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Q06055

- AT5G2_HUMAN

UniProt

Q06055 - AT5G2_HUMAN

Protein

ATP synthase F(0) complex subunit C2, mitochondrial

Gene

ATP5G2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
  1. 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. ATP synthesis coupled proton transport Source: InterPro
    3. response to ethanol Source: Ensembl

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:842. ATP5G2.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    ArrayExpressiQ06055.
    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. 5 interactions.
    IntActiQ06055. 3 interactions.
    STRINGi9606.ENSP00000377878.

    Structurei

    3D structure databases

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

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase C chain family.Curated

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0636.
    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. Align

    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

    MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL    50
    TSLVSSRSFQ TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII 100
    GYARNPSLKQ QLFSYAILGF ALSEAMGLFC LMVAFLILFA M 141
    Length:141
    Mass (Da):14,637
    Last modified:February 1, 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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31812.1. [Q06055-3 ]
    CCDS8863.2. [Q06055-2 ]
    PIRi S34067.
    RefSeqi NP_001002031.1. NM_001002031.2. [Q06055-3 ]
    NP_005167.2. NM_005176.5. [Q06055-2 ]
    UniGenei Hs.524464.

    3D structure databases

    ProteinModelPortali Q06055.
    SMRi Q06055. Positions 68-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107002. 5 interactions.
    IntActi Q06055. 3 interactions.
    STRINGi 9606.ENSP00000377878.

    PTM databases

    PhosphoSitei Q06055.

    Polymorphism databases

    DMDMi 461592.

    Proteomic databases

    PaxDbi Q06055.
    PRIDEi Q06055.

    Protocols and materials databases

    DNASUi 517.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338662 ; ENSP00000340315 ; ENSG00000135390 . [Q06055-3 ]
    ENST00000394349 ; ENSP00000377878 ; ENSG00000135390 . [Q06055-2 ]
    ENST00000549164 ; ENSP00000447317 ; ENSG00000135390 . [Q06055-1 ]
    ENST00000602871 ; ENSP00000473535 ; ENSG00000135390 . [Q06055-1 ]
    GeneIDi 517.
    KEGGi hsa:517.
    UCSCi uc001sec.3. human. [Q06055-2 ]
    uc001sed.3. human. [Q06055-3 ]
    uc009znc.3. human. [Q06055-1 ]

    Organism-specific databases

    CTDi 517.
    GeneCardsi GC12M054030.
    H-InvDB HIX0201895.
    HGNCi HGNC:842. ATP5G2.
    HPAi HPA051469.
    MIMi 603193. gene.
    neXtProti NX_Q06055.
    PharmGKBi PA25132.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0636.
    HOGENOMi HOG000235246.
    HOVERGENi HBG050605.
    InParanoidi Q06055.
    KOi K02128.
    OMAi HPLKMYT.
    OrthoDBi EOG7VHT0K.
    PhylomeDBi Q06055.
    TreeFami TF300140.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    ChiTaRSi ATP5G2. human.
    GeneWikii ATP5G2.
    GenomeRNAii 517.
    NextBioi 2145.
    PROi Q06055.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06055.
    Bgeei Q06055.
    CleanExi HS_ATP5G2.
    Genevestigatori Q06055.

    Family and domain databases

    Gene3Di 1.20.20.10. 1 hit.
    HAMAPi MF_01396. ATP_synth_c_bact.
    InterProi IPR000454. ATPase_F0-cplx_csu.
    IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
    IPR002379. ATPase_proteolipid_c_like_dom.
    [Graphical view ]
    Pfami PF00137. ATP-synt_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00124. ATPASEC.
    SUPFAMi SSF81333. SSF81333. 1 hit.
    PROSITEi PS00605. ATPASE_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiAT5G2_HUMAN
    AccessioniPrimary (citable) accession number: Q06055
    Secondary accession number(s): B3KQQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 138 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