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P30049 (ATPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene names
Name:ATP5D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 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. HAMAP-Rule MF_00530

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 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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane HAMAP-Rule MF_00530.

Sequence similarities

Belongs to the ATPase epsilon chain family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Non-traceable author statement PubMed 12539966. Source: UniProtKB

ATP catabolic process

Non-traceable author statement PubMed 12539966. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial ATP synthesis coupled proton transport

Non-traceable author statement PubMed 12539966. Source: UniProtKB

oxidative phosphorylation

Non-traceable author statement PubMed 12539966. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

response to copper ion

Non-traceable author statement PubMed 12539966. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrial proton-transporting ATP synthase complex, catalytic core F(1)

Non-traceable author statement PubMed 12539966. Source: UniProtKB

mitochondrion

Non-traceable author statement PubMed 12887009. Source: UniProtKB

   Molecular_functionproton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

transporter activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Ref.6
Chain23 – 168146ATP synthase subunit delta, mitochondrial HAMAP-Rule MF_00530
PRO_0000002661

Amino acid modifications

Modified residue1361N6-acetyllysine; alternate By similarity
Modified residue1361N6-succinyllysine; alternate By similarity
Modified residue1651N6-acetyllysine; alternate By similarity
Modified residue1651N6-succinyllysine; alternate By similarity
Cross-link136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P30049 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: B7F0D1D01ADFDFE7

FASTA16817,490
        10         20         30         40         50         60 
MLPAALLRRP GLGRLVRHAR AYAEAAAAPA AASGPNQMSF TFASPTQVFF NGANVRQVDV 

        70         80         90        100        110        120 
PTLTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS SGSIAVNADS SVQLLAEEAV 

       130        140        150        160 
TLDMLDLGAA KANLEKAQAE LVGTADEATR AEIQIRIEAN EALVKALE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS22348.
RefSeqNP_001001975.1. NM_001001975.1.
NP_001678.1. NM_001687.4.
UniGeneHs.418668.

3D structure databases

ProteinModelPortalP30049.
SMRP30049. Positions 37-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106998. 8 interactions.
IntActP30049. 6 interactions.
STRING9606.ENSP00000215375.

Chemistry

DrugBankDB01189. Desflurane.
DB00228. Enflurane.
DB01159. Halothane.
DB00753. Isoflurane.
DB01028. Methoxyflurane.
DB01236. Sevoflurane.

PTM databases

PhosphoSiteP30049.

Polymorphism databases

DMDM584812.

2D gel databases

OGPP30049.
SWISS-2DPAGEP30049.
UCD-2DPAGEP30049.

Proteomic databases

PaxDbP30049.
PeptideAtlasP30049.
PRIDEP30049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215375; ENSP00000215375; ENSG00000099624.
ENST00000395633; ENSP00000378995; ENSG00000099624.
ENST00000591660; ENSP00000464863; ENSG00000099624.
GeneID513.
KEGGhsa:513.
UCSCuc002lrn.3. human.

Organism-specific databases

CTD513.
GeneCardsGC19P001241.
HGNCHGNC:837. ATP5D.
HPAHPA002865.
MIM603150. gene.
neXtProtNX_P30049.
PharmGKBPA25127.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0355.
HOGENOMHOG000216023.
HOVERGENHBG001856.
InParanoidP30049.
KOK02134.
OMALPHQAIF.
OrthoDBEOG7RNK2T.
PhylomeDBP30049.
TreeFamTF313029.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP30049.
CleanExHS_ATP5D.
GenevestigatorP30049.

Family and domain databases

Gene3D2.60.15.10. 1 hit.
HAMAPMF_00530. ATP_synth_epsil_bac.
InterProIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view]
PANTHERPTHR13822. PTHR13822. 1 hit.
PfamPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsTIGR01216. ATP_synt_epsi. 1 hit.
ProtoNetSearch...

Other

GeneWikiATP5D.
GenomeRNAi513.
NextBio2123.
PROP30049.
SOURCESearch...

Entry information

Entry nameATPD_HUMAN
AccessionPrimary (citable) accession number: P30049
Secondary accession number(s): D6W5Y3, Q6FG90
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 138 of the entry and version 2 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 chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM