ATPIF1

From Wikipedia, the free encyclopedia

ATPase inhibitory factor 1

Identifiers

ATPIF1; IP; ATPI; ATPIP; MGC1167; MGC8898

External IDs

MGI: 1196457 HomoloGene: 40581

Gene ontology
Molecular Function:	• enzyme inhibitor activity • calmodulin binding • ATPase inhibitor activity • protein homodimerization activity • angiostatin binding • ATPase binding
Cellular Component:	• mitochondrion • cell surface
Biological Process:	• angiogenesis • negative regulation of endothelial cell proliferation • generation of precursor metabolites and energy • response to pH • negative regulation of nucleotide metabolic process • protein homotetramerization • negative regulation of hydrolase activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_016311 (mRNA)
NP_057395 (protein)

NM_007512 (mRNA)
NP_031538 (protein)

Location

Chr 1: 28.44 - 28.44 Mb

Chr 4: 131.8 - 131.81 Mb

Pubmed search

[1]

[2]

ATPase inhibitory factor 1, also known as ATPIF1, is a human gene.^[1]

This gene encodes a mitochondrial ATPase inhibitor. Alternative splicing occurs at this locus and three transcript variants encoding distinct isoforms have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATPIF1 ATPase inhibitory factor 1.

[edit] Further reading

Ichikawa N, Ushida S, Kawabata M, Masazumi Y (2000). "Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans.". Biosci. Biotechnol. Biochem. 63 (12): 2225–7. PMID 10664857.
Cabezón E, Runswick MJ, Leslie AG, Walker JE (2002). "The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase.". EMBO J. 20 (24): 6990–6. doi:10.1093/emboj/20.24.6990. PMID 11742976.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Burwick NR, Wahl ML, Fang J, et al. (2005). "An Inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface.". J. Biol. Chem. 280 (3): 1740–5. doi:10.1074/jbc.M405947200. PMID 15528193.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
Cortés-Hernández P, Domínguez-Ramírez L, Estrada-Bernal A, et al. (2005). "The inhibitor protein of the F1F0-ATP synthase is associated to the external surface of endothelial cells.". Biochem. Biophys. Res. Commun. 330 (3): 844–9. doi:10.1016/j.bbrc.2005.03.064. PMID 15809073.
Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
Ma J, Dempsey AA, Stamatiou D, et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects.". Atherosclerosis 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
Contessi S, Comelli M, Cmet S, et al. (2008). "IF(1) distribution in HepG2 cells in relation to ecto-F(0)F (1)ATPsynthase and calmodulin.". J. Bioenerg. Biomembr. 39 (4): 291–300. doi:10.1007/s10863-007-9091-0. PMID 17851741.