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Entry version 182 (07 Oct 2020)
Sequence version 1 (01 May 1999)
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Protein

Apoptosis-inducing factor 1, mitochondrial

Gene

Aifm1

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

Functions both as NADH oxidoreductase and as regulator of apoptosis (By similarity). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:9989411). Binds to DNA in a sequence-independent manner. Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (By similarity). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:19447115).By similarity2 Publications
Has NADH oxidoreductase activity. Does not induce nuclear apoptosis.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 48 min(-1) for dichlorophenolindophenol and 34 min(-1) for cytochrome c.1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei171FADCombined sources2 Publications1
      Binding sitei176FADCombined sources2 Publications1
      Binding sitei195NAD 2By similarity1
      Binding sitei232FAD; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
      Binding sitei284FADCombined sources2 Publications1
      Binding sitei335NAD 1Combined sources1 Publication1
      Binding sitei341NAD 1Combined sources1 Publication1
      Binding sitei398NAD 1; via amide nitrogenCombined sources1 Publication1
      Binding sitei437FADCombined sources1 Publication1
      Binding sitei482FAD; via carbonyl oxygenCombined sources2 Publications1
      Binding sitei482NAD 1; via carbonyl oxygenCombined sources1 Publication1
      Binding sitei492NAD 2By similarity1
      Binding sitei582NAD 2By 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 bindingi137 – 141FADCombined sources2 Publications5
      Nucleotide bindingi163 – 164FADCombined sources2 Publications2
      Nucleotide bindingi307 – 310NAD 1Combined sources1 Publication4
      Nucleotide bindingi452 – 453NAD 1Combined sources1 Publication2
      Nucleotide bindingi453 – 454FADCombined sources2 Publications2

      <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

      Molecular functionDNA-binding, Oxidoreductase
      Biological processApoptosis
      LigandFAD, Flavoprotein, NAD

      Enzyme and pathway databases

      SABIO-RK: Biochemical Reaction Kinetics Database

      More...
      SABIO-RKi
      Q9Z0X1

      <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:
      Apoptosis-inducing factor 1, mitochondrialCurated (EC:1.6.99.-1 Publication)
      Alternative name(s):
      Programmed cell death protein 8
      <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:Aifm1Imported
      Synonyms:Aif, Pdcd8
      <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>OrganismiMus musculus (Mouse)
      <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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
      <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
      • UP000000589 <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: Chromosome X

      Organism-specific databases

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

      More...
      MGIi
      MGI:1349419, Aifm1

      <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

      Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi176K → A: Increases catalytic efficiency. 1 Publication1
      Mutagenesisi195W → A: Increases redox potential, reacts faster to NADH and forms two-fold longer-lived CTC. 1 Publication1
      Mutagenesisi313E → A: Increases catalytic efficiency 30-fold. Increases affinity for NADH 20-fold. 1 Publication1

      <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 – 54MitochondrionBy similarityAdd BLAST54
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000040193655 – 101Removed in mature form1 PublicationAdd BLAST47
      <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_0000022031102 – 612Apoptosis-inducing factor 1, mitochondrialAdd BLAST511

      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 residuei108N6-succinyllysineCombined sources1
      Modified residuei115PhosphoserineBy similarity1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
      Modified residuei267PhosphoserineBy similarity1
      Modified residuei370PhosphoserineBy similarity1
      Modified residuei387N6-acetyllysineCombined sources1
      Modified residuei520PhosphothreonineBy similarity1
      Modified residuei523PhosphoserineBy similarity1
      Modified residuei529PhosphoserineBy similarity1
      Modified residuei592N6-acetyllysineCombined sources1

      <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

      Under normal conditions, a 54-residue N-terminal segment is first proteolytically removed during or just after translocation into the mitochondrial intermembrane space (IMS) by the mitochondrial processing peptidase (MPP) to form the inner-membrane-anchored mature form (AIFmit). During apoptosis, it is further proteolytically processed at amino-acid position 101 leading to the generation of the mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis in a caspase-independent manner.By similarity
      Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. Ubiquitination at Lys-254 by XIAP/BIRC4 blocks its ability to bind DNA and induce chromatin degradation, thereby inhibiting its ability to induce cell death.By similarity

      Keywords - PTMi

      Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      Q9Z0X1

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      Q9Z0X1

      MaxQB - The MaxQuant DataBase

      More...
      MaxQBi
      Q9Z0X1

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

      More...
      PaxDbi
      Q9Z0X1

      PeptideAtlas

      More...
      PeptideAtlasi
      Q9Z0X1

      PRoteomics IDEntifications database

      More...
      PRIDEi
      Q9Z0X1

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      Q9Z0X1

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

      More...
      PhosphoSitePlusi
      Q9Z0X1

      SwissPalm database of S-palmitoylation events

      More...
      SwissPalmi
      Q9Z0X1

      <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

      Expressed in liver (at protein level).1 Publication

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSMUSG00000036932, Expressed in cortex of kidney and 301 other tissues

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      Q9Z0X1, baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      Q9Z0X1, 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%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

      Monomer (oxidized form). Homodimer (reduced form). Upon reduction with NADH, undergoes dimerization and forms tight, long-lived FADH2-NAD charge transfer complexes (CTC) resistant to oxidation (PubMed:19447115). Also dimerizes with isoform 3 preventing its release from mitochondria.

      Interacts with XIAP/BIRC4.

      Interacts (via N-terminus) with EIF3G (via C-terminus).

      Interacts with PRELID1.

      Interacts with CHCHD4; the interaction increases in presence of NADH (By similarity).

      By similarity1 Publication

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Hide details

      GO - Molecular functioni

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGRID)

      More...
      BioGRIDi
      205067, 29 interactors

      Protein interaction database and analysis system

      More...
      IntActi
      Q9Z0X1, 28 interactors

      Molecular INTeraction database

      More...
      MINTi
      Q9Z0X1

      STRING: functional protein association networks

      More...
      STRINGi
      10090.ENSMUSP00000041104

      Miscellaneous databases

      RNAct, Protein-RNA interaction predictions for model organisms.

      More...
      RNActi
      Q9Z0X1, protein

      <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

      1612
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

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

      More...
      SMRi
      Q9Z0X1

      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
      Q9Z0X1

      <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

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni133 – 482FAD-dependent oxidoreductaseAdd BLAST350

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1 – 30Mitochondrial localization signal1 PublicationAdd BLAST30
      Motifi62 – 88Mitochondrial localization signal1 PublicationAdd BLAST27
      Motifi445 – 450Nuclear localization signalSequence analysis6

      <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

      Keywords - Domaini

      Transit peptide

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG1346, Eukaryota

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000156455

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      CLU_003291_5_3_1

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      Q9Z0X1

      KEGG Orthology (KO)

      More...
      KOi
      K04727

      Database of Orthologous Groups

      More...
      OrthoDBi
      830428at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      Q9Z0X1

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF314028

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      3.30.390.30, 1 hit
      3.50.50.60, 2 hits

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR029324, AIF_C
      IPR036188, FAD/NAD-bd_sf
      IPR023753, FAD/NAD-binding_dom
      IPR016156, FAD/NAD-linked_Rdtase_dimer_sf

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF14721, AIF_C, 1 hit
      PF07992, Pyr_redox_2, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF51905, SSF51905, 2 hits
      SSF55424, SSF55424, 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>Sequences (2+)i

      <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.

      This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

      Isoform 1 (identifier: Q9Z0X1-1) [UniParc]FASTAAdd to basket

      This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

      « Hide
              10         20         30         40         50
      MFRCGGLAGA FKQKLVPLVR TVYVQRPKQR NRLPGNLFQQ WRVPLELQMA
      60 70 80 90 100
      RQMASSGSSG GKMDNSVLVL IVGLSTIGAG AYAYKTIKED QKRYNERVMG
      110 120 130 140 150
      LGLSPEEKQR RAIASATEGG SVPQIRAPSH VPFLLIGGGT AAFAAARSIR
      160 170 180 190 200
      ARDPGARVLI VSEDPELPYM RPPLSKELWF SDDPNVTKTL QFRQWNGKER
      210 220 230 240 250
      SIYFQPPSFY VSAQDLPNIE NGGVAVLTGK KVVHLDVRGN MVKLNDGSQI
      260 270 280 290 300
      TFEKCLIATG GTPRSLSAID RAGAEVKSRT TLFRKIGDFR ALEKISREVK
      310 320 330 340 350
      SITVIGGGFL GSELACALGR KSQASGIEVI QLFPEKGNMG KILPQYLSNW
      360 370 380 390 400
      TMEKVKREGV KVMPNAIVQS VGVSGGRLLI KLKDGRKVET DHIVTAVGLE
      410 420 430 440 450
      PNVELAKTGG LEIDSDFGGF RVNAELQARS NIWVAGDAAC FYDIKLGRRR
      460 470 480 490 500
      VEHHDHAVVS GRLAGENMTG AAKPYWHQSM FWSDLGPDVG YEAIGLVDSS
      510 520 530 540 550
      LPTVGVFAKA TAQDNPKSAT EQSGTGIRSE SETESEASEI TIPPSAPAVP
      560 570 580 590 600
      QVPVEGEDYG KGVIFYLRDK VVVGIVLWNV FNRMPIARKI IKDGEQHEDL
      610
      NEVAKLFNIH ED
      Length:612
      Mass (Da):66,765
      Last modified:May 1, 1999 - 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:iA17EDFD5CF77BB85
      GO
      Isoform 2 (identifier: Q9Z0X1-2) [UniParc]FASTAAdd to basket
      Also known as: AIFsh21 Publication

      The sequence of this isoform differs from the canonical sequence as follows:
           322-324: SQA → CEY
           325-612: Missing.

      Show »
      Length:324
      Mass (Da):35,458
      Checksum:iA20E68B1BB01CA95
      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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      Gene namesLengthAnnotation
      B1AU25B1AU25_MOUSE
      Apoptosis-inducing factor 1, mitoch...
      Aifm1
      608Annotation 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>

      Alternative sequence

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_060486322 – 324SQA → CEY in isoform 2. 3
      Alternative sequenceiVSP_060487325 – 612Missing in isoform 2. Add BLAST288

      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
      AF100927 mRNA Translation: AAD16435.1
      DQ016499 mRNA Translation: AAY84740.1
      BC003292 mRNA Translation: AAH03292.1

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS30109.1 [Q9Z0X1-1]

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_001277293.1, NM_001290364.1
      NP_036149.1, NM_012019.3 [Q9Z0X1-1]

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENSMUST00000037349; ENSMUSP00000041104; ENSMUSG00000036932 [Q9Z0X1-1]

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      26926

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      mmu:26926

      UCSC genome browser

      More...
      UCSCi
      uc009tcg.1, mouse [Q9Z0X1-1]

      Keywords - Coding sequence diversityi

      Alternative splicing

      <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
      AF100927 mRNA Translation: AAD16435.1
      DQ016499 mRNA Translation: AAY84740.1
      BC003292 mRNA Translation: AAH03292.1
      CCDSiCCDS30109.1 [Q9Z0X1-1]
      RefSeqiNP_001277293.1, NM_001290364.1
      NP_036149.1, NM_012019.3 [Q9Z0X1-1]

      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
      1GV4X-ray2.00A/B122-610[»]
      3GD3X-ray2.95A/B/C/D78-612[»]
      3GD4X-ray2.24A/B102-612[»]
      5MIUX-ray3.50A/B78-612[»]
      5MIVX-ray3.10A/C78-612[»]
      SMRiQ9Z0X1
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein-protein interaction databases

      BioGRIDi205067, 29 interactors
      IntActiQ9Z0X1, 28 interactors
      MINTiQ9Z0X1
      STRINGi10090.ENSMUSP00000041104

      PTM databases

      iPTMnetiQ9Z0X1
      PhosphoSitePlusiQ9Z0X1
      SwissPalmiQ9Z0X1

      Proteomic databases

      EPDiQ9Z0X1
      jPOSTiQ9Z0X1
      MaxQBiQ9Z0X1
      PaxDbiQ9Z0X1
      PeptideAtlasiQ9Z0X1
      PRIDEiQ9Z0X1

      Protocols and materials databases

      Antibodypedia a portal for validated antibodies

      More...
      Antibodypediai
      3528, 828 antibodies

      Genome annotation databases

      EnsembliENSMUST00000037349; ENSMUSP00000041104; ENSMUSG00000036932 [Q9Z0X1-1]
      GeneIDi26926
      KEGGimmu:26926
      UCSCiuc009tcg.1, mouse [Q9Z0X1-1]

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      9131
      MGIiMGI:1349419, Aifm1

      Phylogenomic databases

      eggNOGiKOG1346, Eukaryota
      GeneTreeiENSGT00940000156455
      HOGENOMiCLU_003291_5_3_1
      InParanoidiQ9Z0X1
      KOiK04727
      OrthoDBi830428at2759
      PhylomeDBiQ9Z0X1
      TreeFamiTF314028

      Enzyme and pathway databases

      SABIO-RKiQ9Z0X1

      Miscellaneous databases

      BioGRID ORCS database of CRISPR phenotype screens

      More...
      BioGRID-ORCSi
      26926, 4 hits in 18 CRISPR screens

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

      More...
      ChiTaRSi
      Aifm1, mouse
      EvolutionaryTraceiQ9Z0X1

      Protein Ontology

      More...
      PROi
      PR:Q9Z0X1
      RNActiQ9Z0X1, protein

      The Stanford Online Universal Resource for Clones and ESTs

      More...
      SOURCEi
      Search...

      Gene expression databases

      BgeeiENSMUSG00000036932, Expressed in cortex of kidney and 301 other tissues
      ExpressionAtlasiQ9Z0X1, baseline and differential
      GenevisibleiQ9Z0X1, MM

      Family and domain databases

      Gene3Di3.30.390.30, 1 hit
      3.50.50.60, 2 hits
      InterProiView protein in InterPro
      IPR029324, AIF_C
      IPR036188, FAD/NAD-bd_sf
      IPR023753, FAD/NAD-binding_dom
      IPR016156, FAD/NAD-linked_Rdtase_dimer_sf
      PfamiView protein in Pfam
      PF14721, AIF_C, 1 hit
      PF07992, Pyr_redox_2, 1 hit
      SUPFAMiSSF51905, SSF51905, 2 hits
      SSF55424, SSF55424, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      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 nameiAIFM1_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: Q9Z0X1
      Secondary accession number(s): Q1L6K5
      <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: April 27, 2001
      Last sequence update: May 1, 1999
      Last modified: October 7, 2020
      This is version 182 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. MGD cross-references
        Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families
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