AIFM1_DICDI
ID AIFM1_DICDI Reviewed; 532 AA.
AC Q9GRX6; Q54J72;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Apoptosis-inducing factor 1, mitochondrial;
DE EC=1.6.99.- {ECO:0000250|UniProtKB:O95831};
DE AltName: Full=Ddaif;
DE Flags: Precursor;
GN Name=aif; ORFNames=DDB_G0288247;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11598188; DOI=10.1091/mbc.12.10.3016;
RA Arnoult D., Tatischeff I., Estaquier J., Girard M., Sureau F.,
RA Tissier J.-P., Grodet A., Dellinger M., Traincard F., Kahn A.,
RA Ameisen J.-C., Petit P.X.;
RT "On the evolutionary conservation of the cell death pathway: mitochondrial
RT release of an apoptosis-inducing factor during Dictyostelium discoideum
RT cell death.";
RL Mol. Biol. Cell 12:3016-3030(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable NADH oxidoreductase that acts as a caspase-
CC independent mitochondrial effector of apoptotic cell death.
CC {ECO:0000269|PubMed:11598188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:O95831};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11598188}.
CC Cytoplasm {ECO:0000269|PubMed:11598188}. Nucleus
CC {ECO:0000269|PubMed:11598188}. Note=Translocates from mitochondria to
CC the cytoplasm and secondary to the nucleus after the onset of cell
CC death.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AJ272500; CAC14872.1; -; mRNA.
DR EMBL; AAFI02000109; EAL63305.1; -; Genomic_DNA.
DR RefSeq; XP_636815.1; XM_631723.1.
DR AlphaFoldDB; Q9GRX6; -.
DR SMR; Q9GRX6; -.
DR STRING; 44689.DDB0191137; -.
DR PaxDb; Q9GRX6; -.
DR EnsemblProtists; EAL63305; EAL63305; DDB_G0288247.
DR GeneID; 8626532; -.
DR KEGG; ddi:DDB_G0288247; -.
DR dictyBase; DDB_G0288247; aif.
DR eggNOG; KOG1346; Eukaryota.
DR HOGENOM; CLU_003291_5_3_1; -.
DR InParanoid; Q9GRX6; -.
DR OMA; EVRYERC; -.
DR PhylomeDB; Q9GRX6; -.
DR PRO; PR:Q9GRX6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISS:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:RHEA.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IDA:dictyBase.
DR GO; GO:0006308; P:DNA catabolic process; IDA:dictyBase.
DR GO; GO:0000266; P:mitochondrial fission; IMP:dictyBase.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:dictyBase.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IDA:dictyBase.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IMP:dictyBase.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:dictyBase.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR029324; AIF_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR Pfam; PF14721; AIF_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; FAD; Flavoprotein; Mitochondrion; NAD; Nucleus;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..532
FT /note="Apoptosis-inducing factor 1, mitochondrial"
FT /id="PRO_0000378099"
FT REGION 63..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..440
FT /note="FAD-dependent oxidoreductase"
FT /evidence="ECO:0000250"
FT MOTIF 400..406
FT /note="Nuclear localization signal"
FT BINDING 102..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 128..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 260..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 408..409
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 409..410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 440
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 440
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95831"
FT BINDING 450
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95831"
SQ SEQUENCE 532 AA; 59667 MW; 7FBED7F2C2DA2909 CRC64;
MIRNLTKLTK FTIGNRFYQS SSKGRFSGKN GNNAFKSIVG VSVGVSALFA GCVFLDQEKE
PESTPSIDVK EKKSQPPKTK EDYQKKMDEE YDIEQFKYVI IGGGTAAYHA IDKILENDKE
ATILLISKEY EVPYQRPPLT KSLWATKDDN VVNTLNFSDW SGKKQNLLYE QESAYGNEIL
QFIRTKKVID LHIDEKLVLL NDGKLIRYDK CLIATGGEPR QLKFTSTNDK KISTYRTVED
FRKLYEVVKD GGKHVTVLGG GFLGSELTCA INSNFQDKNI KIDQIFPESG VLSTLFPDYL
SKYATEEIIK SGVNVHTGTL IKDVVDNSEN GRLTVTLNNG KTFETDHVVV AAGIIPNTNV
VKSTTLEIDP INGGYVVNPE LQARTDLYVA GDVASYYDFS LGVRRRVEHH DHARATGEMA
GSNMSTKDTP APYTYQPFFW SDLTPGVGFE AVGNTSSKLK TFSVWEKPSS DETKQSYTKG
NIYYLNDNNN VVGVLCYGNY GKMDTARDLI LKRRTIEDLN QLQHAIDFDE HH
