Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P30049 (ATPD_HUMAN)

Last modified November 24, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

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).

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the ATPase epsilon chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Cross-link136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P30049-1 [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: 1531933] [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: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton 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: 15489334] [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: 1286669] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-38.
Tissue: Liver.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

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.
BC002389 mRNA. Translation: AAH02389.1.
BC004426 mRNA. Translation: AAH04426.1.
BC018079 mRNA. Translation: AAH18079.1.
IPIIPI00024920.
PIRS22348.
RefSeqNP_001001975.1.
NP_001678.1.
UniGeneHs.418668

3D structure databases

SMRP30049. Positions 37-167.
ModBaseSearch...

Protein-protein interaction databases

IntActP30049. 5 interactions.
STRINGP30049.

PTM databases

PhosphoSiteP30049.

2-D gel databases

SWISS-2DPAGEP30049.
OGPP30049.

Proteomic databases

PeptideAtlasP30049.
PRIDEP30049.

Genome annotation databases

EnsemblENST00000215375; ENSP00000215375; ENSG00000099624; Homo sapiens. [Genome view]
ENST00000395633; ENSP00000378995; ENSG00000099624; Homo sapiens. [Genome view]
GeneID513.
KEGGhsa:513.
UCSCuc002lrn.1. human.

Organism-specific databases

CTD513.
GeneCardsGC19P001192.
HGNCHGNC:837. ATP5D.
HPAHPA002865.
MIM603150. gene.
PharmGKBPA25127.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30049.
HOVERGENP30049.
OMAQVDVPTQ
OrthoDBEOG9STVQZ

Enzyme and pathway databases

ReactomeREACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
REACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpressP30049.
BgeeP30049.
CleanExHS_ATP5D.
GenevestigatorP30049.
GermOnlineENSG00000099624. Homo sapiens.

Family and domain databases

InterProIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020547. ATPase_F1-cplx_dsu/esu_C.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]
Gene3DG3DSA:1.20.5.440. ATPase_F1_d/e. 1 hit.
G3DSA:2.60.15.10. ATPase_F1_d/e. 1 hit.
PANTHERPTHR13822. ATPase_F1_d/e. 1 hit.
PfamPF00401. ATP-synt_DE. 1 hit.
PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01216. ATP_synt_epsi. 1 hit.
ProtoNetSearch...

Other Resources

DrugBankDB01189. Desflurane.
DB00228. Enflurane.
DB01159. Halothane.
DB00753. Isoflurane.
DB01028. Methoxyflurane.
DB01236. Sevoflurane.
NextBio2123.
SOURCESearch...

Entry information

Entry nameATPD_HUMAN
AccessionPrimary (citable) accession number: P30049
Secondary accession number(s): Q6FG90
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: November 24, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 19

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents