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8  structures 226  species 0  interactions 329  sequences 5  architectures

Family: IATP (PF04568)

Summary: Mitochondrial ATPase inhibitor, IATP

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This is the Wikipedia entry entitled "ATPIF1". More...

ATPIF1 Edit Wikipedia article

ATPase inhibitory factor 1
Identifiers
Symbols ATPIF1; ATPI; ATPIP; IP
External IDs OMIM614981 MGI1196457 HomoloGene40581 GeneCards: ATPIF1 Gene
RNA expression pattern
PBB GE ATPIF1 218671 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 93974 11983
Ensembl ENSG00000130770 ENSMUSG00000054428
UniProt Q9UII2 O35143
RefSeq (mRNA) NM_016311 NM_007512
RefSeq (protein) NP_057395 NP_031538
Location (UCSC) Chr 1:
28.56 – 28.57 Mb
Chr 4:
132.53 – 132.53 Mb
PubMed search [1] [2]

ATPase inhibitor, mitochondrial is an enzyme that in humans is encoded by the ATPIF1 gene.[1][2]

This gene encodes a mitochondrial ATPase inhibitor. Alternative splicing occurs at this locus and three transcript variants encoding distinct isoforms have been identified.[2]

It prevents ATPase from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation [3] 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.[4] 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.[3]

Model organisms[edit]

Model organisms have been used in the study of ATPIF1 function. A conditional knockout mouse line, called Atpif1tm1a(EUCOMM)Wtsi[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty three tests were carried out on mutant mice and three significant abnormalities were observed.[9] Homozygous mutant animals displayed hyperactivity and brain dysmorphology, while males also had decreased circulating alkaline phosphatase levels.[9]

Mitochondrial ATPase inhibitor, IATP
PDB 1hf9 EBI.jpg
c-terminal coiled-coil domain from bovine if1
Identifiers
Symbol IATP
Pfam PF04568
InterPro IPR007648
SCOP 1hf9
SUPERFAMILY 1hf9

References[edit]

  1. ^ 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. 
  2. ^ a b "Entrez Gene: ATPIF1 ATPase inhibitory factor 1". 
  3. ^ a b 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. 
  4. ^ van Raaij MJ, Orriss GL, Montgomery MG, Runswick MJ, Fearnley IM, Skehel JM, Walker JE (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. 
  5. ^ "Anxiety data for Atpif1". Wellcome Trust Sanger Institute. 
  6. ^ "Clinical chemistry data for Atpif1". Wellcome Trust Sanger Institute. 
  7. ^ "Salmonella infection data for Atpif1". Wellcome Trust Sanger Institute. 
  8. ^ "Citrobacter infection data for Atpif1". Wellcome Trust Sanger Institute. 
  9. ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  10. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  11. ^ "International Knockout Mouse Consortium". 
  12. ^ "Mouse Genome Informatics". 
  13. ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.  edit
  14. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  15. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  16. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 

Further reading[edit]



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

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Mitochondrial ATPase inhibitor, IATP Provide feedback

ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation [1] 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 [2]. The minimum inhibitory region for bovine inhibitor (P01096) is from residues 39 to 72 [2]. 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 [1].

Literature references

  1. Cabezon E, Butler PJ, Runswick MJ, Carbajo RJ, Walker JE; , J Biol Chem 2002;277:41334-41341.: Homologous and heterologous inhibitory effects of ATPase inhibitor proteins on F-ATPases. PUBMED:12186878 EPMC:12186878

  2. van Raaij MJ, Orriss GL, Montgomery MG, Runswick MJ, Fearnley IM, Skehel JM, Walker JE; , Biochemistry 1996;35:15618-15625.: The ATPase inhibitor protein from bovine heart mitochondria: the minimal inhibitory sequence. PUBMED:8961923 EPMC:8961923


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007648

ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation [PUBMED:12186878] 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 [PUBMED:8961923]. The minimum inhibitory region for bovine inhibitor (SWISSPROT) is from residues 39 to 72 [PUBMED:8961923]. 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 [PUBMED:12186878].

Gene Ontology

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Domain organisation

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Full
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Representative proteomes NCBI
(316)
Meta
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RP15
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RP35
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RP55
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RP75
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  Seed
(34)
Full
(329)
Representative proteomes NCBI
(316)
Meta
(0)
RP15
(69)
RP35
(114)
RP55
(179)
RP75
(221)
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Seed source: DOMO:DM04419;
Previous IDs: none
Type: Family
Author: Kerrison ND
Number in seed: 34
Number in full: 329
Average length of the domain: 83.00 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 76.51 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.7 21.6
Noise cut-off 21.5 21.5
Model length: 100
Family (HMM) version: 7
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Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IATP domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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