Reviewed,
UniProtKB/Swiss-Prot P48201 (AT5G3_HUMAN)
Last modified
November 24, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
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Names and origin
| Protein names | Recommended name: ATP synthase lipid-binding protein, mitochondrial Alternative name(s): ATP synthase proteolipid P3 ATPase protein 9 ATPase subunit c | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 142 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 synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. |
| 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 has three main subunits: a, b and c. |
| Subcellular location | |
| Involvement in disease | This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). |
| Miscellaneous | There are three genes which encode the mitochondrial ATP synthase proteolipid and they specify precursors with different import sequences but identical mature proteins. |
| Sequence similarities | Belongs to the ATPase C chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen ion transport Ion transport Transport |
| Cellular component | CF(0) Membrane Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Domain | Transit peptide Transmembrane |
| Ligand | Lipid-binding |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial proton-transporting ATP synthase complex Ref.1Traceable author statement. Source: ProtInc proton-transporting ATP synthase complex, coupling factor F(o)Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 67 | 67 | Mitochondrion | ||||||
| Chain | 68 – 142 | 75 | ATP synthase lipid-binding protein, mitochondrial | PRO_0000002567 | |||||
Regions | |||||||||
| Transmembrane | 83 – 103 | 21 | Potential | ||||||
| Transmembrane | 118 – 138 | 21 | Potential | ||||||
Sites | |||||||||
| Site | 125 | 1 | Reversibly protonated during proton transport By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 93 | 1 | G → E: dbSNP rs1802622. | VAR_011922 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3)." Yan W.L., Lerner T.J., Haines J.L., Gusella J.F. Genomics 24:375-377(1994) [PubMed: 7698763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Subthalamic nucleus. |
| [3] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "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]. |
Cross-references
Sequence databases | |
|---|---|
| U09813 mRNA. Translation: AAA78807.1. AK311999 mRNA. Translation: BAG34937.1. AC096649 Genomic DNA. Translation: AAX88970.1. BC106881 mRNA. Translation: AAI06882.1. | |
| IPI | IPI00008727. |
| PIR | I38612. |
| RefSeq | NP_001002258.1. NP_001680.1. |
| UniGene | Hs.429 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P48201. 1 interaction. |
| STRING | P48201. |
Genome annotation databases | |
| Ensembl | ENST00000284727; ENSP00000284727; ENSG00000154518; Homo sapiens. [Genome view] ENST00000392541; ENSP00000376324; ENSG00000154518; Homo sapiens. [Genome view] ENST00000409194; ENSP00000387317; ENSG00000154518; Homo sapiens. [Genome view] |
| GeneID | 518. |
| KEGG | hsa:518. |
| UCSC | uc002ujz.2. human. |
Organism-specific databases | |
| CTD | 518. |
| GeneCards | GC02M175750. |
| H-InvDB | HIX0023960. |
| HGNC | HGNC:843. ATP5G3. |
| MIM | 602736. gene. |
| PharmGKB | PA25133. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | P48201. |
| HOVERGEN | P48201. |
| OMA | ETRTEEG |
| OrthoDB | EOG9WWV4F |
Gene expression databases | |
| ArrayExpress | P48201. |
| Bgee | P48201. |
| CleanEx | HS_ATP5G3. |
| Genevestigator | P48201. |
| GermOnline | ENSG00000154518. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view] |
| Gene3D | G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit. |
| Pfam | PF00137. ATP-synt_C. 1 hit. [Graphical view] |
| PRINTS | PR00124. ATPASEC. |
| PROSITE | PS00605. ATPASE_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 2151. |
| SOURCE | Search... |
Entry information
| Entry name | AT5G3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P48201 Secondary accession number(s): B2R4Z0, Q4ZFX7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

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