ATPIF1

ATP5IF1
Identifiers
Aliases	ATP5IF1 , ATPI, ATPIP, IP, ATPase inhibitory factor 1, ATP synthase inhibitory factor subunit 1, ATPIF1
External IDs	OMIM: 614981 MGI: 1196457 HomoloGene: 40581 GeneCards: ATP5IF1
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p35.3 Start 28,236,109 bp [1] End 28,246,906 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D2.3 Start 132,257,866 bp [2] End 132,260,970 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 9 prefrontal cortex superior frontal gyrus hypothalamus right uterine tube left ventricle nucleus accumbens amygdala duodenum anterior pituitary Top expressed in Paneth cell atrium external carotid artery proximal tubule internal carotid artery medial vestibular nucleus supraoptic nucleus atrioventricular valve endocardial cushion medullary collecting duct More reference expression data BioGPS More reference expression data
Gene ontology Molecular function 5-formyltetrahydrofolate cyclo-ligase activity enzyme inhibitor activity protein homodimerization activity ATPase binding calmodulin binding ATPase inhibitor activity angiostatin binding enzyme binding mitochondrial proton-transporting ATP synthase complex binding Cellular component mitochondrial proton-transporting ATP synthase complex cell surface mitochondrion Biological process regulation of ATP metabolic process positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway negative regulation of ATP-dependent activity tetrahydrofolate interconversion positive regulation of proteolysis involved in cellular protein catabolic process negative regulation of hydrolase activity generation of precursor metabolites and energy reactive oxygen species metabolic process negative regulation of endothelial cell proliferation heme biosynthetic process regulation of protein targeting to mitochondrion angiogenesis erythrocyte differentiation mitochondrial depolarization protein homooligomerization protein homotetramerization folic acid-containing compound biosynthetic process positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 93974 11983 Ensembl ENSG00000130770 ENSG00000285390 ENSMUSG00000054428 UniProt Q9UII2 O35143 RefSeq (mRNA) NM_178191 NM_016311 NM_178190 NM_007512 RefSeq (protein) NP_057395 NP_835497 NP_835498 NP_031538 Location (UCSC) Chr 1: 28.24 – 28.25 Mb Chr 4: 132.26 – 132.26 Mb PubMed search [3] [4]
Wikidata
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ATPase inhibitor, mitochondrial is an enzyme that in humans is encoded by the ATPIF1 gene. ^{[5] [6]}

This gene encodes a mitochondrial ATPase inhibitor. Alternative splicing occurs at this locus and three transcript variants encoding distinct isoforms have been identified. ^[6]

It prevents ATPase from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation ^[7] ATP synthase inhibitor forms a one-to-one complex with the F1 ATPase, possibly by binding at the alpha-beta interface. It is thought to inhibit ATP synthesis by preventing the release of ATP. ^[8] The inhibitor has two oligomeric states, dimer (the active state) and tetramer. At low pH, the inhibitor forms a dimer via antiparallel coiled coil interactions between the C-terminal regions of two monomers. At high pH, the inhibitor forms tetramers and higher oligomers by coiled coil interactions involving the N terminus and inhibitory region, thus preventing the inhibitory activity. ^[7]

Mitochondrial ATPase inhibitor, IATP
c-terminal coiled-coil domain from bovine if1
Identifiers
Symbol	IATP
Pfam	PF04568
InterPro	IPR007648
SCOP2	1hf9 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

References

1. ENSG00000285390 GRCh38: Ensembl release 89: ENSG00000130770, ENSG00000285390 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000054428 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ichikawa N, Ushida S, Kawabata M, Masazumi Y (Mar 2000). "Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans". Biosci Biotechnol Biochem. 63 (12): 2225–2227. doi: 10.1271/bbb.63.2225 . PMID   10664857.
6. "Entrez Gene: ATPIF1 ATPase inhibitory factor 1".
7. Cabezon E, Butler PJ, Runswick MJ, Carbajo RJ, Walker JE (November 2002). "Homologous and heterologous inhibitory effects of ATPase inhibitor proteins on F-ATPases". J. Biol. Chem. 277 (44): 41334–41. doi: 10.1074/jbc.M207169200 . PMID   12186878. S2CID   25160113.
8. van Raaij MJ, Orriss GL, Montgomery MG, Runswick MJ, Fearnley IM, Skehel JM, et al. (December 1996). "The ATPase inhibitor protein from bovine heart mitochondria: the minimal inhibitory sequence". Biochemistry. 35 (49): 15618–25. doi:10.1021/bi960628f. PMID   8961923.

External links

• Human ATPIF1 genome location and ATPIF1 gene details page in the UCSC Genome Browser .

Further reading

• 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): 6990–6996. doi:10.1093/emboj/20.24.6990. PMC   125800 . PMID   11742976.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, 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): 16899–16903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi: 10.1038/ng1285 . PMID   14702039.
• Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Burwick NR, Wahl ML, Fang J, Zhong Z, Moser TL, Li B, 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): 1740–1745. doi: 10.1074/jbc.M405947200 . PMC   1201548 . PMID   15528193.
• Andersen JS, Lam YW, Leung AK, Ong S, Lyon CE, Lamond AI, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• Cortés-Hernández P, Domínguez-Ramírez L, Estrada-Bernal A, Montes-Sánchez DG, Zentella-Dehesa A, De Gómez-Puyou MT, 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): 844–849. doi:10.1016/j.bbrc.2005.03.064. PMID   15809073.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual J, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–814. doi: 10.1016/j.cell.2006.03.032 . PMID   16713569. S2CID   13709685.
• Ma J, Dempsey AA, Stamatiou D, Marshall K, Liew C (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, Lippe G, Mavelli I (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. S2CID   85086145.

This article incorporates text from the public domain Pfam and InterPro: IPR007648