AIFM1_DROME
ID AIFM1_DROME Reviewed; 739 AA.
AC Q9VQ79; B5RIR8; Q95TL9; Q960F8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Putative apoptosis-inducing factor 1, mitochondrial;
DE Short=DmAIF;
DE EC=1.6.99.- {ECO:0000250|UniProtKB:O95831};
DE Flags: Precursor;
GN Name=AIF; ORFNames=CG7263;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=18309327; DOI=10.1038/cdd.2008.24;
RA Joza N., Galindo K., Pospisilik J.A., Benit P., Rangachari M., Kanitz E.E.,
RA Nakashima Y., Neely G.G., Rustin P., Abrams J.M., Kroemer G.,
RA Penninger J.M.;
RT "The molecular archaeology of a mitochondrial death effector: AIF in
RT Drosophila.";
RL Cell Death Differ. 15:1009-1018(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable NADH oxidoreductase (By similarity). Mitochondrial
CC effector of cell death that plays roles in developmentally regulated
CC cell death and normal mitochondrial function. {ECO:0000250,
CC ECO:0000269|PubMed:18309327}.
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; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:18309327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9VQ79-2; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9VQ79-1; Sequence=VSP_007951;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development with slightly lower levels during pupation.
CC {ECO:0000269|PubMed:18309327}.
CC -!- DISRUPTION PHENOTYPE: Loss of zygotic expression results in decreased
CC embryonic cell death and the persistence of differentiated neuronal
CC cells along the ventral nerve cord at late embryonic stages. Embryos
CC that do hatch undergo growth arrest at early larval stages, accompanied
CC by mitochondrial respiratory dysfunction.
CC {ECO:0000269|PubMed:18309327}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF51299.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10444.2; -; Genomic_DNA.
DR EMBL; AY052083; AAK93507.1; -; mRNA.
DR EMBL; AY058696; AAL13925.1; ALT_INIT; mRNA.
DR EMBL; BT044192; ACH92257.1; -; mRNA.
DR RefSeq; NP_608649.2; NM_134805.4. [Q9VQ79-1]
DR RefSeq; NP_722765.2; NM_164456.3. [Q9VQ79-2]
DR AlphaFoldDB; Q9VQ79; -.
DR SMR; Q9VQ79; -.
DR BioGRID; 59619; 19.
DR IntAct; Q9VQ79; 3.
DR STRING; 7227.FBpp0077504; -.
DR PaxDb; Q9VQ79; -.
DR DNASU; 33390; -.
DR EnsemblMetazoa; FBtr0077830; FBpp0077503; FBgn0031392. [Q9VQ79-1]
DR EnsemblMetazoa; FBtr0077831; FBpp0077504; FBgn0031392. [Q9VQ79-2]
DR GeneID; 33390; -.
DR KEGG; dme:Dmel_CG7263; -.
DR CTD; 33390; -.
DR FlyBase; FBgn0031392; AIF.
DR VEuPathDB; VectorBase:FBgn0031392; -.
DR eggNOG; KOG1346; Eukaryota.
DR GeneTree; ENSGT00940000156455; -.
DR InParanoid; Q9VQ79; -.
DR OMA; EVRYERC; -.
DR PhylomeDB; Q9VQ79; -.
DR BioGRID-ORCS; 33390; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 33390; -.
DR PRO; PR:Q9VQ79; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031392; Expressed in egg chamber and 24 other tissues.
DR ExpressionAtlas; Q9VQ79; baseline and differential.
DR Genevisible; Q9VQ79; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:FlyBase.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IBA:GO_Central.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:FlyBase.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; ISS:UniProtKB.
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; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; FAD; Flavoprotein; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..739
FT /note="Putative apoptosis-inducing factor 1, mitochondrial"
FT /id="PRO_0000022029"
FT REGION 257..564
FT /note="FAD-dependent oxidoreductase"
FT REGION 644..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261..265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 564
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 580..581
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VAR_SEQ 51..115
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:18309327, ECO:0000303|Ref.5"
FT /id="VSP_007951"
FT CONFLICT 639
FT /note="E -> D (in Ref. 4; AAK93507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81217 MW; 71184B1721AB93AF CRC64;
MSIWGVRCLT QRFIRQAYIL ANRRLLGPVP QRSPPAYAPL RPAHSSLYQM VKKRTLEART
KLQANKYPNH QVCVTKPSTT PPVEEYETAV EGAGVPAYAN AQFQAHSQSE PLFKVGFADV
KSVCSAKDVL KSDSAKLSTS QPVLDSCKAT SPCEEFKRKR KETTCQPCDE DGTAPGGGDG
GDEECECRMK DLRLKCLLGA LAALLAGGFL AWFMTRDTDD SEAKKAEAEE EERKRRLVAG
LATSPPSSED LPKHVPYLII GGGTAAFSAF RAIKSNDATA KVLMISNEFR KPYMRPPLSK
ELWYTPNPNE DPIKDYRFKQ WTGSERSLFF EPDEFFIDPE DLDDNANGGI AVAQGFSVKK
VDAQKRIVTL NDGYEISYDE CLIATGCAPK NLPMLRDAPP SVLEKVMVYR TPDDFDRLRK
LAAEKRSITI VGNGFIGSEL ACSLAHYSRE NNGGKVYQVF QENANMSKVL PNYLSRWTTA
KMEAQGVCVI PNASIRSAVR DETNLKLELN NGMTLMSDVV VVCVGCTPNT DLAGPSRLEV
DRSLGGFVVN AELEARRNLY VAGDASCFFD PLLGRRRVEH HDHSVVSGRL AGENMTGAKK
PYQHQSMFWS DLGPEIGYEG IGLVDSSLPT VGVFALPSES ATRVDQLSES SDSDVPETST
SSSQSSKSDA GASQDGVTCD PDEAGNYGKG VIFYLKNDKI VGILLWNLFN RIGLARTIIN
QNKKYDDLNE VAKLFEIHA
