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Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP5D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. ATP synthesis coupled proton transport Source: GO_Central
  4. cellular metabolic process Source: Reactome
  5. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  6. oxidative phosphorylation Source: UniProtKB
  7. respiratory electron transport chain Source: Reactome
  8. response to copper ion Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

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
Complete GO annotation...

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. 9 interactions.
IntActiP30049. 7 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.
GeneTreeiENSGT00390000017576.
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

        10         20         30         40         50
MLPAALLRRP GLGRLVRHAR AYAEAAAAPA AASGPNQMSF TFASPTQVFF
60 70 80 90 100
NGANVRQVDV PTLTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS
110 120 130 140 150
SGSIAVNADS SVQLLAEEAV TLDMLDLGAA KANLEKAQAE LVGTADEATR
160
AEIQIRIEAN EALVKALE
Length:168
Mass (Da):17,490
Last modified:October 1, 1994 - v2
Checksum:iB7F0D1D01ADFDFE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106998. 9 interactions.
IntActiP30049. 7 interactions.
STRINGi9606.ENSP00000215375.

Chemistry

DrugBankiDB01189. Desflurane.
DB00228. Enflurane.
DB01159. Halothane.
DB00753. Isoflurane.
DB01028. Methoxyflurane.
DB01236. Sevoflurane.

PTM databases

PhosphoSiteiP30049.

Polymorphism databases

DMDMi584812.

2D gel databases

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

Proteomic databases

MaxQBiP30049.
PaxDbiP30049.
PeptideAtlasiP30049.
PRIDEiP30049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi513.
GeneCardsiGC19P001241.
HGNCiHGNC:837. ATP5D.
HPAiHPA002865.
MIMi603150. gene.
neXtProtiNX_P30049.
PharmGKBiPA25127.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0355.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
HOVERGENiHBG001856.
InParanoidiP30049.
KOiK02134.
OMAiLPHQAIF.
OrthoDBiEOG7RNK2T.
PhylomeDBiP30049.
TreeFamiTF313029.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5D. human.
GeneWikiiATP5D.
GenomeRNAii513.
NextBioi2123.
PROiP30049.
SOURCEiSearch...

Gene expression databases

BgeeiP30049.
CleanExiHS_ATP5D.
GenevestigatoriP30049.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.