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P30049

- ATPD_HUMAN

UniProt

P30049 - ATPD_HUMAN

Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP5D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    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 turnover in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    GO - Molecular functioni

    1. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
    3. transmembrane transporter activity Source: UniProtKB
    4. transporter activity Source: UniProtKB

    GO - Biological processi

    1. ATP biosynthetic process Source: UniProtKB
    2. ATP catabolic process Source: UniProtKB
    3. cellular metabolic process Source: Reactome
    4. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    5. oxidative phosphorylation Source: UniProtKB
    6. respiratory electron transport chain Source: Reactome
    7. response to copper ion Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit delta, mitochondrial
    Alternative name(s):
    F-ATPase delta subunit
    Gene namesi
    Name:ATP5D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:837. ATP5D.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB
    2. mitochondrial matrix Source: Reactome
    3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    4. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB
    5. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
    BLAST
    Chaini23 – 168146ATP synthase subunit delta, mitochondrialPRO_0000002661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
    Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
    Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP30049.
    PaxDbiP30049.
    PeptideAtlasiP30049.
    PRIDEiP30049.

    2D gel databases

    OGPiP30049.
    SWISS-2DPAGEP30049.
    UCD-2DPAGEP30049.

    PTM databases

    PhosphoSiteiP30049.

    Expressioni

    Gene expression databases

    BgeeiP30049.
    CleanExiHS_ATP5D.
    GenevestigatoriP30049.

    Organism-specific databases

    HPAiHPA002865.

    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 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi106998. 8 interactions.
    IntActiP30049. 6 interactions.
    STRINGi9606.ENSP00000215375.

    Structurei

    3D structure databases

    ProteinModelPortaliP30049.
    SMRiP30049. Positions 37-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase epsilon chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0355.
    HOGENOMiHOG000216023.
    HOVERGENiHBG001856.
    InParanoidiP30049.
    KOiK02134.
    OMAiLPHQAIF.
    OrthoDBiEOG7RNK2T.
    PhylomeDBiP30049.
    TreeFamiTF313029.

    Family and domain databases

    Gene3Di2.60.15.10. 1 hit.
    HAMAPiMF_00530. ATP_synth_epsil_bac.
    InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view]
    PANTHERiPTHR13822. PTHR13822. 1 hit.
    PfamiPF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view]
    ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P30049-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPAALLRRP GLGRLVRHAR AYAEAAAAPA AASGPNQMSF TFASPTQVFF    50
    NGANVRQVDV PTLTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS 100
    SGSIAVNADS SVQLLAEEAV TLDMLDLGAA KANLEKAQAE LVGTADEATR 150
    AEIQIRIEAN EALVKALE 168
    Length:168
    Mass (Da):17,490
    Last modified:October 1, 1994 - v2
    Checksum:iB7F0D1D01ADFDFE7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87916 mRNA. Translation: AAA08055.1.
    S87918 mRNA. Translation: ABB76284.1.
    X63422 mRNA. Translation: CAA45016.1.
    X63423 mRNA. Translation: CAA45017.1.
    CR542218 mRNA. Translation: CAG47014.1.
    AC004221 Genomic DNA. Translation: AAC04304.1.
    CH471139 Genomic DNA. Translation: EAW69532.1.
    CH471139 Genomic DNA. Translation: EAW69533.1.
    CH471139 Genomic DNA. Translation: EAW69534.1.
    BC002389 mRNA. Translation: AAH02389.1.
    BC004426 mRNA. Translation: AAH04426.1.
    BC018079 mRNA. Translation: AAH18079.1.
    CCDSiCCDS12058.1.
    PIRiS22348.
    RefSeqiNP_001001975.1. NM_001001975.1.
    NP_001678.1. NM_001687.4.
    UniGeneiHs.418668.

    Genome annotation databases

    EnsembliENST00000215375; ENSP00000215375; ENSG00000099624.
    ENST00000395633; ENSP00000378995; ENSG00000099624.
    ENST00000591660; ENSP00000464863; ENSG00000099624.
    GeneIDi513.
    KEGGihsa:513.
    UCSCiuc002lrn.3. human.

    Polymorphism databases

    DMDMi584812.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87916 mRNA. Translation: AAA08055.1 .
    S87918 mRNA. Translation: ABB76284.1 .
    X63422 mRNA. Translation: CAA45016.1 .
    X63423 mRNA. Translation: CAA45017.1 .
    CR542218 mRNA. Translation: CAG47014.1 .
    AC004221 Genomic DNA. Translation: AAC04304.1 .
    CH471139 Genomic DNA. Translation: EAW69532.1 .
    CH471139 Genomic DNA. Translation: EAW69533.1 .
    CH471139 Genomic DNA. Translation: EAW69534.1 .
    BC002389 mRNA. Translation: AAH02389.1 .
    BC004426 mRNA. Translation: AAH04426.1 .
    BC018079 mRNA. Translation: AAH18079.1 .
    CCDSi CCDS12058.1.
    PIRi S22348.
    RefSeqi NP_001001975.1. NM_001001975.1.
    NP_001678.1. NM_001687.4.
    UniGenei Hs.418668.

    3D structure databases

    ProteinModelPortali P30049.
    SMRi P30049. Positions 37-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106998. 8 interactions.
    IntActi P30049. 6 interactions.
    STRINGi 9606.ENSP00000215375.

    Chemistry

    DrugBanki DB01189. Desflurane.
    DB00228. Enflurane.
    DB01159. Halothane.
    DB00753. Isoflurane.
    DB01028. Methoxyflurane.
    DB01236. Sevoflurane.

    PTM databases

    PhosphoSitei P30049.

    Polymorphism databases

    DMDMi 584812.

    2D gel databases

    OGPi P30049.
    SWISS-2DPAGE P30049.
    UCD-2DPAGE P30049.

    Proteomic databases

    MaxQBi P30049.
    PaxDbi P30049.
    PeptideAtlasi P30049.
    PRIDEi P30049.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215375 ; ENSP00000215375 ; ENSG00000099624 .
    ENST00000395633 ; ENSP00000378995 ; ENSG00000099624 .
    ENST00000591660 ; ENSP00000464863 ; ENSG00000099624 .
    GeneIDi 513.
    KEGGi hsa:513.
    UCSCi uc002lrn.3. human.

    Organism-specific databases

    CTDi 513.
    GeneCardsi GC19P001241.
    HGNCi HGNC:837. ATP5D.
    HPAi HPA002865.
    MIMi 603150. gene.
    neXtProti NX_P30049.
    PharmGKBi PA25127.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0355.
    HOGENOMi HOG000216023.
    HOVERGENi HBG001856.
    InParanoidi P30049.
    KOi K02134.
    OMAi LPHQAIF.
    OrthoDBi EOG7RNK2T.
    PhylomeDBi P30049.
    TreeFami TF313029.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    GeneWikii ATP5D.
    GenomeRNAii 513.
    NextBioi 2123.
    PROi P30049.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30049.
    CleanExi HS_ATP5D.
    Genevestigatori P30049.

    Family and domain databases

    Gene3Di 2.60.15.10. 1 hit.
    HAMAPi MF_00530. ATP_synth_epsil_bac.
    InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view ]
    PANTHERi PTHR13822. PTHR13822. 1 hit.
    Pfami PF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view ]
    ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsi TIGR01216. ATP_synt_epsi. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of an import precursor of the delta-subunit of the human mitochondrial ATP synthase complex."
      Jordan E.M., Breen G.A.M.
      Biochim. Biophys. Acta 1130:123-126(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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].
      Tissue: Brain and Lung.
    6. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-38.
      Tissue: Liver.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATPD_HUMAN
    AccessioniPrimary (citable) accession number: P30049
    Secondary accession number(s): D6W5Y3, Q6FG90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3