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UniProtKB - P19483 (ATPA_BOVIN)

Entry version 194 (23 Feb 2022)
Sequence version 1 (01 Feb 1991)
Previous versions | rss
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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5F1A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).

By similarity2 Publications

Miscellaneous

The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe3+ and helps bacteria scavenge iron ions from the environment. As a consequence, the mammalian siderocalin LCN2 plays an important role in defense against bacterial infections by sequestering iron bound to microbial siderophores. LCN2 can also bind iron bound to endogenous or nutrient-derived iron chelators and plays an important role in cellular iron homeostasis. Enterobactin produced by non-pathogenic E.coli strains can facilitate mitochondrial iron assimilation, suggesting that iron bound to siderophores from non-pathogenic bacteria may contribute to iron absorption by the host.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei413Required for activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi213 – 220ATPCombined sources4 Publications8
Nucleotide bindingi473 – 475ATPCombined sources4 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		7.1.2.2, 908

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrialCurated
Alternative name(s):
ATP synthase F1 subunit alphaBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATP5F1ABy similarity
Synonyms:ATP5A1, ATP5A2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 43Mitochondrion1 PublicationAdd BLAST43
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000242344 – 553ATP synthase subunit alpha, mitochondrialAdd BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei44Pyrrolidone carboxylic acid1 Publication1
Modified residuei53PhosphoserineBy similarity1
Modified residuei65PhosphoserineBy similarity1
Modified residuei76Phosphoserine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi76O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei123N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei134PhosphothreonineBy similarity1
Modified residuei161N6-acetyllysine; alternateBy similarity1
Modified residuei161N6-succinyllysine; alternateBy similarity1
Modified residuei166PhosphoserineBy similarity1
Modified residuei167N6-acetyllysine; alternateBy similarity1
Modified residuei167N6-succinyllysine; alternateBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei204Omega-N-methylarginineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysine; alternateBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-acetyllysineBy similarity1
Modified residuei261N6-acetyllysine; alternateBy similarity1
Modified residuei261N6-succinyllysine; alternateBy similarity1
Modified residuei305N6-acetyllysine; alternateBy similarity1
Modified residuei305N6-succinyllysine; alternateBy similarity1
Modified residuei427N6-acetyllysine; alternateBy similarity1
Modified residuei427N6-succinyllysine; alternateBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei498N6-acetyllysine; alternateBy similarity1
Modified residuei498N6-succinyllysine; alternateBy similarity1
Modified residuei506N6-acetyllysine; alternateBy similarity1
Modified residuei506N6-succinyllysine; alternateBy similarity1
Modified residuei531N6-acetyllysine; alternateBy similarity1
Modified residuei531N6-succinyllysine; alternateBy similarity1
Modified residuei539N6-acetyllysine; alternateBy similarity1
Modified residuei539N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated on lysine residues. BLOC1S1 is required for acetylation.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P19483

PeptideAtlas

More...PeptideAtlasi		P19483

PRoteomics IDEntifications database

More...PRIDEi		P19483

2D gel databases

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P19483

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Heart muscle (at protein level) (PubMed:2864455). Heart and liver.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1 (PubMed:2864455, PubMed:17570365, PubMed:23407638). CF0 has three main subunits: a, b and c (PubMed:2864455, PubMed:17570365, PubMed:23407638).

Interacts with ATPAF2 (By similarity).

Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (By similarity).

Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:2864455, PubMed:17570365, PubMed:23407638, PubMed:25851905).

Interacts with BLOC1S1.

Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency.

Interacts with CLN5 and PPT1 (By similarity).

Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity).

Interacts with ABCB7; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity).

By similarity6 Publications

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P19483

Database of interacting proteins

More...DIPi		DIP-35479N

Protein interaction database and analysis system

More...IntActi		P19483, 9 interactors

Molecular INTeraction database

More...MINTi		P19483

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000003259

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P19483

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P19483

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P19483

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1353, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P19483

Database of Orthologous Groups

More...OrthoDBi		470054at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd18113, ATP-synt_F1_alpha_C, 1 hit
cd01132, F1_ATPase_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.150.20, 1 hit
2.40.30.20, 1 hit
3.40.50.300, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01346, ATP_synth_alpha_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023366, ATP_synth_asu-like_sf
IPR000793, ATP_synth_asu_C
IPR038376, ATP_synth_asu_C_sf
IPR033732, ATP_synth_F1_a
IPR005294, ATP_synth_F1_asu
IPR020003, ATPase_a/bsu_AS
IPR004100, ATPase_F1/V1/A1_a/bsu_N
IPR036121, ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194, ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR027417, P-loop_NTPase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00006, ATP-synt_ab, 1 hit
PF00306, ATP-synt_ab_C, 1 hit
PF02874, ATP-synt_ab_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF039088, F_ATPase_subunit_alpha, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50615, SSF50615, 1 hit
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00962, atpA, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00152, ATPASE_ALPHA_BETA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P19483-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE 
        60         70         80         90        100
VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 
       110        120        130        140        150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV 
       160        170        180        190        200
VDALGNAIDG KGPIGSKARR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 
       210        220        230        240        250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 
       260        270        280        290        300
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 
       310        320        330        340        350
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 
       360        370        380        390        400
RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 
       410        420        430        440        450
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 
       460        470        480        490        500
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 
       510        520        530        540        550
PSKITKFENA FLSHVISQHQ ALLSKIRTDG KISEESDAKL KEIVTNFLAG 

FEA
Length:553
Mass (Da):59,720
Last modified:February 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i188E9531B3B815E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4V → M in AAI16060 (Ref. 3) Curated1
Sequence conflicti6V → I in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti31 – 33IAA → VGT in AAA30399 (PubMed:2896000).Curated3
Sequence conflicti41S → T in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti51V → M in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti144E → D in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti164I → V in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti168A → I in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti358A → S in AAA30399 (PubMed:2896000).Curated1
Sequence conflicti524S → G in AAI16060 (Ref. 3) Curated1
Sequence conflicti524S → G AA sequence (PubMed:2864455).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M22465 mRNA Translation: AAB59266.1
X64565 Genomic DNA Translation: CAA45865.1
BC116059 mRNA Translation: AAI16060.1
M19680 mRNA Translation: AAA30399.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27693
S27201, PWBOA

NCBI Reference Sequences

More...RefSeqi		NP_777109.1, NM_174684.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		282578

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:282578

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22465 mRNA Translation: AAB59266.1
X64565 Genomic DNA Translation: CAA45865.1
BC116059 mRNA Translation: AAI16060.1
M19680 mRNA Translation: AAA30399.1
PIRiA27693
S27201, PWBOA
RefSeqiNP_777109.1, NM_174684.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BMFX-ray2.85A/B/C44-553[»]
1COWX-ray3.10A/B/C45-553[»]
1E1QX-ray2.61A/B/C44-553[»]
1E1RX-ray2.50A/B/C44-553[»]
1E79X-ray2.40A/B/C44-553[»]
1EFRX-ray3.10A/B/C45-553[»]
1H8EX-ray2.00A/B/C44-553[»]
1H8HX-ray2.90A/B/C44-553[»]
1NBMX-ray3.00A/B/C44-553[»]
1OHHX-ray2.80A/B/C44-553[»]
1QO1X-ray3.90A/B/C44-553[»]
1W0JX-ray2.20A/B/C44-553[»]
1W0KX-ray2.85A/B/C44-553[»]
2CK3X-ray1.90A/B/C44-553[»]
2JDIX-ray1.90A/B/C44-553[»]
2JIZX-ray2.30A/B/C/H/I/J44-553[»]
2JJ1X-ray2.70A/B/C/H/I/J44-553[»]
2JJ2X-ray2.40A/B/C/H/I/J44-553[»]
2JMXNMR-B44-68[»]
2V7QX-ray2.10A/B/C45-553[»]
2W6EX-ray6.50A/B/C1-553[»]
2W6FX-ray6.00A/B/C1-553[»]
2W6GX-ray6.00A/B/C1-553[»]
2W6HX-ray5.00A/B/C1-553[»]
2W6IX-ray4.00A/B/C1-553[»]
2W6JX-ray3.84A/B/C1-553[»]
2WSSX-ray3.20A/B/C/J/K/L44-553[»]
2XNDX-ray3.50A/B/C62-553[»]
4ASUX-ray2.60A/B/C44-553[»]
4TSFX-ray3.20A/B/C44-553[»]
4TT3X-ray3.21A/B/C44-553[»]
4YXWX-ray3.10A/B/C44-553[»]
4Z1MX-ray3.30A/B/C44-553[»]
5ARAelectron microscopy6.70A/B/C44-553[»]
5AREelectron microscopy7.40A/B/C44-553[»]
5ARHelectron microscopy7.20A/B/C44-553[»]
5ARIelectron microscopy7.40A/B/C44-553[»]
5FIJelectron microscopy7.40A/B/C44-553[»]
5FIKelectron microscopy6.40A/B/C44-553[»]
5FILelectron microscopy7.10A/B/C44-553[»]
6YY0electron microscopy3.23A/B/C44-553[»]
6Z1Relectron microscopy3.29A/B/C44-553[»]
6Z1Uelectron microscopy3.47A/B/C44-553[»]
6ZIQelectron microscopy4.33C44-553[»]
6ZITelectron microscopy3.49C44-553[»]
6ZIUelectron microscopy6.02C44-553[»]
6ZPOelectron microscopy4.00A/B/C44-553[»]
6ZQMelectron microscopy3.29A/B/C44-553[»]
6ZQNelectron microscopy4.00A/B/C44-553[»]
7AJBelectron microscopy9.20A/AA/AB/AC/B/C44-553[»]
7AJCelectron microscopy11.90A/AA/AB/AC/B/C44-553[»]
7AJDelectron microscopy9.00A/AA/AB/AC/B/C44-553[»]
7AJEelectron microscopy9.40A/AA/AB/AC/B/C44-553[»]
7AJFelectron microscopy8.45A/AA/AB/AC/B/C44-553[»]
7AJGelectron microscopy10.70A/AA/AB/AC/B/C44-553[»]
7AJHelectron microscopy9.70A/AA/AB/AC/B/C44-553[»]
7AJIelectron microscopy11.40A/AA/AB/AC/B/C44-553[»]
7AJJelectron microscopy13.10A/AA/AB/AC/B/C44-553[»]
BMRBiP19483
SMRiP19483
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

CORUMiP19483
DIPiDIP-35479N
IntActiP19483, 9 interactors
MINTiP19483
STRINGi9913.ENSBTAP00000003259

2D gel databases

UCD-2DPAGEiP19483

Proteomic databases

PaxDbiP19483
PeptideAtlasiP19483
PRIDEiP19483

Genome annotation databases

GeneIDi282578
KEGGibta:282578

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		498

Phylogenomic databases

eggNOGiKOG1353, Eukaryota
InParanoidiP19483
OrthoDBi470054at2759

Enzyme and pathway databases

BRENDAi7.1.2.2, 908

Miscellaneous databases

EvolutionaryTraceiP19483

Family and domain databases

CDDicd18113, ATP-synt_F1_alpha_C, 1 hit
cd01132, F1_ATPase_alpha, 1 hit
Gene3Di1.20.150.20, 1 hit
2.40.30.20, 1 hit
3.40.50.300, 1 hit
HAMAPiMF_01346, ATP_synth_alpha_bact, 1 hit
InterProiView protein in InterPro
IPR023366, ATP_synth_asu-like_sf
IPR000793, ATP_synth_asu_C
IPR038376, ATP_synth_asu_C_sf
IPR033732, ATP_synth_F1_a
IPR005294, ATP_synth_F1_asu
IPR020003, ATPase_a/bsu_AS
IPR004100, ATPase_F1/V1/A1_a/bsu_N
IPR036121, ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194, ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR027417, P-loop_NTPase
PfamiView protein in Pfam
PF00006, ATP-synt_ab, 1 hit
PF00306, ATP-synt_ab_C, 1 hit
PF02874, ATP-synt_ab_N, 1 hit
PIRSFiPIRSF039088, F_ATPase_subunit_alpha, 1 hit
SUPFAMiSSF50615, SSF50615, 1 hit
SSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00962, atpA, 1 hit
PROSITEiView protein in PROSITE
PS00152, ATPASE_ALPHA_BETA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiATPA_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19483
Secondary accession number(s): P05629, P19482, Q1JQC4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 23, 2022
This is version 194 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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