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Q9JM53

- AIFM1_RAT

UniProt

Q9JM53 - AIFM1_RAT

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Protein

Apoptosis-inducing factor 1, mitochondrial

Gene

Aifm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Functions both as NADH oxidoreductase and as regulator of apoptosis. 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. In contrast, functions as an antiapoptotic factor in normal mitochondria via its NADH oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby inhibits the EIF3 machinery and protein synthesis,and activates casapse-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. Binds to DNA in a sequence-independent manner By similarity.By similarity

Cofactori

FAD.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711FADBy similarity
Binding sitei176 – 1761FADBy similarity
Binding sitei232 – 2321FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei284 – 2841FADBy similarity
Binding sitei437 – 4371FADBy similarity
Binding sitei482 – 4821FAD; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 1415FADBy similarity
Nucleotide bindingi163 – 1642FADBy similarity
Nucleotide bindingi453 – 4542FADBy similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. FAD binding Source: Ensembl
  3. NAD(P)H oxidase activity Source: Ensembl

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. cell redox homeostasis Source: InterPro
  3. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  4. mitochondrial respiratory chain complex I assembly Source: Ensembl
  5. neuron apoptotic process Source: Ensembl
  6. neuron differentiation Source: Ensembl
  7. positive regulation of cell death Source: Ensembl
  8. regulation of apoptotic DNA fragmentation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

DNA-binding, FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis-inducing factor 1, mitochondrial (EC:1.1.1.-)
Alternative name(s):
Programmed cell death protein 8
Gene namesi
Name:Aifm1
Synonyms:Aif, Pdcd8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome X

Organism-specific databases

RGDi620817. Aifm1.

Subcellular locationi

Mitochondrion intermembrane space. Mitochondrion inner membrane By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity
Note: Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a 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. Colocalizes with EIF3G in the nucleus and perinuclear region By similarity.By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrial inner membrane Source: UniProtKB-KW
  3. mitochondrial intermembrane space Source: UniProtKB
  4. mitochondrion Source: RGD
  5. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454MitochondrionBy similarityAdd
BLAST
Propeptidei55 – 10147Removed in mature formBy similarityPRO_0000401937Add
BLAST
Chaini102 – 612511Apoptosis-inducing factor 1, mitochondrialPRO_0000022032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081N6-succinyllysineBy similarity
Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei267 – 2671PhosphoserineBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei592 – 5921N6-acetyllysineBy similarity

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.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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JM53.
PRIDEiQ9JM53.

PTM databases

PhosphoSiteiQ9JM53.

Expressioni

Gene expression databases

GenevestigatoriQ9JM53.

Interactioni

Subunit structurei

Monomer (oxidized form). Homodimer (reduced form). Interacts with XIAP/BIRC4. Interacts (via N-terminus) with EIF3G (via C-terminus). Interacts with PRELID1 By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9JM53.
SMRiQ9JM53. Positions 121-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 482350FAD-dependent oxidoreductaseBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi445 – 4506Nuclear localization signalSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0446.
GeneTreeiENSGT00530000063416.
HOGENOMiHOG000264253.
HOVERGENiHBG053538.
InParanoidiQ9JM53.
KOiK04727.
OMAiKDGEEHA.
OrthoDBiEOG7C2R0V.
PhylomeDBiQ9JM53.
TreeFamiTF314028.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR029324. AIF_C.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF14721. AIF_C. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JM53-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFRCGGLAGA FKQKLVPLVR SVCVQRPKQR NRLPGNLFQQ WRVPLELQMA
60 70 80 90 100
RQMASSGPSG GKMDNSVLVL IVGLSTIGAG AYAYKTIKED QKRYNERIMG
110 120 130 140 150
LGLSPEEKQR RAIASAAEGG SVPPIRVPSH VPFLLIGGGT AAFAAARSIR
160 170 180 190 200
ARDPGARVLI VSEDPELPYM RPPLSKELWF SDDPNVTKTL QFRQWNGKER
210 220 230 240 250
SIYFQPPSFY VSAQDLPHIE NGGVAVLTGK KVVHLDVRGN MVKLNDGSQI
260 270 280 290 300
TFEKCLIATG GTPRSLSAID RAGAEVKSRT TLFRKIGDFR ALEKISREVK
310 320 330 340 350
SITVIGGGFL GSELACALGR KSQASGIEVI QLFPEKGNMG KILPEYLSNW
360 370 380 390 400
TMEKVKREGV KVMPNAIVQS VGVSGGKLLI 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 TIPPSDPAVP
560 570 580 590 600
QVPVEGEDYG KGVIFYLRDK VVVGIVLWNV FNRMPIARKI IKDGEQHEDL
610
NEVAKLFNIH ED
Length:612
Mass (Da):66,723
Last modified:October 1, 2000 - v1
Checksum:i02ECF24FA7400A86
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB041723 mRNA. Translation: BAA94745.1.
AF375656 mRNA. Translation: AAM46094.1.
BC072697 mRNA. Translation: AAH72697.1.
RefSeqiNP_112646.1. NM_031356.1.
UniGeneiRn.203165.

Genome annotation databases

EnsembliENSRNOT00000008503; ENSRNOP00000008503; ENSRNOG00000006067.
GeneIDi83533.
KEGGirno:83533.
UCSCiRGD:620817. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB041723 mRNA. Translation: BAA94745.1 .
AF375656 mRNA. Translation: AAM46094.1 .
BC072697 mRNA. Translation: AAH72697.1 .
RefSeqi NP_112646.1. NM_031356.1.
UniGenei Rn.203165.

3D structure databases

ProteinModelPortali Q9JM53.
SMRi Q9JM53. Positions 121-610.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9JM53.

Proteomic databases

PaxDbi Q9JM53.
PRIDEi Q9JM53.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000008503 ; ENSRNOP00000008503 ; ENSRNOG00000006067 .
GeneIDi 83533.
KEGGi rno:83533.
UCSCi RGD:620817. rat.

Organism-specific databases

CTDi 9131.
RGDi 620817. Aifm1.

Phylogenomic databases

eggNOGi COG0446.
GeneTreei ENSGT00530000063416.
HOGENOMi HOG000264253.
HOVERGENi HBG053538.
InParanoidi Q9JM53.
KOi K04727.
OMAi KDGEEHA.
OrthoDBi EOG7C2R0V.
PhylomeDBi Q9JM53.
TreeFami TF314028.

Miscellaneous databases

NextBioi 616033.
PROi Q9JM53.

Gene expression databases

Genevestigatori Q9JM53.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR029324. AIF_C.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF14721. AIF_C. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of rat apoptosis-inducing factor (AIF)."
    Ohsakaya S., Mihara K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Cloning and characterization of rat apoptosis-inducing factor: implications for DNA fragmentation in cerebral ischemia."
    Cao G., Sheng L., Pei W., Chen J.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Cerebellum.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  4. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 378-386, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiAIFM1_RAT
AccessioniPrimary (citable) accession number: Q9JM53
Secondary accession number(s): Q548E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3