
    Strain: 129, C57BL/6J and FVB/N.
    Tissue: Brain, Colon and Mammary tumor.

Entry informationi

Entry nameiAT5G2_MOUSE
AccessioniPrimary (citable) accession number: P56383
Secondary accession number(s): Q3KQM0, Q9CQ23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.