| Tag |
Content |
LipidDB ID |
LipidDB-9606-00207 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
9.16 |
Molecular Weight |
40526.7 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Apoptosis-inducing factor 2 |
Protein Synonyms/Alias |
1.-.-.-; Apoptosis-inducing factor homologous mitochondrion-associated inducer of death; Apoptosis-inducing factor-like mitochondrion-associated inducer of death; p53-responsive gene 3 protein; |
Gene Name |
AIFM2 |
Gene Synonyms/Alias |
AMID; PRG3; |
Created Date |
30-MAY-2006 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGSQVSVES | [1] | N-Myristoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[ PMID:20213681]
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Functional Description |
Oxidoreductase, which may play a role in mediating a p53/TP53-dependent apoptosis response. Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death. Binds to DNA in a sequence-independent manner. May contribute to genotoxin-induced growth arrest. |
Sequence Annotation |
Transmembrane: 7 27 Helical.
Nucleotide-binding: 18 22 6-hydroxy-FAD.
Binding site: 54 54 6-hydroxy-FAD.
Binding site: 82 82 6-hydroxy-FAD; via amide nitrogen andcarbonyl oxygen.
Binding site: 285 285 6-hydroxy-FAD.
|
Protein Length |
373 AA. |
Protein Sequence
(Canonical) |
MGSQVSVESG ALHVVIVGGG FGGIAAASQL QALNVPFMLV DMKDSFHHNV AALRASVETG 60
FAKKTFISYS VTFKDNFRQG LVVGIDLKNQ MVLLQGGEAL PFSHLILATG STGPFPGKFN 120
EVSSQQAAIQ AYEDMVRQVQ RSRFIVVVGG GSAGVEMAAE IKTEYPEKEV TLIHSQVALA 180
DKELLPSVRQ EVKEILLRKG VQLLLSERVS NLEELPLNEY REYIKVQTDK GTEVATNLVI 240
LCTGIKINSS AYRKAFESRL ASSGALRVNE HLQVEGHSNV YAIGDCADVR TPKMAYLAGL 300
HANIAVANIV NSVKQRPLQA YKPGALTFLL SMGRNDGVGQ ISGFYVGRLM VRLTKSRDLF 360
VSTSWKTMRQ SPP 373
|
FASTA
(Canonical) |
>LipidDB-9606-00207|Q9BRQ8
MGSQVSVESGALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETG
FAKKTFISYSVTFKDNFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGKFN
EVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYPEKEVTLIHSQVALA
DKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVI
LCTGIKINSSAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGL
HANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLTKSRDLF
VSTSWKTMRQSPP
|
Gene Ontology |
GO:0005737; C:cytoplasm; IDA:MGI GO:0005829; C:cytosol; IDA:UniProtKB GO:0005615; C:extracellular space; IDA:UniProt GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0005811; C:lipid particle; IDA:UniProtKB GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB GO:0005739; C:mitochondrion; IDA:MGI GO:0003677; F:DNA binding; IDA:UniProtKB GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IDA:UniProtKB GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:RefGenome GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB |
Interpro |
InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2 |
Pfam |
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SMART |
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PROSITE |
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PRINTS |
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