Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
21  structures 772  species 4  interactions 1025  sequences 18  architectures

Family: IATP (PF04568)

Summary: Mitochondrial ATPase inhibitor, IATP

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

ATPIF1 Edit Wikipedia article

ATPIF1
Identifiers
Aliases ATPIF1, ATPI, ATPIP, IP, ATPase inhibitory factor 1
External IDs MGI: 1196457 HomoloGene: 40581 GeneCards: ATPIF1
Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ATPIF1
Genomic location for ATPIF1
Band No data available Start 28,236,109 bp[1]
End 28,246,906 bp[1]
RNA expression pattern
PBB GE ATPIF1 218671 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
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 1: 132.53 – 132.53 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

Model organisms

Model organisms have been used in the study of ATPIF1 function. A conditional knockout mouse line, called Atpif1tm1a(EUCOMM)Wtsi[15][16] 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.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] Twenty three tests were carried out on mutant mice and three significant abnormalities were observed.[13] Homozygous mutant animals displayed hyperactivity and brain dysmorphology, while males also had decreased circulating alkaline phosphatase levels.[13]

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130770 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000054428 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  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. PMID 10664857. doi:10.1271/bbb.63.2225. 
  6. ^ a b "Entrez Gene: ATPIF1 ATPase inhibitory factor 1". 
  7. ^ 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. PMID 12186878. doi:10.1074/jbc.M207169200. 
  8. ^ 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. PMID 8961923. doi:10.1021/bi960628f. 
  9. ^ "Anxiety data for Atpif1". Wellcome Trust Sanger Institute. 
  10. ^ "Clinical chemistry data for Atpif1". Wellcome Trust Sanger Institute. 
  11. ^ "Salmonella infection data for Atpif1". Wellcome Trust Sanger Institute. 
  12. ^ "Citrobacter infection data for Atpif1". Wellcome Trust Sanger Institute. 
  13. ^ 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. 
  14. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  15. ^ "International Knockout Mouse Consortium". 
  16. ^ "Mouse Genome Informatics". 
  17. ^ 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. PMC 3572410Freely accessible. PMID 21677750. doi:10.1038/nature10163. 
  18. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. PMID 21677718. doi:10.1038/474262a. 
  19. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. PMID 17218247. doi:10.1016/j.cell.2006.12.018. 
  20. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol. 12 (6): 224. PMC 3218837Freely accessible. PMID 21722353. doi:10.1186/gb-2011-12-6-224. 

External links

Further reading


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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(7)
Full
(1025)
Representative proteomes UniProt
(1495)
NCBI
(1515)
Meta
(0)
RP15
(257)
RP35
(547)
RP55
(806)
RP75
(1015)
Jalview View  View  View  View  View  View  View  View   
HTML View  View               
PP/heatmap 1 View               

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(7)
Full
(1025)
Representative proteomes UniProt
(1495)
NCBI
(1515)
Meta
(0)
RP15
(257)
RP35
(547)
RP55
(806)
RP75
(1015)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(7)
Full
(1025)
Representative proteomes UniProt
(1495)
NCBI
(1515)
Meta
(0)
RP15
(257)
RP35
(547)
RP55
(806)
RP75
(1015)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: DOMO:DM04419;
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Kerrison ND
Number in seed: 7
Number in full: 1025
Average length of the domain: 85.30 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 71.88 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.9 22.9
Trusted cut-off 22.9 22.9
Noise cut-off 22.8 22.8
Model length: 98
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Interactions

There are 4 interactions for this family. More...

ATP-synt_ab ATP-synt_ab_C ATP-synt IATP

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 21 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 sequence.

Loading structure mapping...