ATPase inhibitor, mitochondrial precursor - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot P01096 (ATIF1_BOVIN)

Last modified November 25, 2008. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
ATPase inhibitor, mitochondrial

Gene names

Name:	ATPIF1
Synonyms:	ATPI

Organism

Bos taurus (Bovine)

Taxonomic identifier

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	Thought to be a regulatory component of the ATP-synthesizing complex in the mitochondria.
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 Direct protein sequencing
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
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

25

Mitochondrion

Chain

84

ATPase inhibitor, mitochondrial

PRO_0000002546

Regions

Coiled coil

41

Experimental info

Sequence conflict

1

E → Q AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

109

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P01096-1 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 0F8816DECCAABA7E
Show »

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

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

PIR

IWBO. C27382.

RefSeq

UniGene

3D structure databases

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	[»]

ModBase

Genome annotation databases

Ensembl

ENSBTAG00000006342. Bos taurus. [Contig view]

GeneID

KEGG

Phylogenomic databases

HOVERGEN

Family and domain databases

InterPro

IPR007648. IATP.
[Graphical view]

Pfam

PF04568. IATP. 1 hit.
[Graphical view]

ProtoNet

Other Resources

LinkHub

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 25, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents