P01096 (ATIF1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATPase inhibitor, mitochondrial

Alternative name(s):
Inhibitor of F(1)F(o)-ATPase
Short name=IF(1)
Short name=IF1

Gene names

Name:	ATPIF1
Synonyms:	ATPI

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	109 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	Endogenous F1F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F1F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix.
Subunit structure	Homodimer at a pH value below 6.5, inactive homotetramer above.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the ATPase inhibitor family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Coiled coil Transit peptide
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of endothelial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of hydrolase activity Inferred from direct assay. Source: UniProtKB negative regulation of nucleotide metabolic process Inferred from electronic annotation. Source: InterPro protein homotetramerization Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay. Source: UniProtKB
Molecular function	ATPase binding Inferred from direct assay. Source: UniProtKB ATPase inhibitor activity Inferred from direct assay. Source: UniProtKB angiostatin binding Inferred from sequence or structural similarity. Source: UniProtKB calmodulin binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 25

25

Mitochondrion Ref.3

Chain

26 – 109

84

ATPase inhibitor, mitochondrial

PRO_0000002546

Regions

Coiled coil

69 – 109

41

Experimental info

Sequence conflict

55

1

E → Q AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

109

Helix Strand Turn

Details...

Helix

39 – 42

4

Helix

45 – 107

63

Sequences

	Sequence		Length	Mass (Da)
	P01096 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 0F8816DECCAABA7E	FASTA	109	12,301
	10 20 30 40 50 60 MAATALAART RQAVWSVWAM QGRGFGSESG DNVRSSAGAV RDAGGAFGKR EQAEEERYFR 70 80 90 100 ARAKEQLAAL KKHHENEISH HAKEIERLQK EIERHKQSIK KLKQSEDDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ATP synthase from bovine mitochondria: sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein." Walker J.E., Gay N.J., Powell S.J., Kostina M., Dyer M.R. Biochemistry 26:8613-8619(1987) [PubMed: 2894843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.
[3]	"Amino acid sequence of the protein inhibitor of mitochondrial adenosine triphosphatase." Frangione B., Rosenwasser E., Penefsky H.S., Pullman M.E. Proc. Natl. Acad. Sci. U.S.A. 78:7403-7407(1981) [PubMed: 6461003] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-109.
[4]	"Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase." Gordon-Smith D.J., Carbajo R.J., Yang J.C., Videler H., Runswick M.J., Walker J.E., Neuhaus D. J. Mol. Biol. 308:325-339(2001) [PubMed: 11327770] [Abstract] Cited for: STRUCTURE BY NMR OF 69-109.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22559 mRNA. Translation: AAA30396.1.
BC111645 mRNA. Translation: AAI11646.1.

IPI

IPI00715260.

PIR

IWBO. C27382.

RefSeq

NP_787010.1. NM_175816.2.

UniGene

Bt.59150.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GMJ	X-ray	2.20	A/B/C/D	26-109	[»]
1HF9	NMR	-	A/B	69-109	[»]
1OHH	X-ray	2.80	H	26-109	[»]
2V7Q	X-ray	2.10	J	26-85	[»]

ProteinModelPortal

P01096.

SMR

P01096. Positions 29-65, 69-109.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46311N.

STRING

P01096.

Proteomic databases

PRIDE

P01096.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000008319; ENSBTAP00000008319; ENSBTAG00000006342.

GeneID

327699.

KEGG

bta:327699.

Organism-specific databases

CTD

93974.

Phylogenomic databases

eggNOG

maNOG21148.

GeneTree

ENSGT00390000006264.

HOVERGEN

HBG061381.

InParanoid

P01096.

OMA

NEISHHA.

OrthoDB

EOG4X0MTZ.

PhylomeDB

P01096.

Family and domain databases

InterPro

IPR007648. ATPase_inhibitor_IATP_mt.
[Graphical view]

Pfam

PF04568. IATP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATIF1_BOVIN

Accession

Primary (citable) accession number: P01096
Secondary accession number(s): Q2M2T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1990
Last modified:	November 16, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program