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Entry version 200 (18 Sep 2019)
Sequence version 1 (01 Oct 1993)
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Protein

ATP synthase subunit alpha, mitochondrial

Gene

Atp5f1a

Organism
Mus musculus (Mouse)
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 (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).By similarity

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_section">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 – 220ATPBy similarity8
Nucleotide bindingi473 – 475ATPBy similarity3

<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

GO - Biological processi

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

<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_and_taxonomy_section">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_and_taxonomy_section">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome 18

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88115 Atp5a1

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 – 43MitochondrionBy similarityAdd BLAST43
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000242544 – 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 residuei53PhosphoserineCombined sources1
Modified residuei65PhosphoserineBy similarity1
Modified residuei76Phosphoserine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 residuei106PhosphoserineCombined sources1
Modified residuei123N6-acetyllysineCombined sources1
Modified residuei126N6-acetyllysineCombined sources1
Modified residuei132N6-acetyllysineCombined sources1
Modified residuei134PhosphothreonineBy similarity1
Modified residuei161N6-acetyllysine; alternateCombined sources1
Modified residuei161N6-succinyllysine; alternateCombined sources1
Modified residuei166PhosphoserineBy similarity1
Modified residuei167N6-acetyllysine; alternateCombined sources1
Modified residuei167N6-succinyllysine; alternateCombined sources1
Modified residuei184PhosphoserineBy similarity1
Modified residuei204Omega-N-methylarginineCombined sources1
Modified residuei230N6-acetyllysine; alternateCombined sources1
Modified residuei230N6-succinyllysine; alternateCombined sources1
Modified residuei239N6-acetyllysine; alternateCombined sources1
Modified residuei239N6-succinyllysine; alternateCombined sources1
Modified residuei240N6-acetyllysineCombined sources1
Modified residuei261N6-acetyllysine; alternateCombined sources1
Modified residuei261N6-succinyllysine; alternateCombined sources1
Modified residuei305N6-acetyllysine; alternateCombined sources1
Modified residuei305N6-succinyllysine; alternateCombined sources1
Modified residuei427N6-acetyllysine; alternateCombined sources1
Modified residuei427N6-succinyllysine; alternateCombined sources1
Modified residuei434N6-acetyllysineCombined sources1
Modified residuei498N6-acetyllysine; alternateCombined sources1
Modified residuei498N6-succinyllysine; alternateCombined sources1
Modified residuei506N6-acetyllysine; alternateCombined sources1
Modified residuei506N6-succinyllysine; alternateCombined sources1
Modified residuei521PhosphoserineCombined sources1
Modified residuei531N6-acetyllysine; alternateCombined sources1
Modified residuei531N6-succinyllysine; alternateCombined sources1
Modified residuei539N6-acetyllysine; alternateCombined sources1
Modified residuei539N6-succinyllysine; alternateCombined sources1
Modified residuei541N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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). Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3765

Encyclopedia of Proteome Dynamics

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EPDi
Q03265

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q03265

MaxQB - The MaxQuant DataBase

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MaxQBi
Q03265

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

More...
PaxDbi
Q03265

PeptideAtlas

More...
PeptideAtlasi
Q03265

PRoteomics IDEntifications database

More...
PRIDEi
Q03265

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00130280
Q03265

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
Q03265

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
Q03265

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q03265

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q03265

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q03265

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q03265

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000025428 Expressed in 327 organ(s), highest expression level in brown adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q03265 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q03265 MM

<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_section">'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_section">'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. CF0 has three main subunits: a, b and c (By similarity).

Interacts with ATPAF2.

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

Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (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, ATP5MD and ATP5MPL (By similarity).

Interacts with BLOC1S1 (By similarity).

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 (By similarity).

Interacts with CLN5 and PPT1 (PubMed:19941651).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
198253, 27 interactors

Protein interaction database and analysis system

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IntActi
Q03265, 36 interactors

Molecular INTeraction database

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MINTi
Q03265

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000026495

<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

3D structure databases

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

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SMRi
Q03265

Database of comparative protein structure models

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ModBasei
Search...

<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

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eggNOGi
KOG1353 Eukaryota
COG0056 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074846

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03265

KEGG Orthology (KO)

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KOi
K02132

Database of Orthologous Groups

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OrthoDBi
470054at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q03265

TreeFam database of animal gene trees

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TreeFami
TF300321

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01132 F1_ATPase_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.150.20, 1 hit
2.40.30.20, 1 hit

HAMAP database of protein families

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HAMAPi
MF_01346 ATP_synth_alpha_bact, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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SUPFAMi
SSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q03265-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE
60 70 80 90 100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV
160 170 180 190 200
VDALGNAIDG KGPIGSKTRR 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
RAAKMNDSFG 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 SLLGNIRSDG KISEQSDAKL KEIVTNFLAG

FEP
Length:553
Mass (Da):59,753
Last modified:October 1, 1993 - 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:iCF35B4FBA7ED431D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z6F5D3Z6F5_MOUSE
ATP synthase subunit alpha
Atp5a1 mCG_18273
503Annotation score:

Annotation score:2 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>
D6RJ16D6RJ16_MOUSE
ATP synthase, H+-transporting, mito...
Atp5a1
89Annotation score:

Annotation score:1 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 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 conflicti3S → T in BAE37632 (PubMed:16141072).Curated1
Sequence conflicti63D → Y in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti119F → L in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti126K → N in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti315S → Y in BAE34114 (PubMed:16141072).Curated1
Sequence conflicti321Y → C in BAE40868 (PubMed:16141072).Curated1
Sequence conflicti422 – 456Missing in BAE27439 (PubMed:16141072).CuratedAdd BLAST35
Sequence conflicti486A → T in BAE40158 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L01062 mRNA Translation: AAA37271.1
AK043976 mRNA Translation: BAC31722.1
AK076572 mRNA Translation: BAC36399.1
AK146797 mRNA Translation: BAE27439.1
AK150426 mRNA Translation: BAE29549.1
AK150843 mRNA Translation: BAE29901.1
AK151004 mRNA Translation: BAE30027.1
AK151128 mRNA Translation: BAE30136.1
AK151224 mRNA Translation: BAE30216.1
AK151920 mRNA Translation: BAE30798.1
AK152054 mRNA Translation: BAE30910.1
AK152890 mRNA Translation: BAE31573.1
AK157529 mRNA Translation: BAE34114.1
AK159540 mRNA Translation: BAE35167.1
AK159491 mRNA Translation: BAE35125.1
AK159758 mRNA Translation: BAE35349.1
AK160043 mRNA Translation: BAE35585.1
AK164110 mRNA Translation: BAE37632.1
AK164193 mRNA Translation: BAE37675.1
AK166709 mRNA Translation: BAE38962.1
AK166812 mRNA Translation: BAE39039.1
AK167159 mRNA Translation: BAE39300.1
AK167863 mRNA Translation: BAE39881.1
AK168198 mRNA Translation: BAE40158.1
AK168617 mRNA Translation: BAE40482.1
AK168879 mRNA Translation: BAE40697.1
AK168890 mRNA Translation: BAE40707.1
AK168932 mRNA Translation: BAE40744.1
AK169080 mRNA Translation: BAE40864.1
AK169084 mRNA Translation: BAE40868.1
AK169105 mRNA Translation: BAE40887.1
AK169142 mRNA Translation: BAE40921.1
AK169300 mRNA Translation: BAE41056.1
AK169308 mRNA Translation: BAE41063.1
AK169414 mRNA Translation: BAE41160.1
BC014854 mRNA Translation: AAH14854.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS29358.1

Protein sequence database of the Protein Information Resource

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PIRi
JC1473

NCBI Reference Sequences

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RefSeqi
NP_031531.1, NM_007505.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428
ENSMUST00000231086; ENSMUSP00000154864; ENSMUSG00000116276

Database of genes from NCBI RefSeq genomes

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GeneIDi
11946

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:11946

UCSC genome browser

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UCSCi
uc008fru.1 mouse

<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
L01062 mRNA Translation: AAA37271.1
AK043976 mRNA Translation: BAC31722.1
AK076572 mRNA Translation: BAC36399.1
AK146797 mRNA Translation: BAE27439.1
AK150426 mRNA Translation: BAE29549.1
AK150843 mRNA Translation: BAE29901.1
AK151004 mRNA Translation: BAE30027.1
AK151128 mRNA Translation: BAE30136.1
AK151224 mRNA Translation: BAE30216.1
AK151920 mRNA Translation: BAE30798.1
AK152054 mRNA Translation: BAE30910.1
AK152890 mRNA Translation: BAE31573.1
AK157529 mRNA Translation: BAE34114.1
AK159540 mRNA Translation: BAE35167.1
AK159491 mRNA Translation: BAE35125.1
AK159758 mRNA Translation: BAE35349.1
AK160043 mRNA Translation: BAE35585.1
AK164110 mRNA Translation: BAE37632.1
AK164193 mRNA Translation: BAE37675.1
AK166709 mRNA Translation: BAE38962.1
AK166812 mRNA Translation: BAE39039.1
AK167159 mRNA Translation: BAE39300.1
AK167863 mRNA Translation: BAE39881.1
AK168198 mRNA Translation: BAE40158.1
AK168617 mRNA Translation: BAE40482.1
AK168879 mRNA Translation: BAE40697.1
AK168890 mRNA Translation: BAE40707.1
AK168932 mRNA Translation: BAE40744.1
AK169080 mRNA Translation: BAE40864.1
AK169084 mRNA Translation: BAE40868.1
AK169105 mRNA Translation: BAE40887.1
AK169142 mRNA Translation: BAE40921.1
AK169300 mRNA Translation: BAE41056.1
AK169308 mRNA Translation: BAE41063.1
AK169414 mRNA Translation: BAE41160.1
BC014854 mRNA Translation: AAH14854.1
CCDSiCCDS29358.1
PIRiJC1473
RefSeqiNP_031531.1, NM_007505.2

3D structure databases

SMRiQ03265
ModBaseiSearch...

Protein-protein interaction databases

BioGridi198253, 27 interactors
IntActiQ03265, 36 interactors
MINTiQ03265
STRINGi10090.ENSMUSP00000026495

PTM databases

CarbonylDBiQ03265
iPTMnetiQ03265
PhosphoSitePlusiQ03265
SwissPalmiQ03265

2D gel databases

REPRODUCTION-2DPAGEiIPI00130280
Q03265
SWISS-2DPAGEiQ03265
UCD-2DPAGEiQ03265

Proteomic databases

CPTACinon-CPTAC-3765
EPDiQ03265
jPOSTiQ03265
MaxQBiQ03265
PaxDbiQ03265
PeptideAtlasiQ03265
PRIDEiQ03265

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428
ENSMUST00000231086; ENSMUSP00000154864; ENSMUSG00000116276
GeneIDi11946
KEGGimmu:11946
UCSCiuc008fru.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11946
MGIiMGI:88115 Atp5a1

Phylogenomic databases

eggNOGiKOG1353 Eukaryota
COG0056 LUCA
GeneTreeiENSGT00550000074846
InParanoidiQ03265
KOiK02132
OrthoDBi470054at2759
PhylomeDBiQ03265
TreeFamiTF300321

Enzyme and pathway databases

ReactomeiR-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Atp5a1 mouse

Protein Ontology

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PROi
PR:Q03265

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000025428 Expressed in 327 organ(s), highest expression level in brown adipose tissue
ExpressionAtlasiQ03265 baseline and differential
GenevisibleiQ03265 MM

Family and domain databases

CDDicd01132 F1_ATPase_alpha, 1 hit
Gene3Di1.20.150.20, 1 hit
2.40.30.20, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_MOUSE
<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: Q03265
Secondary accession number(s): Q3TFN0
, Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 18, 2019
This is version 200 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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