P30049 (ATPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit delta, mitochondrial

Alternative name(s):
F-ATPase delta subunit

Gene names

Name:

ATP5D

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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). 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.
Sequence similarities	Belongs to the ATPase epsilon chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Non-traceable author statement PubMed 12539966. Source: UniProtKB 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
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Non-traceable author statement PubMed 12539966. Source: UniProtKB
Molecular_function	proton-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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 22	22	Mitochondrion Ref.6
	Chain	23 – 168	146	ATP synthase subunit delta, mitochondrial		PRO_0000002661
Amino acid modifications
	Cross-link	136		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30049 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: B7F0D1D01ADFDFE7	FASTA	168	17,490
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00024920.
PIR	S22348.
RefSeq	NP_001001975.1. NM_001001975.1. NP_001678.1. NM_001687.4.
UniGene	Hs.418668.
3D structure databases
ProteinModelPortal	P30049.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30049. 4 interactions.
STRING	9606.ENSP00000215375.
PTM databases
PhosphoSite	P30049.
Polymorphism databases
DMDM	584812.
2D gel databases
OGP	P30049.
SWISS-2DPAGE	P30049.
UCD-2DPAGE	P30049.
Proteomic databases
PaxDb	P30049.
PeptideAtlas	P30049.
PRIDE	P30049.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000215375; ENSP00000215375; ENSG00000099624. ENST00000395633; ENSP00000378995; ENSG00000099624. ENST00000591660; ENSP00000464863; ENSG00000099624.
GeneID	513.
KEGG	hsa:513.
UCSC	uc002lrn.3. human.
Organism-specific databases
CTD	513.
GeneCards	GC19P001241.
HGNC	HGNC:837. ATP5D.
HPA	HPA002865.
MIM	603150. gene.
neXtProt	NX_P30049.
PharmGKB	PA25127.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0355.
HOGENOM	HOG000216023.
HOVERGEN	HBG001856.
InParanoid	P30049.
KO	K02134.
OMA	GILANHI.
OrthoDB	EOG4894NT.
PhylomeDB	P30049.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	P30049.
CleanEx	HS_ATP5D.
Genevestigator	P30049.
GermOnline	ENSG00000099624. Homo sapiens.
Family and domain databases
Gene3D	2.60.15.10. 1 hit.
InterPro	IPR001469. ATPase_F1-cplx_dsu/esu. IPR020547. ATPase_F1-cplx_dsu/esu_C. IPR020546. ATPase_F1-cplx_dsu/esu_N. [Graphical view]
PANTHER	PTHR13822. PTHR13822. 1 hit.
Pfam	PF02823. ATP-synt_DE_N. 1 hit. [Graphical view]
ProDom	PD000944. ATPase_F1-cplx_dsu/esu. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF46604. ATPsynt_DE. 1 hit. SSF51344. ATPsynt_DE. 1 hit.
TIGRFAMs	TIGR01216. ATP_synt_epsi. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB01189. Desflurane. DB00228. Enflurane. DB01159. Halothane. DB00753. Isoflurane. DB01028. Methoxyflurane. DB01236. Sevoflurane.
GenomeRNAi	513.
NextBio	2123.
SOURCE	Search...

Entry information

Entry name

ATPD_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.